P. J. Gerber, A. Mottet, C. I. Opio, A. Falcucci, and F. Teillard, Environmental impacts of beef production: Review of challenges and perspectives for durability, Meat Sci, vol.109, pp.2-12, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02637607

T. G. O'quinn, J. F. Legako, J. C. Brooks, and M. F. Miller, Evaluation of the contribution of tenderness, juiciness, and flavor to the overall consumer beef eating experience1, Transl. Anim. Sci, vol.2, pp.26-36, 2018.

M. Gagaoua, C. Terlouw, D. Micol, A. Boudjellal, J. Hocquette et al., Proteomic Biomarkers of Meat Colour of Blonde D'Aquitaine Young Bulls: Towards a Better Comprehension of the Biological Mechanisms, 61th Int, Proceedings of the 61st International Congress of Meat Science and Meat Technology, p.31, 2015.

C. Mccormick, Applied Muscle Biology and Meat Science

M. Du, R. J. Mccormick, and . Eds, , pp.128-148, 2009.

E. Dransfield, J. Martin, D. Bauchart, S. Abouelkaram, J. Lepetit et al., Meat quality and composition of three muscles from French cull cows and young bulls, Anim. Sci, vol.76, pp.387-399, 2003.
URL : https://hal.archives-ouvertes.fr/hal-02683095

, Int. J. Mol. Sci, vol.2020, p.664

K. D. Sinclair, G. E. Lobley, G. W. Horgan, D. J. Kyle, A. D. Porter et al., Factors influencing beef eating quality 1. Effects of nutritional regimen and genotype on organoleptic properties and instrumental texture, Anim. Sci, vol.72, pp.269-277, 2001.

S. Hansen, M. Therkildsen, and D. V. Byrne, Effects of a compensatory growth strategy on sensory and physical properties of meat from young bulls, Meat Sci, vol.74, pp.628-643, 2006.

J. Soulat, B. Picard, S. Léger, and V. Monteils, Prediction of beef carcass and meat quality traits from factors characterising the rearing management system applied during the whole life of heifers, Meat Sci, vol.140, pp.88-100, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02623831

M. Gagaoua, B. Picard, J. Soulat, and V. Monteils, Clustering of sensory eating qualities of beef: Consistencies and differences within carcass, muscle, animal characteristics and rearing factors, Livest. Sci, vol.214, pp.245-258, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01824994

C. Terlouw, . Stress, and . Reactivity, Stress at Slaughter and Meat Quality. In Meat Quality: Genetic and Environmental Factors, p.22, 2015.

A. Ouali, Sensory quality of meat as affected by muscle biochemistry and modern technologies, In Animal Biotechnology and the Quality of Meat Production, pp.85-105, 1991.
URL : https://hal.archives-ouvertes.fr/hal-02778894

S. D. Shackelford, T. L. Wheeler, and M. Koohmaraie, Tenderness classification of beef: I. Evaluation of beef longissimus shear force at 1 or 2 days postmortem as a predictor of aged beef tenderness, J. Anim. Sci, vol.75, pp.2417-2422, 1997.

R. K. Miller, The Eating Quality of Meat: V-Sensory Evaluation of Meat, Lawrie´s Meat Science, pp.461-499, 2017.

, Sensory and Tenderness Evaluation Guidelines, p.15, 2020.

J. Hocquette, S. Lehnert, W. Barendse, I. Cassar-malek, and B. Picard, Recent advances in cattle functional genomics and their application to beef quality, Animal, vol.1, pp.159-173, 2007.
URL : https://hal.archives-ouvertes.fr/hal-02756208

M. Taye, J. Kim, S. H. Yoon, W. Lee, O. Hanotte et al., Whole genome scan reveals the genetic signature of African Ankole cattle breed and potential for higher quality beef, BMC Genet, vol.18, 2017.

C. Bernard, I. Cassar-malek, M. Le-cunff, H. Dubroeucq, G. Renand et al., New indicators of beef sensory quality revealed by expression of specific genes, J. Agric. Food Chem, vol.55, pp.5229-5237, 2007.
URL : https://hal.archives-ouvertes.fr/hal-02667197

J. Hocquette, C. Bernard-capel, V. Vidal, B. Jesson, H. Levéziel et al., The GENOTEND chip: A new tool to analyse gene expression in muscles of beef cattle for beef quality prediction, BMC Vet. Res, vol.8, p.135, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01211927

R. Lametsch, A. Karlsson, K. Rosenvold, H. J. Andersen, P. Roepstorff et al., Postmortem Proteome Changes of Porcine Muscle Related to Tenderness, J. Agric. Food Chem, vol.51, pp.6992-6997, 2003.

W. Przybylski and D. Hopkins, Meat Quality: Genetic and Environmental Factors, 2015.

B. Picard and M. Gagaoua, Proteomic Investigations of Beef Tenderness, Proteom. Food Sci, vol.2017, pp.177-197
URL : https://hal.archives-ouvertes.fr/hal-01580641

M. Gagaoua, E. M. Terlouw, D. Micol, J. Hocquette, A. P. Moloney et al., Sensory quality of meat from eight different types of cattle in relation with their biochemical characteristics, J. Integr. Agric, vol.15, pp.1550-1563, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02638038

B. Picard, M. Gagaoua, D. Micol, I. Cassar-malek, J. Hocquette et al., Inverse Relationships between Biomarkers and Beef Tenderness According to Contractile and Metabolic Properties of the Muscle, J. Agric. Food Chem, vol.62, pp.9808-9818, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02636820

I. Cassar-malek and B. Picard, Expression Marker-Based Strategy to Improve Beef Quality, Sci. World J, pp.1-11, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02629648

X. Jia, E. Veiseth-kent, H. Grove, P. Kuziora, L. Aass et al., Peroxiredoxin-6 A potential protein marker for meat tenderness in bovine longissimus thoracis muscle, J. Anim. Sci, vol.87, pp.2391-2399, 2009.

, Int. J. Mol. Sci, vol.2020, pp.664-693

G. Kim, H. Yang, and J. Jeong, Comparison of Characteristics of Myosin Heavy Chain-based Fiber and Meat Quality among Four Bovine Skeletal Muscles, Korean J. Food Sci. Anim. Resour, vol.36, pp.819-828, 2016.

A. Lana, V. Longo, A. Dalmasso, A. D'alessandro, M. T. Bottero et al., Omics integrating physical techniques: Aged Piedmontese meat analysis, Food Chem, vol.172, pp.731-741, 2015.

E. Laville, T. Sayd, M. Morzel, S. Blinet, C. Chambon et al., Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization, J. Agric. Food Chem, vol.57, pp.10755-10764, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02663751

B. Picard, N. Guillemin, M. Bonnet, S. G. Champanelle, I. Cassar-malek et al., 32-Quest for Novel Muscle Pathway Biomarkers by Proteomics in Beef Production, Compr. Biotechnol, vol.1, pp.395-405, 2011.

K. J. Thornton, K. C. Chapalamadugu, E. M. Eldredge, and G. K. Murdoch, Analysis of Longissimus thoracis Protein Expression Associated with Variation in Carcass Quality Grade and Marbling of Beef Cattle Raised in the Pacific Northwestern United States, J. Agric. Food Chem, vol.65, pp.1434-1442, 2017.

B. C. Bowker, J. S. Eastridge, and M. B. Solomon, Measurement of Muscle Exudate Protein Composition as an Indicator of Beef Tenderness, J. Food Sci, vol.79, pp.1292-1297, 2014.

C. Zhao, L. Zan, Y. Wang, M. S. Updike, G. Liu et al., Functional proteomic and interactome analysis of proteins associated with beef tenderness in Angus cattle, Livest. Sci, vol.161, pp.201-209, 2014.

A. D'alessandro, S. Rinalducci, C. Marrocco, V. Zolla, F. Napolitano et al., Love me tender: An Omics window on the bovine meat tenderness network, J. Proteom, vol.75, pp.4360-4380, 2012.

M. Morzel, C. Terlouw, C. Chambon, D. Micol, and B. Picard, Muscle proteome and meat eating qualities of Longissimus thoracis of "Blonde d'Aquitaine" young bulls: A central role of HSP27 isoforms, Meat Sci, vol.78, pp.297-304, 2008.
URL : https://hal.archives-ouvertes.fr/hal-02666814

N. K. Kim, S. Cho, S. H. Lee, H. R. Park, C. S. Lee et al., Proteins in longissimus muscle of Korean native cattle and their relationship to meat quality, Meat Sci, vol.80, pp.1068-1073, 2008.

J. Bouley, C. Chambon, and B. Picard, Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry, Proteomics, vol.4, pp.1811-1824, 2004.
URL : https://hal.archives-ouvertes.fr/hal-02681208

S. G. Bjarnadottir, K. Hollung, M. Høy, E. Bendixen, M. C. Codrea et al., Changes in protein abundance between tender and tough meat from bovine Longissimus thoracis muscle assessed by isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis analysis, J. Anim. Sci, vol.90, pp.2035-2043, 2012.

M. E. Carvalho, G. Gasparin, M. D. Poleti, A. F. Rosa, J. C. Balieiro et al., Heat shock and structural proteins associated with meat tenderness in Nellore beef cattle, a Bos indicus breed, Meat Sci, vol.96, pp.1318-1324, 2014.

T. Chaze, J. Hocquette, B. Meunier, G. Renand, C. Jurie et al., Biological Markers for Meat Tenderness of the Three Main French Beef Breeds Using 2-DE and MS Approach, Proteomics in Foods, pp.127-146, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01193863

N. P. Guillemin, C. Jurie, G. Renand, J. Hocquette, D. Micol et al., Different phenotypic and proteomic markers explain variability of beef tenderness across muscles, Int. J. Biol, vol.4, pp.26-38, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01000621

N. Guillemin, B. Meunier, C. Jurie, I. Cassar-malek, J. Hocquette et al., Validation of a Dot-Blot quantitative technique for large scale analysis of beef tenderness biomarkers, J. Physiol. Pharmacol, vol.60, p.23, 2009.
URL : https://hal.archives-ouvertes.fr/hal-01211921

W. A. Baldassini, C. P. Braga, L. A. Chardulo, J. A. Silva, J. M. Malheiros et al., Bioanalytical methods for the metalloproteomics study of bovine longissimus thoracis muscle tissue with different grades of meat tenderness in the Nellore breed (Bos indicus), Food Chem, vol.169, pp.65-72, 2015.

, Int. J. Mol. Sci, vol.2020, p.664

Y. Boudida, M. Gagaoua, S. Becila, B. Picard, A. Boudjellal et al., Serine Protease Inhibitors as Good Predictors of Meat Tenderness: Which Are They and What Are Their Functions?, Crit. Rev. Food Sci. Nutr, vol.56, pp.957-972, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02635546

A. Y. Chulayo, G. Bradley, and V. Muchenje, Effects of transport distance, lairage time and stunning efficiency on cortisol, glucose, HSPA1A and how they relate with meat quality in cattle, Meat Sci, vol.117, pp.89-96, 2016.

D. Franco, A. Mato, F. J. Salgado, M. López-pedrouso, M. Carrera et al., Tackling proteome changes in the longissimus thoracis bovine muscle in response to pre-slaughter stress, J. Proteom, vol.122, pp.73-85, 2015.

V. Grabe?, M. Kathri, V. Phung, K. M. Moe, E. Slinde et al., Protein expression and oxygen consumption rate of early postmortem mitochondria relate to meat tenderness, J. Anim. Sci, vol.93, pp.1967-1979, 2015.

N. Guillemin, C. Jurie, I. Cassar-malek, J. F. Hocquette, G. Renand et al., Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type, Animal, vol.5, pp.885-894, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01000706

L. F. Fonseca, D. F. Gimenez, D. B. Silva, R. Barthelson, F. Baldi et al., Differences in global gene expression in muscle tissue of Nellore cattle with divergent meat tenderness, vol.18, p.945, 2017.

H. J. Kee, E. W. Park, and C. K. Lee, Characterization of beef transcripts correlated with tenderness and moisture, Mol. Cells, vol.25, pp.428-437, 2008.

S. Bongiorni, C. E. Gruber, S. Bueno, G. Chillemi, F. Ferre et al., Transcriptomic investigation of meat tenderness in two Italian cattle breeds, Anim. Genet, vol.47, pp.273-287, 2016.

X. H. Zhang, Y. X. Qi, X. Gao, J. Y. Li, and S. Z. Xu, Expression of ADAMTS4 and ADAMTS5 in longissimus dorsi muscle related to meat tenderness in Nanyang cattle, Genet. Mol. Res, vol.12, pp.4639-4647, 2013.

C. Zhao, F. Tian, Y. Yu, J. Luo, Q. Hu et al., Muscle transcriptomic analyses in Angus cattle with divergent tenderness, Mol. Biol. Rep, vol.39, pp.4185-4193, 2012.

J. M. Malheiros, C. E. Enríquez-valencia, B. O. Da-silva-duran, T. G. De-paula, R. A. Curi et al., Association of CAST2, HSP90AA1, DNAJA1 and HSPB1 genes with meat tenderness in Nellore cattle, Meat Sci, vol.138, pp.49-52, 2018.

A. Gurgul, T. Szmato?a, K. Ropka-molik, I. Jasielczuk, K. Pawlina et al., Identification of genome-wide selection signatures in the Limousin beef cattle breed, J. Anim. Breed. Genet, vol.133, pp.264-276, 2016.

G. Hou, Z. Yuan, X. Gao, J. Li, H. Gao et al., Genetic Polymorphisms of the CACNA2D1 Gene and Their Association with Carcass and Meat Quality Traits in Cattle, Biochem. Genet, vol.48, pp.751-759, 2010.

L. F. Pinto, J. B. Ferraz, V. B. Pedrosa, J. P. Eler, F. V. Meirelles et al., Single nucleotide polymorphisms in CAPN and leptin genes associated with meat color and tenderness in Nellore cattle, Genet. Mol. Res, vol.10, pp.2057-2064, 2011.

Y. Ramayo-caldas, G. Renand, M. Ballester, R. Saintilan, and D. Rocha, Multi-breed and multi-trait co-association analysis of meat tenderness and other meat quality traits in three French beef cattle breeds, Genet. Sel. Evol, vol.48, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01341371

Y. Y. Fan, L. S. Zan, C. Z. Fu, W. Q. Tian, H. B. Wang et al., Three novel SNPs in the coding region of PPAR? gene and their associations with meat quality traits in cattle, Mol. Biol. Rep, vol.38, pp.131-137, 2011.

S. Allais, L. Journaux, H. Levéziel, N. Payet-duprat, P. Raynaud et al., Effects of polymorphisms in the calpastatin and µ-calpain genes on meat tenderness in 3 French beef breeds, J. Anim. Sci, vol.89, pp.1-11, 2011.

, Int. J. Mol. Sci, vol.2020, p.664

C. Avilés, F. Peña, O. Polvillo, M. Barahona, M. M. Campo et al., Association between functional candidate genes and organoleptic meat traits in intensively-fed beef, Meat Sci, vol.107, pp.33-38, 2015.

L. Gui, H. Wang, S. Wei, Y. Zhang, and L. Zan, Molecular characterization, expression profiles, and analysis of Qinchuan cattle SIRT1 gene association with meat quality and body measurement traits (Bos taurus), Mol. Biol. Rep, vol.41, pp.5237-5246, 2014.

C. E. Rexroad-iii, G. L. Bennett, R. T. Stone, J. W. Keele, S. C. Fahrenkrug et al., Comparative mapping of BTA15 and HSA11 including a region containing a QTL for meat tenderness, Mamm. Genome, vol.12, pp.561-565, 2001.

P. C. Tizioto, J. E. Decker, J. F. Taylor, R. D. Schnabel, M. A. Mudadu et al., Genome scan for meat quality traits in Nelore beef cattle, Physiol. Genom, vol.45, pp.1012-1020, 2013.

S. Boudon and I. Cassar-malek, Dataset of Proteins Related to Beef Tenderness. Portail Data INRAE, V1, p.16, 2019.

M. Stastna and J. E. Van-eyk, Secreted proteins as a fundamental source for biomarker discovery, Proteomics, vol.12, pp.722-735, 2012.

N. Rifai, M. A. Gillette, and S. A. Carr, Protein biomarker discovery and validation: The long and uncertain path to clinical utility, Nat. Biotechnol, vol.24, pp.971-983, 2006.

M. Bonnet, J. Tournayre, and I. Cassar-malek, Integrated data mining of transcriptomic and proteomic datasets to predict the secretome of adipose tissue and muscle in ruminants, Mol. Biosyst, vol.12, pp.2722-2734, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02638660

B. Picard and M. Gagaoua, Meta-proteomics for the discovery of protein biomarkers of beef tenderness: An overview of integrated studies, Food Res. Int, vol.127, 2020.
URL : https://hal.archives-ouvertes.fr/hal-02627755

D. Caccia, M. Dugo, M. Callari, and I. Bongarzone, Bioinformatics tools for secretome analysis, Biochim. Biophys. Acta Proteins Proteom, vol.1834, pp.2442-2453, 2013.

S. Keerthikumar, A catalogue of human secreted proteins and its implications, AIMS Biophys, vol.3, pp.563-570, 2016.

M. Uhlén, L. Fagerberg, B. M. Hallström, C. Lindskog, P. Oksvold et al., Tissue-based map of the human proteome, vol.347, p.1260419, 2015.

C. Rabouille, Pathways of Unconventional Protein Secretion, Trends Cell Biol, vol.27, pp.230-240, 2017.

M. Dean and T. Annilo, Evolution of the Atp-Binding Cassette (ABC) Transporter Superfamily in Vertebrates, Annu. Rev. Genom. Hum. Genet, vol.6, pp.123-142, 2005.

J. J. Repa and D. J. Mangelsdorf, The Role of Orphan Nuclear Receptors in the Regulation of Cholesterol Homeostasis, Annu. Rev. Cell Dev. Biol, vol.16, pp.459-481, 2000.

J. Robelin and L. Casteilla, Différenciation, croissance et développement du tissu adipeux, Prod. Anim, vol.3, p.17, 1990.

B. Picard, C. Jurie, M. P. Duris, and G. Renand, Consequences of selection for higher growth rate on muscle fibre development in cattle, Livest. Sci, vol.102, pp.107-120, 2006.
URL : https://hal.archives-ouvertes.fr/hal-02654026

S. P. Bonny, G. E. Gardner, D. W. Pethick, I. Legrand, R. J. Polkinghorne et al., Biochemical measurements of beef are a good predictor of untrained consumer sensory scores across muscles, Animal, vol.9, pp.179-190, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02638458

J. B. Wallingford and B. Mitchell, Strange as it may seem: The many links between Wnt signaling, planar cell polarity, and cilia, Genes Dev, vol.25, pp.201-213, 2011.

P. Satir, L. B. Pedersen, and S. T. Christensen, The primary cilium at a glance, J. Cell Sci, vol.123, pp.499-503, 2010.

N. H. Marican, S. B. Cruz-migoni, and A. G. Borycki, Asymmetric distribution of primary cilia allocates satellite cells for self-renewal, Stem Cell Rep, vol.6, pp.798-805, 2016.

G. Tian, P. Ropelewski, I. Nemet, R. Lee, K. H. Lodowski et al., An unconventional secretory pathway mediates the cilia targeting of peripherin/rds, J. Neurosci, vol.34, pp.992-1006, 2014.

, Int. J. Mol. Sci, vol.2020, p.664

M. F. Ribeiro, H. Zhu, R. W. Millard, and G. Fan, Exosomes Function in Pro-and Anti-Angiogenesis, Curr. Angiogenes, vol.2, pp.54-59, 2013.

J. Meldolesi, Exosomes and Ectosomes in Intercellular Communication, Curr. Biol, vol.28, pp.435-444, 2018.

P. Kharaziha, S. Ceder, Q. Li, and T. Panaretakis, Tumor cell-derived exosomes: A message in a bottle, Biochim. Biophys. Acta Rev. Cancer, vol.1826, pp.103-111, 2012.

G. Raposo and W. Stoorvogel, Extracellular vesicles: Exosomes, microvesicles, and friends, J. Cell Biol, pp.373-383, 0200.

M. Yáñez-mó, P. R. Siljander, Z. Andreu, A. Bedina-zavec, F. E. Borràs et al., Biological properties of extracellular vesicles and their physiological functions, J. Extracell. Vesicles, 2015.

M. H. Vasconcelos, H. R. Caires, A. ?bols, C. P. Xavier, and A. Lin?, Extracellular vesicles as a novel source of biomarkers in liquid biopsies for monitoring cancer progression and drug resistance, Drug Resist. Updates, vol.47, 2019.

D. P. Romancino, G. Paterniti, Y. Campos, A. De-luca, V. Di-felice et al., Identification and characterization of the nano-sized vesicles released by muscle cells, FEBS Lett, vol.587, pp.1379-1384, 2013.

A. Forterre, A. Jalabert, E. Berger, M. Baudet, K. Chikh et al., Proteomic Analysis of C2C12 Myoblast and Myotube Exosome-Like Vesicles: A New Paradigm for Myoblast-Myotube Cross Talk?, PLoS ONE, vol.9, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01859453

R. M. Canet-avilés, M. A. Wilson, D. W. Miller, R. Ahmad, C. Mclendon et al., The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization, Proc. Natl. Acad. Sci, vol.101, pp.9103-9108, 2004.

M. Eldh, K. Ekström, H. Valadi, M. Sjöstrand, B. Olsson et al., Exosomes Communicate Protective Messages during Oxidative Stress; Possible Role of Exosomal Shuttle RNA, PLoS ONE, vol.5, 2010.

D. Cruz-garcia, A. J. Curwin, J. Popoff, C. Bruns, J. M. Duran et al., Remodeling of secretory compartments creates CUPS during nutrient starvation, J. Cell Biol, vol.207, pp.695-703, 2014.

S. Rome, A. Forterre, M. L. Mizgier, and K. Bouzakri, Skeletal Muscle-Released Extracellular Vesicles: State of the Art, Front. Physiol, vol.10, p.929, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02466242

L. Bihan, M. C. Bigot, A. Jensen, S. S. Dennis, J. L. Rogowska-wrzesinska et al., In-depth analysis of the secretome identifies three major independent secretory pathways in differentiating human myoblasts, J. Proteom, vol.77, pp.344-356, 2012.

S. S. Chauhan and E. M. England, Postmortem glycolysis and glycogenolysis: Insights from species comparisons, Meat Sci, vol.144, pp.118-126, 2018.

P. D. Stahl and G. Raposo, Extracellular Vesicles: Exosomes and Microvesicles, Integrators of Homeostasis, Physiology (Bethesda), vol.34, pp.169-177, 2019.

I. Parolini, C. Federici, C. Raggi, L. Lugini, S. Palleschi et al., Microenvironmental pH is a key factor for exosome traffic in tumor cells, J. Biol. Chem, vol.284, pp.34211-34222, 2009.

V. L. Vega, M. Rodríguez-silva, T. Frey, M. Gehrmann, J. C. Diaz et al., Hsp70 Translocates into the Plasma Membrane after Stress and Is Released into the Extracellular Environment in a Membrane-Associated Form that Activates Macrophages, J. Immunol, vol.180, pp.4299-4307, 2008.

R. Gastpar, M. Gehrmann, M. A. Bausero, A. Asea, C. Gross et al., Heat Shock Protein 70 Surface-Positive Tumor Exosomes Stimulate Migratory and Cytolytic Activity of Natural Killer Cells, Cancer Res, vol.65, pp.5238-5247, 2005.

A. Clayton, A. Turkes, H. Navabi, M. D. Mason, and Z. Tabi, Induction of heat shock proteins in B-cell exosomes, J. Cell Sci, vol.118, pp.3631-3638, 2005.

J. Mccready, J. D. Sims, D. Chan, and D. G. Jay, Secretion of extracellular hsp90? via exosomes increases cancer cell motility: A role for plasminogen activation, BMC Cancer, vol.10, 2010.

, Int. J. Mol. Sci, vol.2020, p.664

J. R. Bamburg and B. W. Bernstein, Roles of ADF/cofilin in actin polymerization and beyond, Biol. Rep, 1000.

S. Dunner, N. Sevane, D. Garcia, H. Levéziel, J. L. Williams et al., Genes involved in muscle lipid composition in 15 European Bos taurus breeds, Anim. Genet, vol.44, pp.493-501, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01211969

X. Jia, K. Hollung, M. Therkildsen, K. I. Hildrum, and E. Bendixen, Proteome analysis of early post-mortem changes in two bovine muscle types:M. longissimus dorsi andM, Semitendinosis. Proteomics, vol.6, pp.936-944, 2006.

T. M. Svitkina, A. B. Verkhovsky, and G. G. Borisy, Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton, J. Cell Biol, vol.135, pp.991-1007, 1996.

G. Zernig and G. Wiche, Morphological integrity of single adult cardiac myocytes isolated by collagenase treatment: Immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin, Eur. J. Cell Biol, vol.38, p.14, 1985.

O. Jaka, L. Casas-fraile, A. L. De-munain, and A. Sáenz, Costamere proteins and their involvement in myopathic processes, Expert Rev. Mol. Med, vol.17, 2015.

I. M. Thornell and M. O. Bevensee, Regulators of Slc4 bicarbonate transporter activity, Front. Physiol, vol.6, 2015.

N. Kaspric, B. Picard, M. Reichstadt, J. Tournayre, and M. Bonnet, ProteINSIDE to easily investigate proteomics data from ruminants: Application to mine proteome of adipose and muscle tissues in bovine foetuses, PLoS ONE, vol.10, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02635637

F. Supek, M. Bo?njak, N. ?kunca, and T. ?muc, REVIGO Summarizes and Visualizes Long Lists of Gene Ontology Terms, PLoS ONE, vol.6, 2011.

W. Nickel and C. Rabouille, Mechanisms of regulated unconventional protein secretion, Nat. Rev. Mol. Cell Biol, vol.10, pp.148-155, 2009.

P. Shannon, A. Markiel, O. Ozier, N. S. Baliga, J. T. Wang et al., Cytoscape: A software Environment for integrated models of biomolecular interaction networks, Genome Res, vol.13, pp.2498-2504, 2003.

. Psicquic-registry, Available online, 2020.

S. Boudon, J. Henry-berger, and I. Cassar-malek, Aggregation of Omic Data and Secretome Prediction Enable the Discovery of Candidate Plasma Biomarkers for Beef Tenderness, Int. J. Mol. Sci, vol.21, p.664, 2020.
URL : https://hal.archives-ouvertes.fr/hal-02516737

C. Bernard, I. Cassar-malek, M. L. Cunff, H. Dubroeucq, G. Renand et al., New indicators of beef sensory quality revealed by expression of specific genes, J. Agric. Food Chem, vol.55, pp.5229-5237, 2007.
URL : https://hal.archives-ouvertes.fr/hal-02667197

N. K. Kim, S. Cho, S. H. Lee, H. R. Park, C. S. Lee et al., Proteins in longissimus muscle of Korean native cattle and their relationship to meat quality, Meat Sci, vol.80, pp.1068-1073, 2008.

J. Bouley, C. Chambon, and B. Picard, Mapping of bovine skeletal muscle proteins using twodimensional gel electrophoresis and mass spectrometry, Proteomics, vol.4, pp.1811-1824, 2004.
URL : https://hal.archives-ouvertes.fr/hal-02681208

S. G. Bjarnadóttir, K. Hollung, M. Høy, E. Bendixen, M. C. Codrea et al., Protein expression and oxygen consumption rate of early postmortem mitochondria relate to meat tenderness1, Changes Egelandsdal, vol.93, pp.1967-1979, 2015.

A. Lana, V. Longo, A. Dalmasso, A. D'alessandro, M. T. Bottero et al., Omics integrating physical techniques: Aged Piedmontese meat analysis, Food Chem, vol.172, pp.731-741, 2015.

B. Picard, N. Guillemin, M. Bonnet, S. G. Champanelle, I. Cassar-malek et al., Bonnet, 4.32 -Quest for Novel Muscle Pathway Biomarkers by Proteomics in Beef Production, Compr. Biotechnol, vol.1, pp.395-405, 2011.

B. C. Bowker, J. S. Eastridge, and M. B. Solomon, Measurement of Muscle Exudate Protein Composition as an Indicator of Beef Tenderness, J. Food Sci, vol.79, pp.1292-1297, 2014.

C. Zhao, L. Zan, Y. Wang, M. Scott-updike, G. Liu et al., Functional proteomic and interactome analysis of proteins associated with beef tenderness in Angus cattle, Livest. Sci, vol.161, pp.201-209, 2014.

A. D'alessandro, S. Rinalducci, C. Marrocco, V. Zolla, F. Napolitano et al., Love me tender: An Omics window on the bovine meat tenderness network, J. Proteomics, vol.75, pp.4360-4380, 2012.

S. Bongiorni, C. E. Gruber, S. Bueno, G. Chillemi, F. Ferr?? et al., Transcriptomic investigation of meat tenderness in two Italian cattle breeds, Anim. Genet, vol.47, pp.273-287, 2016.

C. Zhao, F. Tian, Y. Yu, J. Luo, Q. Hu et al., Muscle transcriptomic analyses in Angus cattle with divergent tenderness, Mol. Biol. Rep, vol.39, pp.4185-4193, 2012.

J. M. Malheiros, C. E. Enríquez-valencia, B. O. Da-silva-duran, T. G. De-paula, R. A. Curi et al., Association of CAST2 , HSP90AA1 , DNAJA1 and HSPB1 genes with meat tenderness in Nellore cattle, Meat Sci, vol.138, pp.49-52, 2018.

L. F. Fonseca, D. F. Gimenez, D. B. Dos-santos, R. Silva, F. Barthelson et al., Differences in global gene expression in muscle tissue of Nellore cattle with divergent meat tenderness, BMC Genomics, vol.18, p.945, 2017.

J. Hocquette, C. Bernard-capel, V. Vidal, B. Jesson, H. Levéziel et al., The GENOTEND chip: a new tool to analyse gene expression in muscles of beef cattle for beef quality prediction, BMC Vet. Res, vol.8, p.135, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01211927

H. J. Kee, E. W. Park, and C. K. Lee, Characterization of beef transcripts correlated with tenderness and moisture, Mol. Cells, vol.25, pp.428-437, 2008.

Y. Y. Fan, L. Sen-zan, C. Z. Fu, W. Q. Tian, H. B. Wang et al., Three novel SNPs in the coding region of PPAR? gene and their associations with meat quality traits in cattle, Mol. Biol. Rep, vol.38, pp.131-137, 2011.

S. Allais, L. Journaux, H. Levéziel, N. Payet-duprat, P. Raynaud et al., Effects of polymorphisms in the calpastatin and ?-calpain genes on meat tenderness in 3 French beef breeds, J. Anim. Sci, vol.89, pp.1-11, 2011.

C. E. Rexroad, I. , G. L. Bennett, R. T. Stone, J. W. Keele et al., Comparative mapping of BTA15 and HSA11 including a region containing a QTL for meat tenderness, Mamm. Genome, vol.12, pp.561-565, 2001.

P. C. Tizioto, J. E. Decker, J. F. Taylor, R. D. Schnabel, M. A. Mudadu et al., , vol.29

, DO and SB performed the statistical analysis. VM designed and co-managed the experiments

, All authors collaborated to interpretation and discussion of the results. All authors have given approval to the final version of the manuscript

G. Renand, B. Picard, C. Touraille, P. Berge, and J. Lepetit, Relationships between 728 muscle characteristics and meat quality traits of young Charolais bulls, Meat 729 Sci, vol.59, pp.49-60, 2001.

S. Chriki, G. Renand, B. Picard, D. Micol, L. Journaux et al., Meta-731 analysis of the relationships between beef tenderness and muscle 732 characteristics, Livest. Sci, vol.155, 2013.

M. P. Ellies-oury, R. Dumont, G. Perrier, M. Roux, D. Micol et al., Effect 734 of age and carcass weight on quality traits of m. rectus abdominis from 735 Charolais heifers, Animal, pp.1-8, 2016.

M. Gagaoua, B. Picard, J. Soulat, and V. Monteils, Clustering of sensory eating 737 qualities of beef: Consistencies and differences within carcass, muscle, animal 738 characteristics and rearing factors, Livest. Sci, vol.214, pp.245-258, 2018.

A. Ouali, C. H. Herrera-mendez, G. Coulis, S. Becila, A. Boudjellal et al., , p.741

M. A. Sentandreu, Revisiting the conversion of muscle into meat and the 742 underlying mechanisms, Meat Sci, vol.74, pp.44-58, 2006.

B. Picard and M. Gagaoua, Proteomic Investigations of Beef Tenderness, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01580641

A. D'alessandro, S. Rinalducci, C. Marrocco, V. Zolla, F. Napolitano et al.,

. Zolla, Love me tender: An Omics window on the bovine meat tenderness 748 network, J. Proteomics, vol.75, pp.4360-4380, 2012.

N. Guillemin, M. Bonnet, C. Jurie, and B. Picard, Functional analysis of beef 750 tenderness, J. Proteomics, vol.75, pp.352-365, 2011.

B. Picard, M. Gagaoua, D. Micol, I. Cassar-malek, J. Hocquette et al.,

. Terlouw, Inverse Relationships between Biomarkers and Beef Tenderness 753 According to Contractile and Metabolic Properties of the Muscle, J. Agric

, Food Chem, vol.62, pp.9808-9818, 2014.

S. Surinova, R. Schiess, R. Ttenhain, F. Cerciello, B. Wollscheid et al.,

. Aebersold, On the Development of Plasma Protein Biomarkers, J. Proteome 757 Res, vol.10, pp.5-16, 2011.

S. Lista, F. Faltraco, D. Prvulovic, and H. Hampel, Blood and plasma-based 759 proteomic biomarker research in Alzheimer's disease, Prog. Neurobiol. 101, vol.760, pp.1-17, 2013.

S. G. Coca, G. N. Nadkarni, Y. Huang, D. G. Moledina, V. Rao et al.,

S. T. Ferket, L. F. Crowley, C. R. Fried, and . Parikh, Plasma Biomarkers and Kidney 763 Function Decline in Early and Established Diabetic Kidney Disease, J. Am

, Soc. Nephrol, vol.28, pp.2786-2793, 2017.

H. C. Beck, M. Overgaard, and L. M. Rasmussen, Plasma proteomics to 766 identify biomarkers -application to cardiovascular diseases

, Proteomics, vol.7, pp.40-48, 2015.

A. Marco-ramell, R. Pato, R. Peña, Y. Saco, X. Manteca et al., , p.769

A. Torre and . Bassols, Identification of serum stress biomarkers in pigs housed at 770 different stocking densities, Vet. J, vol.190, 2011.

L. R. Legleiter and J. W. Spears, Plasma diamine oxidase: A biomarker of copper 773 deficiency in the bovine1, J. Anim. Sci, vol.2, pp.2198-2204, 2007.

J. K. Grubbs, J. C. Dekkers, E. Huff-lonergan, C. K. Tuggle, and S. M. Lonergan, 776 Identification of potential serum biomarkers to predict feed efficiency in young 777 pigs, J. Anim. Sci, vol.94, pp.1482-1492, 2016.

J. Soulat, B. Picard, S. Léger, M. Ellies-oury, and V. Monteils, Preliminary 779 Study to Determinate the Effect of the Rearing Managements Applied during 780 eifers' Whole Life on Carcass and Flank Steak Quality, 2018.

J. Soulat, V. Monteils, and B. Picard, Effect of the Rearing Managements Applied 783 during eifers' Whole Life on Quality Traits of Five Muscles of the Beef Rib, 784 Foods, vol.8, p.157, 2019.

E. Dransfield, J. Martin, D. Bauchart, S. Abouelkaram, J. Lepetit et al., Meat quality and composition of three muscles from French 787 cull cows and young bulls, Anim. Sci, vol.76, pp.387-399, 2003.

J. Soulat, B. Picard, S. Léger, and V. Monteils, Prediction of beef carcass and meat 790 quality traits from factors characterising the rearing management system 791 applied during the whole life of heifers, Meat Sci, vol.140, 2018.

S. Allais, H. Lev??ziel, J. F. Hocquette, S. Rousset, C. Denoyelle et al., , p.794

G. Renand, Fine mapping of quantitative trait loci underlying sensory meat 795 quality traits in three French beef cattle breeds, J. Anim. Sci, vol.92, p.4341, 2014.

T. Chaze, J. Hocquette, B. Meunier, G. Renand, C. Jurie et al.,

S. Journaux, C. Rousset, J. Denoyelle, B. Lepetit, and . Picard, Biological Markers 799 for Meat Tenderness of the Three Main French Beef Breeds Using 2-DE and 800 MS Approach, Proteomics in Foods, pp.801-127, 2013.

B. Picard, M. Gagaoua, M. Al-jammas, L. Koning, A. Valais et al., Bonnet, 803 Beef tenderness and intramuscular fat proteomic biomarkers: muscle type 804 effect, PeerJ, vol.6, p.4891, 2018.

S. Murphy and P. Dowling, DIGE Analysis of ProteoMinerTM Fractionated, vol.806

, Serum/Plasma Samples, vol.807, pp.109-114, 2018.

L. Li, Dynamic Range Compression with ProteoMiner TM : Principles and 809 Examples, vol.810, pp.99-107, 2015.

A. Chawade, E. Alexandersson, and F. Levander, Normalyzer: A Tool for Rapid 812 Evaluation of Normalization Methods for Omics Data Sets, J. Proteome Res, vol.813, pp.3114-3120, 2014.

T. Mehmood, K. H. Liland, L. Snipen, and S. Saebø, A review of variable selection 815 methods in Partial Least Squares Regression, Chemom. Intell. Lab. Syst, vol.118, pp.62-69, 2012.

I. Chong and C. Jun, Performance of some variable selection methods when 818 multicollinearity is present, Chemom. Intell. Lab. Syst, vol.78, pp.103-112, 2005.

M. Gagaoua, V. Monteils, and B. Picard, Data from the Farmgate-to-Meat 821 Continuum Including Omics-Based Biomarkers to Better Understand the 822 Variability of Beef Tenderness: An Integromics Approach, J. Agric. Food 823 Chem, vol.66, pp.13552-13563, 2018.

M. P. Ellies-oury, M. Chavent, A. Conanec, M. Bonnet, B. Picard et al., 825 Statistical model choice including variable selection based on variable 826 importance: A relevant way for biomarkers selection to predict meat 827 tenderness, Sci. Rep, vol.9, p.10014, 2019.

N. Kaspric, B. Picard, M. Reichstadt, J. Tournayre, and M. Bonnet, ProteINSIDE to 829 easily investigate proteomics data from ruminants: Application to mine 830 proteome of adipose and muscle tissues in bovine foetuses, PLoS One, vol.10, pp.1-24, 2015.

B. Picard, B. Lebret, I. Cassar-malek, L. Liaubet, C. Berri et al., Recent advances in omic technologies for meat 834 quality management, Meat Sci, vol.109, pp.18-26, 2015.

I. Cassar-malek and B. Picard, Expression Marker-Based Strategy to Improve Beef 837 Quality, Sci. World J, vol.2016, pp.1-11, 2016.

B. Picard, N. Guillemin, M. Bonnet, S. G. Champanelle, I. Cassar-malek et al.,

M. Guillemin, Bonnet, 4.32 -Quest for Novel Muscle Pathway Biomarkers by 840 Proteomics in Beef Production, Compr. Biotechnol, vol.1, pp.395-405, 2011.

S. Magdeldin, S. Enany, Y. Yoshida, B. Xu, Y. Zhang et al.,

E. Lokamani, T. Yaoita, and . Yamamoto, Basics and recent advances of two 844 dimensional-polyacrylamide gel electrophoresis, Clin. Proteomics, vol.11, p.16, 2014.

A. Görg, W. Weiss, and M. J. Dunn, Current two-dimensional electrophoresis 847 technology for proteomics, Proteomics, vol.4, pp.3665-3685, 2004.

V. Santoni, M. Molloy, and T. Rabilloud, Membrane proteins and proteomics: Un 850 amour impossible?, Electrophoresis, vol.21, pp.2-8, 2000.

M. P. Molloy, Two-Dimensional Electrophoresis of Membrane Proteins Using 854 Immobilized pH Gradients, Anal. Biochem, vol.280, 2000.

B. Picard and M. Gagaoua, Proteomic Investigations of Beef Tenderness, p.857
URL : https://hal.archives-ouvertes.fr/hal-01580641

, Proteomics Food Sci, pp.177-197, 2017.

B. Picard and M. Gagaoua, Meta-proteomics for the discovery of protein 860 biomarkers of beef tenderness: An overview of integrated studies, Food Res

. Int, , vol.127, p.108739, 2020.

K. A. Clark, A. S. Mcelhinny, M. C. Beckerle, and C. C. Gregorio, Striated Muscle 863 Cytoarchitecture: An Intricate Web of Form and Function, Annu. Rev. Cell

, Dev. Biol, vol.18, pp.637-706, 2002.

I. Papa, C. Astier, O. Kwiatek, F. Raynaud, C. Bonnal et al.,

Y. Roustan and . Benyamin, Alpha actinin-CapZ, an anchoring complex for thin 867 filaments in Z-line, J. Muscle Res. Cell Motil, vol.20, pp.187-97, 1999.

. ?-rené-lametsch, . Anders-karlsson, ?. Katja-rosenvold, and . Enrik, Jørgen, vol.870

?. Andersen and P. Roepstorff, ? Emøke Bendixen*, Postmortem Proteome 871 Changes of Porcine Muscle Related to Tenderness, vol.872, 2003.

S. G. Bjarnadóttir, K. Hollung, E. M. Frgestad, and E. Veiseth-kent, Proteome 874 changes in bovine longissimus thoracis muscle during the first 48 h 875 postmortem: Shifts in energy status and myofibrillar stability, J. Agric. Food, vol.876, pp.7408-7414, 2010.

J. Bouley, B. Meunier, J. Culioli, and B. Picard, Analyse protéomique du muscle de 878 Bovin appliquée à la recherche de marqueurs de la tendreté de la viande

, Rech. Rumin, pp.87-89, 2004.

M. E. Carvalho, G. Gasparin, M. D. Poleti, A. F. Rosa, J. C. Balieiro et al.,

R. T. Labate, R. R. Nassu, L. C. Tullio, G. B. Regitano, and L. L. Mourão,

. Coutinho, Heat shock and structural proteins associated with meat tenderness 883 in Nellore beef cattle, a Bos indicus breed, Meat Sci, vol.96, 2014.

K. T. Vaughan, F. E. Weber, T. Ried, D. C. Ward, F. C. Reinach et al., , p.886

, Human Myosin-Binding Protein H (MyBP-H): Complete Primary Sequence, p.887

, Genomic Organization, and Chromospinal Localization, Genomics, vol.16, pp.34-40, 1993.

M. J. Anderson, S. M. Lonergan, and E. Huff-lonergan, Myosin light chain 1 release 890 from myofibrillar fraction during postmortem aging is a potential indicator of 891 proteolysis and tenderness of beef, Meat Sci, vol.90, pp.345-351, 2012.

C. Bernard, I. Cassar-malek, M. L. Cunff, H. Dubroeucq, G. Renand et al.,

. Hocquette, New indicators of beef sensory quality revealed by expression of 895 specific genes, J. Agric. Food Chem, vol.55, pp.5229-5237, 2007.

C. Zhao, L. Zan, Y. Wang, M. Scott-updike, G. Liu et al.,

V. I. Baldwin and J. Song, Functional proteomic and interactome analysis of proteins 899 associated with beef tenderness in Angus cattle, Livest. Sci, vol.161, pp.201-900, 2014.

S. Dunner, N. Sevane, D. García, O. Cortés, A. Valentini et al.,

J. Mangin, H. Cañón, and . Levéziel, Association of genes involved in carcass and 903 meat quality traits in 15 European bovine breeds, Livest. Sci, vol.154, pp.34-904, 2013.

J. Bazile, B. Picard, C. Chambon, A. Valais, and M. Bonnet, Pathways and 906 biomarkers of marbling and carcass fat deposition in bovine revealed by a 907 combination of gel-based and gel-free proteomic analyses, Meat Sci, vol.156, pp.146-155, 2019.

Q. Yu, X. Tian, L. Shao, L. Xu, R. Dai et al., Label-free proteomic strategy to 910 compare the proteome differences between longissimus lumborum and psoas 911 major muscles during early postmortem periods, Food Chem, vol.269, p.435, 2018.

S. Jiang, Y. Liu, Z. Shen, B. Zhou, and Q. W. Shen, Acetylome profiling reveals 914 extensive involvement of lysine acetylation in the conversion of muscle to 915 meat, J. Proteomics, vol.205, p.103412, 2019.

H. Kee, E. P. , and C. Lee, Characterization of Beef Transcripts 917 Correlated with Tenderness and Moisture, Mol. Cells, vol.25, pp.428-437, 2008.

, January, vol.29, 2018.

L. O. Fiems, S. D. Campeneere, S. De, G. Smet, J. M. Van-de-voorde et al., Relationship between fat depots in carcasses of beef bulls and 922 effect on meat colour and tenderness, vol.56, pp.17-23, 2000.

E. Tolosano and F. Altruda, Hemopexin: Structure, Function, and Regulation, vol.21, pp.297-306, 2002.

A. Di-luca, G. Elia, R. Hamill, and A. M. Mullen, 2D DIGE proteomic analysis of 927 early post mortem muscle exudate highlights the importance of the stress 928 response for improved water-holding capacity of fresh pork meat, Proteomics, vol.929, pp.1528-1544, 2013.

G. Ge, N. Seo, X. Liang, D. R. Hopkins, M. Höök et al., Bone 931 morphogenetic protein-1/tolloid-related metalloproteinases process osteoglycin 932 and enhance its ability to regulate collagen fibrillogenesis, J. Biol. Chem, vol.279, pp.41626-41659, 2004.

K. Tanaka, E. Matsumoto, Y. Higashimaki, T. Katagiri, T. Sugimoto et al., Role of osteoglycin in the linkage between muscle and bone, J. Biol

, Chem, vol.287, pp.11616-11644, 2012.

P. Beeckmann, J. Schroffel, G. Moser, H. Bartenschlager, G. Reiner et al.,

. Geldermann, Linkage and QTL mapping for Sus scrofa chromosome 3

, Anim. Breed. Genet, vol.120, pp.20-27, 2003.

A. Stratil, M. Van-poucke, H. Bartenschlager, A. Knoll, M. Yerle et al.,

M. Peelman, H. Kope?ny, and . Geldermann, Porcine OGN and ASPN: mapping, 943 polymorphisms and use for quantitative trait loci identification for growth and 944 carcass traits in a Meishan × Pietrain intercross, Anim. Genet, vol.37, pp.415-945, 2006.

M. Morzel, C. Terlouw, C. Chambon, D. Micol, and B. Picard, Muscle proteome 947 and meat eating qualities of Longissimus thoracis of "Blonde d'Aquitaine" 948 young bulls: A central role of HSP27 isoforms, Meat Sci, vol.78, pp.297-304, 2008.

B. Picard, C. Berri, L. Lefaucheur, C. Molette, T. Sayd et al., Skeletal 951 muscle proteomics in livestock production, Briefings Funct. Genomics 952 Proteomics, vol.9, pp.259-278, 2010.

A. D?alessandro, C. Marrocco, V. Zolla, M. D?andrea, and L. Zolla, Meat quality 954 of the longissimus lumborum muscle of Casertana and Large White pigs: 955 Metabolomics and proteomics intertwined, J. Proteomics, vol.75, pp.610-627, 2011.

V. Grabe?, M. Kathri, V. Phung, K. M. Moe, E. Slinde et al.,

B. Saarem, V. Egelandsdal, M. Grabe??, V. Kathri, K. M. Phung et al.,

M. Slinde, K. Skaugen, and B. Saarem, Protein expression and 960 oxygen consumption rate of early postmortem mitochondria relate to meat 961 tenderness, J. Anim. Sci, vol.93, pp.1967-1979, 2015.

X. Jia, E. Veiseth-kent, H. Grove, P. Kuziora, L. Aass et al.,

. Hollung, Peroxiredoxin-6 A potential protein marker for meat tenderness in 964 bovine longissimus thoracis muscle, J. Anim. Sci, vol.87, 2009.

A. Kwasiborski, T. Sayd, C. Chambon, V. Santé-lhoutellier, D. Rocha et al.,

. Terlouw, Pig Longissimus lumborum proteome: Part II: Relationships between 968 protein content and meat quality, Meat Sci, vol.80, 2008.

N. Guillemin, C. Jurie, I. Cassar-malek, J. F. Hocquette, G. Renand et al., 971 Variations in the abundance of 24 protein biomarkers of beef tenderness 972 according to muscle and animal type, Animal, vol.5, pp.885-894, 2011.

M. C. Le-bihan, A. Bigot, S. S. Jensen, J. L. Dennis, A. Rogowska-wrzesinska et al., Coulton, 976 G. Butler-Browne, In-depth analysis of the secretome identifies three major 977 independent secretory pathways in differentiating human myoblasts

, Proteomics, vol.77, pp.344-356, 2012.

E. Cocucci, G. Racchetti, and J. Meldolesi, Shedding microvesicles: artefacts no 980 more, Trends Cell Biol, vol.19, pp.43-51, 2009.

C. Théry, M. Ostrowski, and E. Segura, Membrane vesicles as conveyors of 982 immune responses, Nat. Rev. Immunol, vol.9, pp.581-593, 2009.

M. F. Ribeiro, H. Zhu, R. W. Millard, and G. Fan, Exosomes Function in Pro-985 and Anti-Angiogenesis, Curr. Angiogenes, vol.2, pp.54-59, 2013.

S. Ailawadi, X. Wang, H. Gu, and G. Fan, Pathologic function and therapeutic 988 potential of exosomes in cardiovascular disease, Biochim. Biophys. Acta -Mol

, , pp.1-11, 2015.

R. M. Johnstone, M. Adam, J. R. Hammond, L. Orr, and C. Turbide, Vesicle 991 formation during reticulocyte maturation. Association of plasma membrane 992 activities with released vesicles (exosomes), J. Biol. Chem, vol.262, p.9412, 1987.

J. Meldolesi, Exosomes and Ectosomes in Intercellular Communication, Curr

, Biol, vol.28, pp.435-444, 2018.

E. I. Buzas, B. György, G. Nagy, A. Falus, and S. Gay, Emerging role of 997 extracellular vesicles in inflammatory diseases, Nat. Rev. Rheumatol, vol.10, pp.356-364, 2014.

M. Record, K. Carayon, M. Poirot, and S. Silvente-poirot, Exosomes as new 1000 vesicular lipid transporters involved in cell-cell communication and various 1001 pathophysiologies, Biochim. Biophys. Acta -Mol. Cell Biol. Lipids, vol.1841, pp.108-120, 2014.

P. Kharaziha, S. Ceder, Q. Li, and T. Panaretakis, Tumor cell-derived exosomes: A 1004 message in a bottle, Biochim. Biophys. Acta -Rev. Cancer, vol.1826, pp.103-1005, 2012.

S. Rome, A. Forterre, M. L. Mizgier, and K. Bouzakri, , p.1007

, Extracellular Vesicles: State of the Art, Front. Physiol, vol.10, 2019.

M. Guescini, D. Guidolin, L. Vallorani, L. Casadei, A. M. Gioacchini et al.,

M. Tibollo, E. Battistelli, L. Falcieri, L. F. Battistin, V. Agnati et al., C2C12 1011 myoblasts release micro-vesicles containing mtDNA and proteins involved in 1012 signal transduction, Exp. Cell Res, vol.316, pp.1977-1984, 1013.

D. P. Romancino, G. Paterniti, Y. Campos, A. De-luca, V. Di-felice et al., Identification and characterization of the nano-sized 1016 vesicles released by muscle cells, FEBS Lett, vol.587, pp.1379-1384, 1017.

A. Forterre, A. Jalabert, E. Berger, M. Baudet, K. Chikh et al., , 1019.

S. Larichaudy, M. Chanon, A. Weiss-gayet, M. Hesse, A. Record et al., Proteomic Analysis of C2C12 Myoblast 1021 and Myotube Exosome-Like Vesicles: A New Paradigm for Myoblast-Myotube 1022 Cross Talk?, PLoS One, vol.9, p.84153, 2014.

X. Jia, K. Hollung, M. Therkildsen, K. I. Hildrum, and E. Bendixen, Proteome 1024 analysis of early post-mortem changes in two bovine muscle types:M. 1025 longissimus dorsi andM. semitendinosis, pp.936-944, 1026.

E. Laville, T. Sayd, M. Morzel, S. Blinet, C. Chambon et al., Proteome changes during meat aging in tough and tender beef 1029 suggest the importance of apoptosis and protein solubility for beef aging and 1030 tenderization, J. Agric. Food Chem, vol.57, pp.10755-10764, 1031.

M. Matsushita, S. Thiel, J. C. Jensenius, I. Terai, and T. Fujita, Proteolytic activities 1033 of two types of mannose-binding lectin-associated serine protease, J. Immunol, vol.1034, pp.2637-2679, 2000.

J. M. Gutiérrez and C. L. Ownby, Skeletal muscle degeneration induced by venom 1036 phospholipases A2: insights into the mechanisms of local and systemic 1037 myotoxicity, Toxicon, vol.42, pp.915-931, 1038.

A. Ouali, M. Gagaoua, Y. Boudida, S. Becila, A. Boudjellal et al., , p.1040

M. A. Mendez and . Sentandreu, Biomarkers of meat tenderness: Present knowledge 1041 and perspectives in regards to our current understanding of the mechanisms 1042 involved, Meat Sci, vol.95, pp.854-870, 2013.

M. Gagaoua, K. Hafid, Y. Boudida, S. Becila, A. Ouali et al.,

M. A. Boudjellal and . Sentandreu, Caspases and Thrombin Activity Regulation by 1045 Specific Serpin Inhibitors in Bovine Skeletal Muscle, Appl. Biochem

, Biotechnol, vol.177, pp.279-303, 2015.

M. Gagaoua, Y. Boudida, S. Becila, B. Picard, A. Boudjellal et al.,

A. Sentandreu and . Ouali, New Caspases' inhibitors belonging to the serpin 1050 superfamily: A novel key control point of apoptosis in mammalian tissues, p.1051

, Adv. Biosci. Biotechnol, pp.740-750, 2012.

Z. Hu, C. A. Park, X. Wu, and J. M. Reecy, Animal QTLdb: an improved 1053 database tool for livestock animal QTL/association data dissemination in the 1054 post-genome era, Nucleic Acids Res, vol.41, pp.871-879, 2013.

M. Abril, M. Campo, A. Önenç, C. Sañudo, P. Albert?? et al., Beef colour evolution as a function of ultimate pH, Meat Sci, vol.58, pp.69-78, 2001.

A. Albert, On the use and computation of likelihood ratios in clinical chemistry, Clin. Chem, vol.28, 1982.

E. Aleo, C. J. Henderson, A. Fontanini, B. Solazzo, and C. Brancolini, Identification of New Compounds That Trigger Apoptosome-Independent Caspase Activation and Apoptosis, Cancer Res, vol.66, pp.9235-9244, 2006.

S. Allard, P. Adin, L. Gouédard, N. Di-clemente, N. Josso et al., Molecular mechanisms of hormone-mediated Müllerian duct regression: involvement of betacatenin, Development, vol.127, pp.3349-60, 2000.

P. G. Allingham, G. S. Harper, and R. A. Hunter, Effect of growth path on the tenderness of the semitendinosus muscle of Brahman-cross steers, Meat Sci, vol.48, pp.65-73, 1998.

A. M. De-almeida, I. Miller, and D. Eckersall, Proteomics in domestic animals: From farm to systems biology, p.p, 2017.

R. Alonso, C. Mazzeo, M. C. Rodriguez, M. Marsh, A. Fraile-ramos et al., Diacylglycerol kinase ? regulates the formation and polarisation of mature multivesicular bodies involved in the secretion of Fas ligand-containing exosomes in T lymphocytes, Cell Death Differ, vol.18, pp.1161-1173, 2011.

S. Van-altena, B. De-klerk, K. A. Hettinga, R. Van-neerven, S. Boeren et al., A proteomics-based identification of putative biomarkers for disease in bovine milk, Vet. Immunol. Immunopathol, vol.174, pp.11-18, 2016.

E. B. Altinta? and A. Denizli, Efficient removal of albumin from human serum by monosize dye-affinity beads, J. Chromatogr. B Anal. Technol. Biomed. Life Sci, vol.832, pp.216-223, 2006.

C. A. Andac, M. Andac, and A. Denizli, Predicting the binding properties of cibacron blue F3GA in affinity separation systems, Int. J. Biol. Macromol, vol.41, pp.430-438, 2007.

M. Andaç, Cibacron blue immobilized poly(glycidyl-methacrylate) nanobeads for albumin removal in proteome studies, Nanomedicine Biotechnol, vol.43, pp.133-139, 2015.

M. Andac, I. Galaev, and A. Denizli, Dye attached poly(hydroxyethyl methacrylate) cryogel for albumin depletion from human serum, J. Sep. Sci, vol.35, pp.1173-1182, 2012.

H. J. Andersen, N. Oksbjerg, J. F. Young, and M. Therkildsen, Feeding and meat quality -a future approach, Meat Sci, vol.70, pp.543-554, 2005.

M. J. Anderson, S. M. Lonergan, and E. Huff-lonergan, Myosin light chain 1 release from myofibrillar fraction during postmortem aging is a potential indicator of proteolysis and tenderness of beef, Meat Sci, vol.90, pp.345-351, 2012.

N. L. Anderson and N. G. Anderson, Proteome and proteomics: New technologies, new concepts, and new words, vol.19, pp.1853-1861, 1998.

N. L. Anderson and N. G. Anderson, The human plasma proteome: history, character, and diagnostic prospects, Mol. Cell. Proteomics, vol.1, pp.845-867, 2002.

. Anses, INCA 2. Etude individuelle Nationale sur les Consommations Alimentaires, 2007.

. Anses, INCA 3. Evolution des habitudes et modes de consommation, 2017.

B. Aranda, H. Blankenburg, S. Kerrien, F. Brinkman, A. Ceol et al., PSICQUIC and PSISCORE: accessing and scoring molecular interactions, Nat. Methods, vol.8, pp.528-529, 2011.

A. Arrigo, C. Paul, C. Ducasse, F. Manero, C. Kretz-remy et al., Small stress proteins: novel negative modulators of apoptosis induced independently of reactive oxygen species, Prog. Mol. Subcell. Biol, vol.28, pp.185-204, 2002.

A. Ashkenazi, Targeting death and decoy receptors of the tumour-necrosis factor superfamily, Nat. Rev. Cancer, vol.2, pp.420-430, 2002.

T. Astruc, Connective tissue: structure, function, and influence on meat quality, Encycl. Meat Sci, issue.1, pp.321-328, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02801237

A. Atak, S. Khurana, K. Gollapalli, P. J. Reddy, R. Levy et al., Quantitative mass spectrometry analysis reveals a panel of nine proteins as diagnostic markers for colon adenocarcinomas, Oncotarget, vol.9, pp.13530-13544, 2018.

A. J. Bailey, N. Light, and D. Nicholas, Connective tissue in meat and meat products, vol.355, 1989.

F. Baixauli, C. López-otín, and M. Mittelbrunn, Exosomes and autophagy: Coordinated mechanisms for the maintenance of cellular fitness, Front. Immunol, vol.5, 2014.

P. Balan, Y. Kim, and R. Blijenburg, Small heat shock protein degradation could be an indicator of the extent of myofibrillar protein degradation, Meat Sci, vol.97, pp.220-222, 2014.

W. A. Baldassini, C. P. Braga, L. Chardulo, J. Silva, J. M. Malheiros et al., Bioanalytical methods for the metalloproteomics study of bovine longissimus thoracis muscle tissue with different grades of meat tenderness in the Nellore breed, 2015.

, Food Chem, vol.169, pp.65-72

N. Bansal, A. K. Gupta, A. Gupta, S. N. Sankhwar, and A. A. Mahdi, Serum-based protein biomarkers of bladder cancer: A pre-and post-operative evaluation, J. Pharm. Biomed. Anal, vol.124, pp.22-25, 2016.

W. J. Barendse, DNA MARKERS FOR MEAT TENDERNESS, 2002.

C. Barlowe, L. Orci, T. Yeung, M. Hosobuchi, S. Hamamoto et al., COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum, Cell, vol.77, pp.895-907, 1994.

V. Bartheld, C. S. Altick, and A. L. , Multivesicular bodies in neurons: Distribution, protein content, and trafficking functions, Prog. Neurobiol, vol.93, pp.313-340, 2011.

S. Bas, Variations de la composition des dépôts lipidiques chez les bovins, Inra Prod. Anim, vol.14, issue.5, pp.311-322, 2001.

G. Bauchart, Qualite nutritionnelle des viandes et abats de bovins, Muscle et viande de ruminant, pp.115-130, 2010.

J. Bazile, Intégration de données publiques et analyses protéomiques pour relever les mécanismes et biomarqueurs du dépôt lipide dans la carcasse ou le muscle bovin, 2019.

J. Bazile, B. Picard, C. Chambon, A. Valais, and M. Bonnet, Pathways and biomarkers of marbling and carcass fat deposition in bovine revealed by a combination of gel-based and gel-free proteomic analyses, Meat Sci, vol.156, pp.146-155, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02626230

S. Beauclercq, L. Nadal-desbarats, C. Hennequet-antier, C. A. Tesseraud, S. Bourin et al., Serum and Muscle Metabolomics for the Prediction of Ultimate pH, a Key Factor for Chicken-Meat Quality, J. Proteome Res, vol.15, pp.1168-1178, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02639588

L. A. Beer, B. Ky, K. T. Barnhart, and D. W. Speicher, In-depth, reproducible analysis of human plasma using IgY 14 and SuperMix immunodepletion, Methods in Molecular Biology, pp.81-101, 2017.

H. M. Beere, "The stress of dying": the role of heat shock proteins in the regulation of apoptosis, J. Cell Sci, vol.117, pp.2641-51, 2004.

H. M. Beere, Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways, J. Clin. Invest, vol.115, pp.2633-2639, 2005.

M. Bellone, G. Iezzi, P. Rovere, G. Galati, A. Ronchetti et al., Processing of engulfed apoptotic bodies yields T cell epitopes, J. Immunol, vol.159, pp.5391-5400, 1997.

J. R. Bendall, Relations between muscle pH and important biochemical parameters during the postmortem changes in mammalian muscles, Meat Sci, vol.3, pp.143-157, 1979.

E. Bendixen, The use of proteomics in meat science, Meat Sci, vol.71, pp.138-149, 2005.

E. Bendixen, Understanding the Proteome, Proteomics in Foods, pp.3-19, 2013.

M. W. Berchtold, H. Brinkmeier, and M. Müntener, Calcium Ion in Skeletal Muscle: Its Crucial Role for Muscle Function, Plasticity, and Disease, Physiol. Rev, vol.80, pp.1215-1265, 2000.

Y. Berda-haddad, S. Robert, P. Salers, L. Zekraoui, C. Farnarier et al., Sterile inflammation of endothelial cell-derived apoptotic bodies is mediated by interleukin-1?, Proc. Natl. Acad. Sci. U. S. A, vol.108, pp.20684-20689, 2011.

T. O. Berg, M. Fengsrud, P. E. Strømhaug, T. Berg, and P. O. Seglen, Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes, J. Biol. Chem, vol.273, pp.21883-92, 1998.

J. Van-den-bergh, K. J. Button, J. Van-den-bergh, and K. Button, Meta-analysis of Environmental Références bibliographiques, 1997.

, Issues in Regional, Urban and Transport Economics. Urban Stud, vol.34, pp.927-944

E. S. Bergmann-leitner, R. M. Mease, E. H. Duncan, F. Khan, J. Waitumbi et al., Evaluation of immunoglobulin purification methods and their impact on quality and yield of antigen-specific antibodies, Malar. J, vol.7, 2008.

C. Bernard, I. Cassar-malek, L. Cunff, M. Dubroeucq, H. Renand et al., New indicators of beef sensory quality revealed by expression of specific genes, J. Agric. Food Chem, vol.55, pp.5229-5237, 2007.
URL : https://hal.archives-ouvertes.fr/hal-02667197

C. Bidault, Conservation de la viande et du poisson, 1927.

L. M. Biga, S. Dawson, A. Harwell, R. Hopkins, J. Kaufmann et al., Anatomy & Physiology. In: Anatomy & Physiology, 2020.

, Biomarkers and surrogate endpoints: Preferred definitions and conceptual framework, Biomarkers Definitions Working Group, vol.69, pp.89-95, 2001.

N. Bizat, J. Hermel, H. S. Jacquard, C. Créminon, C. Escartin et al., In Vivo Calpain/Caspase Cross-talk during 3-Nitropropionic Acid-induced Striatal Degeneration, J. Biol. Chem, vol.278, pp.43245-43253, 2003.
URL : https://hal.archives-ouvertes.fr/cea-02290633

S. G. Bjarnadóttir, K. Hollung, E. M. Frgestad, and E. Veiseth-kent, Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: Shifts in energy status and myofibrillar stability, J. Agric. Food Chem, vol.58, pp.7408-7414, 2010.

S. G. Bjarnadóttir, K. Hollung, M. Høy, E. Bendixen, M. C. Codrea et al., Changes in protein abundance between tender and tough meat from bovine Longissimus thoracis muscle assessed by isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis analysis, J. Anim. Sci, vol.90, pp.2035-2043, 2012.

L. V. Black, S. C. Saunderson, F. P. Coutinho, M. R. Muhsin-sharafaldine, T. T. Damani et al., The CD169 sialoadhesin molecule mediates cytotoxic T-cell responses to tumour apoptotic vesicles, Immunol. Cell Biol, vol.94, pp.430-438, 2016.

L. Blanc and M. Vidal, New insights into the function of Rab GTPases in the context of exosomal secretion, Small GTPases, vol.9, pp.95-106, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02307940

R. C. Bollineni, I. J. Guldvik, H. Grönberg, F. Wiklund, I. G. Mills et al., A differential protein solubility approach for the depletion of highly abundant proteins in plasma using ammonium sulfate, Analyst, vol.140, pp.8109-8117, 2015.

J. S. Bonifacino and B. S. Glick, The Mechanisms of Vesicle Budding and Fusion, Cell, vol.116, pp.153-166, 2004.

V. Bonifati, P. Rizzu, F. Squitieri, E. Krieger, N. Vanacore et al., Oostra Références bibliographiques

B. Meco, G. Heutink, and P. , DJ-1( PARK7), a novel gene for autosomal recessive, early onset parkinsonism, Neurol. Sci, vol.24, pp.159-160, 2003.

M. Bonnet, I. Cassar-malek, Y. Chilliard, and B. Picard, Ontogenesis of muscle and adipose tissues and their interactions in ruminants and other species, animal, vol.4, pp.1093-1109, 2010.
URL : https://hal.archives-ouvertes.fr/hal-02667753

S. Bortoluzzi, P. Scannapieco, A. Cestaro, G. A. Danieli, and S. Schiaffino, Computational reconstruction of the human skeletal muscle secretome, Proteins Struct. Funct. Bioinforma, vol.62, pp.776-792, 2005.

E. Boschetti and P. G. Righetti, Optimized sample treatment protocol by solid-phase peptide libraries to enrich for protein traces, Amino Acids, vol.45, pp.1431-1442, 2013.

P. M. Bossuyt, J. B. Reitsma, D. E. Bruns, C. A. Gatsonis, P. P. Glasziou et al., Standards for Reporting of Diagnostic Accuracy. 2003. The STARD Statement for Reporting Studies of Diagnostic Accuracy: Explanation and Elaboration, Ann. Intern. Med, vol.138, p.1
URL : https://hal.archives-ouvertes.fr/inserm-01327683

R. Bottinelli and C. Reggiani, Human skeletal muscle fibres: molecular and functional diversity, Prog. Biophys. Mol. Biol, vol.73, pp.195-262, 2000.

A. Boudjellal, S. Becila, G. Coulis, C. H. Herrera-mendez, A. L. Lepetit et al., Is the pH drop profile curvilinear and either monophasic or polyphasic? Consequences on the ultimate bovine meat texture, 2008.

S. Boudon and I. Cassar-malek, Dataset of proteins related to beef tenderness, V1e. deposed on the Portail Data Inrae, 2019.

J. Bouley, B. Meunier, C. Chambon, D. Smet, S. Hocquette et al., Proteomic analysis of bovine skeletal muscle hypertrophy, Proteomics, vol.5, pp.490-500, 2005.
URL : https://hal.archives-ouvertes.fr/hal-02680776

J. Bouley, B. Meunier, J. Culioli, and B. Picard, Analyse protéomique du muscle de Bovin appliquée à la recherche de marqueurs de la tendreté de la viande, Renc. Rech. Rumin, pp.87-89, 2004.

. Bourre, Apports nutritifs des viandes bovines, 2011.

M. D. Brand, The sites and topology of mitochondrial superoxide production, Exp. Gerontol, vol.45, pp.466-472, 2010.

T. Brandebourg, Growth of Muscle from the Myoblast to Whole Muscle, The Science of Meat Références bibliographiques, 2013.

. Quality and . Oxford, , pp.1-27

N. A. Bright, M. J. Gratian, and J. P. Luzio, Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells, Curr. Biol, vol.15, pp.360-365, 2005.

J. K. Brown, K. B. Lauer, E. L. Ironmonger, N. F. Inglis, T. H. Bourne et al., Shotgun Proteomics Identifies Serum Fibronectin as a Candidate Diagnostic Biomarker for Inclusion in Future Multiplex Tests for Ectopic Pregnancy, PLoS One, vol.8, p.66974, 2013.

B. Brügger and V. A. Bankaitis, Lipids and vesicular transport, Biochim. Biophys. Acta -Mol. Cell Biol. Lipids, vol.1821, p.1039, 2012.

C. Brulé, E. Dargelos, R. Diallo, A. Listrat, D. Béchet et al., Proteomic study of calpain interacting proteins during skeletal muscle aging, Biochimie, vol.92, pp.1923-1933, 2010.

C. Bruns, J. M. Mccaffery, A. J. Curwin, J. M. Duran, and V. Malhotra, Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion, J. Cell Biol, vol.195, pp.979-992, 2011.

T. M. Bunnell, B. J. Burbach, Y. Shimizu, and J. M. Ervasti, ?-Actin specifically controls cell growth, migration, and the G-actin pool, Mol. Biol. Cell, vol.22, pp.4047-4058, 2011.

D. W. Burt, The cattle genome reveals its secrets, J. Biol, vol.8, 2009.

C. A. Burtis, E. R. Ashwood, and D. E. Bruns, Tietz Textbook of Clinical Chemistry and Molecular Diagnostics, vol.2259, 2012.

S. I. Buschow, J. Liefhebber, R. Wubbolts, and W. Stoorvogel, Exosomes contain ubiquitinated proteins, Blood Cells, Mol. Dis, vol.35, pp.398-403, 2005.

D. Caccia, M. Dugo, M. Callari, and I. Bongarzone, Bioinformatics tools for secretome analysis, Biochim. Biophys. Acta -Proteins Proteomics, vol.1834, pp.2442-2453, 2013.

M. M. Campo, G. R. Nute, S. I. Hughes, M. Enser, J. D. Wood et al., Flavour perception of oxidation in beef, Meat Sci, vol.72, pp.303-311, 2006.

G. Candiano, L. Santucci, M. Bruschi, A. Petretto, C. D. Ambrosio et al., Cheek-to-cheek" urinary proteome profiling via combinatorial peptide ligand libraries: A novel, unexpected elution system, J. Proteomics, vol.75, pp.796-805, 2012.

D. I. Cantor, E. C. Nice, and M. S. Baker, Recent findings from the human proteome project: Opening the mass spectrometry toolbox to advance cancer diagnosis, surveillance and treatment, Expert Rev. Proteomics, vol.12, pp.279-293, 2015.

A. Cappiello, G. Famiglini, P. Palma, and A. Siviero, Liquid chromatography-electron ionization mass spectrometry: Fields of application and evaluation of the performance of a Direct-EI interface, Mass Spectrom. Rev, vol.24, pp.978-989, 2005.

E. Carafoli, Calcium signaling: A tale for all seasons, Proc. Natl. Acad. Sci. U. S. A, vol.99, pp.1115-1122, 2002.

K. Carayon, K. Chaoui, E. Ronzier, I. Lazar, J. Bertrand-michel et al., Proteolipidic composition of exosomes changes during reticulocyte maturation, J. Biol. Chem, vol.286, pp.34426-34439, 2011.

M. E. Carvalho, G. Gasparin, M. D. Poleti, A. F. Rosa, J. Balieiro et al., Heat shock and structural proteins associated with meat tenderness in Nellore beef cattle, a Bos indicus breed, Meat Sci, vol.96, 2014.

I. Cassar-malek, J. F. Hocquette, C. Jurie, A. Listrat, R. Jailler et al., Musclespecific metabolic, histochemical and biochemical responses to a nutritionally induced discontinuous growth path, Anim. Sci, vol.79, pp.49-59, 2004.
URL : https://hal.archives-ouvertes.fr/hal-02683168

I. Cassar-malek and B. Picard, Expression Marker-Based Strategy to Improve Beef Quality, Sci. World J, vol.2016, pp.1-11, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02629648

V. Cenni, S. Kojic, C. Capanni, G. Faulkner, and G. Lattanzi, Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies, Oxid. Med. Cell. Longev, p.7318796, 2019.

A. Chairoungdua, D. L. Smith, P. Pochard, M. Hull, and M. J. Caplan, Exosome release of ?-catenin: A novel mechanism that antagonizes Wnt signaling, J. Cell Biol, vol.190, pp.1079-1091, 2010.
URL : https://hal.archives-ouvertes.fr/hal-01134267

S. Chasserot-golaz, N. Vitale, E. Umbrecht-jenck, D. Knight, V. Gerke et al., Annexin 2 promotes the formation of lipid microdomains required for calcium-regulated exocytosis of densecore vesicles, Mol. Biol. Cell, vol.16, pp.1108-1127, 2005.
URL : https://hal.archives-ouvertes.fr/hal-00094017

Y. Y. Chen, S. Y. Lin, Y. Y. Yeh, H. H. Hsiao, C. Y. Wu et al., A modified protein precipitation procedure for efficient removal of albumin from serum, Electrophoresis, vol.26, pp.2117-2127, 2005.

Y. Cheng and J. S. Schorey, Targeting soluble proteins to exosomes using a ubiquitin tag, Biotechnol. Bioeng, vol.113, pp.1315-1324, 2016.

K. Chikuni, S. Muroya, and I. Nakajima, Myosin heavy chain isoforms expressed in bovine skeletal muscles, Meat Sci, vol.67, pp.87-94, 2004.

I. Chowdhury, B. Tharakan, and G. Bhat, Current concepts in apoptosis: The physiological suicide program revisited, Cell. Mol. Biol. Lett, vol.11, pp.506-525, 2006.

P. U. Christensen, J. Davey, and O. Nielsen, The Schizosaccharomyces pombe mam1 gene encodes an ABC transporter mediating secretion of M-factor, Mol. Gen. Genet. MGG, vol.255, pp.226-236, 1997.

A. Ciechanover, A. Orian, and A. L. Schwartz, Ubiquitin-mediated proteolysis: biological regulation via destruction, BioEssays, vol.22, pp.442-451, 2000.

K. A. Clark, A. S. Mcelhinny, M. C. Beckerle, and C. C. Gregorio, Striated Muscle Cytoarchitecture: An Intricate Web of Form and Function, Annu. Rev. Cell Dev. Biol, vol.18, pp.637-706, 2002.

B. A. Cocca, A. M. Cline, and M. Z. Radic, Blebs and Apoptotic Bodies Are B Cell Autoantigens, J. Immunol, vol.169, pp.159-166, 2002.

E. Cocucci, G. Racchetti, and J. Meldolesi, Shedding microvesicles: artefacts no more, Trends Cell Biol, vol.19, pp.43-51, 2009.

D. A. Colantonio, C. Dunkinson, D. E. Bovenkamp, V. Eyk, and J. E. , Effective removal of albumin from serum, Proteomics, vol.5, pp.3831-3835, 2005.

M. Colombo, C. Moita, G. Van-niel, J. Kowal, J. Vigneron et al., Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles, J. Cell Sci, vol.126, pp.5553-5565, 2013.

M. Colombo, G. Raposo, and C. Théry, Biogenesis, Secretion, and Intercellular Interactions of Exosomes and Other Extracellular Vesicles, Annu. Rev. Cell Dev. Biol, vol.30, pp.255-289, 2014.
URL : https://hal.archives-ouvertes.fr/inserm-02452769

D. E. Corpet, Red meat and colon cancer: Should we become vegetarians, or can we make meat safer?, Meat Sci, vol.89, pp.310-316, 2011.
URL : https://hal.archives-ouvertes.fr/hal-02802096

J. D. Crouse, B. D. Schanbacher, H. R. Cross, S. C. Seideman, and S. B. Smith, Growth and carcass traits of heifers as affected by hormonal treatment, J. Anim. Sci, vol.64, pp.1434-1440, 1987.

J. Culioli, La qualité de la viande bovine : aspects biologiques et technologiques de la gestion de la tendreté, Bull Acad Vét Fr, vol.72, pp.25-46, 1999.

V. Cunsolo, V. Muccilli, R. Saletti, and S. Foti, Mass spectrometry in food proteomics: a tutorial, J. Mass Spectrom, vol.49, pp.768-784, 2014.

A. J. Curwin, N. Brouwers, A. Y. Adell, M. Teis, D. Turacchio et al., ESCRT-III drives the final stages of CUPS maturation for unconventional protein secretion, 2016.

C. Cuvelier, J. F. Cabaraux, I. Dufrasne, A. Clinquart, J. F. Hocquette et al., Performance, slaughter characteristics and meat quality of young bulls from Belgian Blue, Limousin and Aberdeen Angus breeds fattened with a sugar-beet pulp or a cereal-based diet, Anim. Sci, vol.82, pp.125-132, 2006.
URL : https://hal.archives-ouvertes.fr/hal-02657960

R. B. D'agostino and M. Weintraub, Meta-analysis: A method for synthesizing research*, Clin. Pharmacol. Ther, vol.58, pp.605-616, 1995.

D. , A. A. Marrocco, C. Rinalducci, S. Mirasole, C. Failla et al., Chianina beef tenderness investigated through integrated Omics, J. Proteomics, vol.75, pp.4381-4398, 2012.

D. , A. A. Rinalducci, S. Marrocco, C. Zolla, V. Napolitano et al., Love me tender: An Omics window on the bovine meat tenderness network, J. Proteomics, vol.75, pp.4360-4380, 2012.

A. D'alessandro and L. Zolla, Foodomics to investigate meat tenderness, TrAC Trends Anal. Chem, vol.52, pp.47-53, 2013.

A. D'alessandro and L. Zolla, Meat science: From proteomics to integrated omics towards system biology, J. Proteomics, vol.78, pp.558-577, 2013.

N. N. Danial and S. J. Korsmeyer, Cell Death: Critical Control Points. Cell, vol.116, pp.205-219, 2004.

M. Dean and T. Annilo, EVOLUTION OF THE ATP-BINDING CASSETTE (ABC) TRANSPORTER SUPERFAMILY IN VERTEBRATES, Annu. Rev. Genomics Hum. Genet, vol.6, pp.123-142, 2005.

P. Dean and D. H. Watson, Protein purification using immobilised triazine dyes, J. Chromatogr. A, vol.165, pp.301-319, 1979.

, Décret relatif à la protection des animaux utilisés à des fins scientifiques, p.2199, 2013.

R. Delerins and P. Raffard, Comprendre la consommation de viande : aujourd'hui et demain, Comprendre la consommation de viande : aujourd'hui, 2017.

M. Delosière, J. Pires, L. Bernard, I. Cassar-malek, and M. Bonnet, Milk proteome from in silico data aggregation allows the identification of putative biomarkers of negative energy balance in dairy cows, Sci. Rep, vol.9, p.9718, 2019.

A. Dementiev, M. Simonovic, K. Volz, and P. Gettins, Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases, J. Biol. Chem, vol.278, pp.37881-37888, 2003.

, Democratizing proteomics data, Nat. Biotechnol, vol.25, p.262, 2007.

A. Denizli and E. Pi?kin, Dye-ligand affinity systems, J. Biochem. Biophys. Methods, vol.49, pp.391-416, 2001.

S. Desagher, A. Osen-sand, A. Nichols, R. Eskes, S. Montessuit et al., Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis, J. Cell Biol, vol.144, pp.891-901, 1999.

G. Desdín-micó and M. Mittelbrunn, Role of exosomes in the protection of cellular homeostasis, Cell Adhes. Migr, vol.11, pp.127-134, 2017.

J. Diamond, Evolution, consequences and future of plant and animal domestication, Nature, vol.418, pp.700-707, 2002.

Z. Dlamini, Z. Mbita, and M. Zungu, Genealogy, expression, and molecular mechanisms in apoptosis, Pharmacol. Ther, vol.101, pp.1-15, 2004.

A. Dubost, D. Micol, B. Picard, C. Lethias, D. Andueza et al., Structural and biochemical characteristics of bovine intramuscular connective tissue and beef quality, Meat Sci, vol.95, pp.555-561, 2013.
URL : https://hal.archives-ouvertes.fr/hal-02646937

B. Dujon and G. Pelletier, Trajectoires de la génétique, 2019.

N. Dupont, S. Jiang, M. Pilli, W. Ornatowski, D. Bhattacharya et al., Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1?, EMBO J, vol.30, pp.4701-4711, 2011.

J. M. Duran, C. Anjard, C. Stefan, W. F. Loomis, and V. Malhotra, Unconventional secretion of Acb1 is mediated by autophagosomes, J. Cell Biol, vol.188, pp.527-563, 2010.

M. Durcin, A. Fleury, E. Taillebois, G. Hilairet, Z. Krupova et al., Characterisation of adipocyte-derived extracellular vesicle subtypes identifies distinct protein and lipid signatures for large and small extracellular vesicles, J. Extracell. Vesicles, vol.6, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01606680

D. Dutaud, A. L. Sentandreu, M. A. Ouali, and A. , Bovine muscle 20S proteasome: I. Simple purification procedure and enzymatic characterization in relation with postmortem conditions, Meat Sci, vol.74, pp.327-336, 2006.

A. D. Ebert, M. Laußmann, S. Wegehingel, L. Kaderali, H. Erfle et al., Tec-Kinase-Mediated Phosphorylation of Fibroblast Growth Factor 2 is Essential for Unconventional Secretion, Traffic, vol.11, pp.813-826, 2010.

S. Elmore, Apoptosis: A Review of Programmed Cell Death, Toxicol. Pathol, vol.35, pp.495-516, 2007.

C. G. Elsik, R. L. Tellam, K. C. Worley, R. A. Gibbs, D. M. Muzny et al., , vol.324, pp.522-528, 2009.

P. Ertbjerg and E. Puolanne, Muscle structure, sarcomere length and influences on meat quality: A review, Meat Sci, vol.132, pp.139-152, 2017.

J. M. Escola, M. J. Kleijmeer, W. Stoorvogel, J. M. Griffith, Y. O. Geuze et al., Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes, J. Biol. Chem, vol.273, pp.20121-20127, 1998.

C. Evrat-georgel, Bibliographie critique des méthodes instrumentales de mesure de la tendreté de la viande bovine, Département technique d'Elevage et Santé SQ des VP, 2008.

C. M. Fader, D. G. Sánchez, M. B. Mestre, and M. I. Colombo, TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways, Biochim. Biophys. Acta -Mol. Cell Res, vol.1793, pp.1901-1916, 2009.

C. M. Fader, A. Savina, D. Sánchez, and M. I. Colombo, Exosome secretion and red cell maturation: Exploring molecular components involved in the docking and fusion of multivesicular bodies in K562 cells, Blood Cells, Mol. Dis, vol.35, pp.153-157, 2005.

T. N. Feinstein and A. D. Linstedt, GRASP55 Regulates Golgi Ribbon Formation, Mol. Biol. Cell, vol.19, pp.2696-2707, 2008.

C. Fernández, H. M. Santos, C. Ruíz-romero, F. J. Blanco, and J. L. Capelo-martínez, A comparison of depletion versus equalization for reducing high-abundance proteins in human serum, Electrophoresis, vol.32, pp.2966-2974, 2011.

S. Ferro-novick and N. Brose, Physiology or medicine: Traffic control system within cells, Nature, vol.504, p.98, 2013.

S. W. Fesik and Y. Shi, STRUCTURAL BIOLOGY: Controlling the Caspases. Science (80-. ), vol.294, pp.1477-1478, 2001.

A. Fidzia?ska, A. Kami?ska, and Z. Glinka, Ultrastructural differences between muscle cell necrosis and apoptosis, Neuropatol. Pol, vol.29, pp.19-28, 1991.

C. Fischer and R. Hamm, Biochemical studies on fast glycolysing bovine muscle, Meat Sci, vol.4, pp.41-49, 1980.

A. B. Fisher, Peroxiredoxin 6: A Bifunctional Enzyme with Glutathione Peroxidase and Phospholipase A 2 Activities, Antioxid. Redox Signal, vol.15, pp.831-844, 2011.

L. Fonseca, D. Gimenez, S. Silva, D. B. Barthelson, R. Baldi et al., Differences in global gene expression in muscle tissue of Nellore cattle with divergent meat tenderness, BMC Genomics, vol.18, p.945, 2017.

L. Fontanesi, R. Davoli, N. Costa, L. Scotti, E. Russo et al., Study of candidate genes for glycolytic potential of porcine skeletal muscle: identification and analysis of mutations, linkage and physical mapping and association with meat quality traits in pigs, Cytogenet. Genome Res, vol.102, pp.145-151, 2003.

A. Forterre, A. Jalabert, E. Berger, M. Baudet, K. Chikh et al., Proteomic Analysis of C2C12 Myoblast and Myotube Exosome-Like Vesicles: A New Paradigm for Myoblast-Myotube Cross Talk?, PLoS One, vol.9, p.84153, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01859453

S. J. Franco and A. Huttenlocher, Regulating cell migration: calpains make the cut, J. Cell Sci, vol.118, pp.3829-3867, 2005.

P. Fuentes-priors and G. S. Salvesen, The protein structures that shape caspase activity, specificity, activation and inhibition, Biochem. J, vol.384, pp.201-232, 2004.

C. E. Futter and I. J. White, Annexins and endocytosis. Traffic, vol.8, pp.951-958, 2007.

M. Gagaoua, Y. Boudida, S. Becila, B. Picard, A. Boudjellal et al., New Caspases' inhibitors belonging to the serpin superfamily: A novel key control point of apoptosis in mammalian tissues, Adv. Biosci. Biotechnol, vol.03, pp.740-750, 2012.
URL : https://hal.archives-ouvertes.fr/hal-02646139

M. Gagaoua, A. Boudjellal, S. Becila, Y. Boudida, C. Herrera-mendez et al., Apoptosis regulation in postmortem muscle: cross-class inhibition of caspases by two bovine serpins | Request PDF, Proceedings of the 59th International Congress of Meat Science and Technology, 2013.

M. Gagaoua, C. Terlouw, E. M. Boudjellal, A. Picard, and B. , Coherent correlation networks among protein biomarkers of beef tenderness: What they reveal, J. Proteomics, vol.128, pp.365-374, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02641553

M. Gagaoua, S. Couvreur, L. Bec, G. Aminot, G. Picard et al., Associations among Protein Biomarkers and pH and Color Traits in Longissimus thoracis and Rectus abdominis Muscles in Protected Designation of Origin Maine-Anjou Cull Cows, J. Agric. Food Chem, vol.65, pp.3569-3580, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01604179

M. Gagaoua, K. Hafid, Y. Boudida, S. Becila, A. Ouali et al., Caspases and Thrombin Activity Regulation by Specific Serpin Inhibitors in Bovine Skeletal Muscle. Appl. Biochem. Biotechnol, vol.177, pp.279-303, 2015.

M. Gagaoua, C. Terlouw, D. Micol, A. Boudjellal, J. Hocquette et al., Proteomic biomarkers of meat colour of blonde d'aquitaine young bulls: towards a better comprehension of the biological mechanisms. 61th Int, Int. Congr. Meat Sci. Technol. (ICoMST), vol.61, pp.93-93, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02742906

M. Gagaoua, C. Terlouw, and B. Picard, The associations between proteomic biomarkers and beef tenderness depend on the end-point cooking temperature, the country origin of the panelists and breed, Meat Sci, vol.157, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02629415

M. Gagaoua, E. Terlouw, D. Micol, A. Boudjellal, J. Hocquette et al., Understanding Early Post-Mortem Biochemical Processes Underlying Meat Color and pH Decline in the Longissimus thoracis Muscle of Young Blond d'Aquitaine Bulls Using Protein Biomarkers, J. Agric. Food Chem, vol.63, pp.6799-6809, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01191442

M. Gagaoua, E. Terlouw, D. Micol, J. Hocquette, A. P. Moloney et al., Sensory quality of meat from eight different types of cattle in relation with their biochemical characteristics, J. Integr. Agric, vol.15, pp.1550-1563, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02638038

L. Gam, Breast cancer and protein biomarkers, World J. Exp. Med, vol.2, p.0, 2012.

S. Garcia, P. A. Baldasso, P. C. Guest, and D. Martins-de-souza, Depletion of highly abundant proteins of the human blood plasma: Applications in proteomics studies of psychiatric disorders, Methods in Molecular Biology, pp.195-204, 2017.

D. Gassart, A. Géminard, C. Février, B. Raposo, G. Vidal et al., Lipid raft-associated protein sorting in exosomes, Blood, vol.102, pp.4336-4344, 2003.

P. Gatellier, Y. Mercier, H. Juin, and M. Renerre, Effect of finishing mode (pasture-or mixed-diet) on lipid composition, colour stability and lipid oxidation in meat from Charolais cattle, Meat Sci, vol.69, pp.175-186, 2005.
URL : https://hal.archives-ouvertes.fr/hal-02682482

Y. Ge, M. P. Molloy, J. S. Chamberlain, and P. C. Andrews, Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity, Proteomics, vol.3, pp.1895-1903, 2003.

R. Geay, Importance de la variabilité génétique et du mode d'élevage des bovins sur les caractéristiques musculaires et les qualités organoleptiques de leurs viandes, Renc. Rech. Rumin, pp.177-182, 1994.

Y. Geay, D. Bauchart, J. F. Hocquette, and J. Culioli, Valeur di??t??tique et qualit??s sensorielles des viandes de ruminants. Incidence de l'alimentation des animaux, Prod. Anim, vol.15, pp.37-52, 2002.

H. Y. Gee, S. H. Noh, B. L. Tang, K. H. Kim, and M. G. Lee, Rescue of ?F508-CFTR Trafficking via a GRASP-Dependent Unconventional Secretion Pathway, Cell, vol.146, pp.746-760, 2011.

V. Gene and . Glass, Meta-Analysis at 25, 2000.

V. Gerke, C. E. Creutz, and S. E. Moss, Annexins: Linking Ca2+ signalling to membrane dynamics, Nat. Rev. Mol. Cell Biol, vol.6, pp.449-461, 2005.

V. Gerke and S. E. Moss, Annexins: From structure to function, Physiol. Rev, vol.82, pp.331-371, 2002.

D. E. Gerrard, S. J. Jones, E. D. Aberle, R. P. Lemenager, M. A. Diekman et al., Collagen Stability, Testosterone Secretion and Meat Tenderness in Growing Bulls and Steers, J. Anim. Sci, vol.65, pp.1236-1242, 1987.

P. Gettins, Serpin Structure, Mechanism, and Function, 2002.

P. E. Geyer, L. M. Holdt, D. Teupser, and M. Mann, Revisiting biomarker discovery by plasma proteomics, Mol. Syst. Biol, vol.13, p.942, 2017.

P. E. Geyer, N. A. Kulak, G. Pichler, L. M. Holdt, D. Teupser et al., Plasma Proteome Profiling to Assess Human Health and Disease, Cell Syst, vol.2, pp.185-195, 2016.

D. Girolamo, F. Righetti, P. G. Soste, M. Feng, Y. Picotti et al., Reproducibility of combinatorial peptide ligand libraries for proteome capture evaluated by selected reaction monitoring, J. Proteomics, vol.89, pp.215-226, 2013.

B. Glancy and R. S. Balaban, Role of Mitochondrial Ca 2+ in the Regulation of Cellular Energetics, Biochemistry, vol.51, pp.2959-2973, 2012.

M. Gobert, D. Gruffat, M. Habeanu, E. Parafita, D. Bauchart et al., Plant extracts combined with vitamin E in PUFA-rich diets of cull cows protect processed beef against lipid oxidation, Meat Sci, vol.85, pp.676-683, 2010.
URL : https://hal.archives-ouvertes.fr/hal-02665213

I. Göktürk, E. Tamahkar, F. Y?lmaz, and A. Denizli, Protein depletion with bacterial cellulose nanofibers, J. Chromatogr. B Anal. Technol. Biomed. Life Sci, vol.1099, pp.1-9, 2018.

D. E. Goll, V. F. Thompson, H. Li, W. Wei, and J. Cong, The Calpain System, Physiol. Rev, vol.83, pp.731-801, 2003.
URL : https://hal.archives-ouvertes.fr/hal-02836662

C. J. Gomes-lima, A. Maciel, O. Andrade-m-de, V. S. Cunha, . Da et al., Thyroxine-binding globulin deficiency due to a novel SERPINA7 mutation: Clinical characterization, analysis of X-chromosome inactivation pattern and protein structural modeling, Gene, vol.666, pp.58-63, 2018.

. Van-der-goot, . Fg, and J. Gruenberg, Intra-endosomal membrane traffic, Trends Cell Biol, vol.16, pp.514-521, 2006.

A. M. Gordon, E. Homsher, and M. Regnier, Regulation of Contraction in Striated Muscle, Physiol. Rev, vol.80, pp.853-924, 2000.

A. Görg, G. Boguth, A. Köpf, G. Reil, H. Parlar et al., Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels, Proteomics, vol.2, pp.1652-1657, 2002.

A. Görg, W. Weiss, and M. J. Dunn, Current two-dimensional electrophoresis technology for proteomics, Proteomics, vol.4, pp.3665-3685, 2004.

T. Gotoh, A. E. Teuscher, F. Kawabata, K. Sakashita, K. Iwamoto et al., Differences in muscle and fat accretion in Japanese Black and European cattle, Meat Sci, vol.82, pp.300-308, 2009.

M. M. Gottesman, T. Fojo, and S. E. Bates, Multidrug resistance in cancer: role of ATP-dependent transporters, Nat. Rev. Cancer, vol.2, pp.48-58, 2002.

V. Grabe?, M. Kathri, V. Phung, K. M. Moe, E. Slinde et al., Protein expression and oxygen consumption rate of early postmortem mitochondria relate to meat tenderness1, J. Anim. Sci, vol.93, pp.1967-1979, 2015.

A. G. Grieve and C. Rabouille, Golgi bypass: skirting around the heart of classical secretion, Cold Spring Harb. Perspect. Biol, vol.3, p.5298, 2011.

L. Grobet, R. Martin, L. J. Poncelet, D. Pirottin, D. Brouwers et al., A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle, Nat. Genet, vol.17, pp.71-74, 1997.
URL : https://hal.archives-ouvertes.fr/hal-02686447

K. G. Grunert, L. Bredahl, and K. Brunsø, Consumer perception of meat quality and implications for product development in the meat sector-a review, Meat Sci, vol.66, pp.259-272, 2004.

L. Guerrier, P. G. Righetti, and E. Boschetti, Reduction of dynamic protein concentration range of biological extracts for the discovery of low-abundance proteins by means of hexapeptide ligand library, Nat. Protoc, vol.3, pp.883-890, 2008.

M. Guescini, D. Guidolin, L. Vallorani, L. Casadei, A. M. Gioacchini et al., C2C12 myoblasts release micro-vesicles containing mtDNA and proteins involved in signal transduction, Exp. Cell Res, vol.316, pp.1977-1984, 2010.

N. Guillemin, M. Bonnet, C. Jurie, and B. Picard, Functional analysis of beef tenderness, J. Proteomics, vol.75, pp.352-365, 2011.
URL : https://hal.archives-ouvertes.fr/hal-02646580

N. Guillemin, I. Cassar-malek, J. F. Hocquette, C. Jurie, D. Micol et al., La maîtrise de la tendreté de la viande bovine : Identification de marqueurs biologiques, Prod. Anim, vol.22, pp.331-344, 2009.

N. Guillemin, C. Malek, I. Hocquette, J. Jurie, C. Micol et al., La maîtrise de la tendreté de la viande bovine : identification de marqueurs biologiques, pp.331-344, 2009.

R. L. Gundry, Q. Fu, C. A. Jelinek, J. E. Van-eyk, and R. J. Cotter, Investigation of an albumin-enriched fraction of human serum and its albuminome, Proteomics -Clin. Appl, vol.1, pp.73-88, 2007.

B. Guo, Z. K. Zhang, C. Liang, J. Li, J. Liu et al., Molecular Communication from Skeletal Muscle to Bone: A Review for Muscle-Derived Myokines Regulating Bone Metabolism, Calcif. Tissue Int, vol.100, pp.184-192, 2017.

S. Gupta, Molecular signaling in death receptor and mitochondrial pathways of apoptosis (Review), 2003.

, Int. J. Oncol, vol.22, pp.15-20

J. Gutteridge, Biological origin of free radicals, and mechanisms of antioxidant protection, Chem. Biol. Interact, vol.91, pp.133-140, 1994.

S. P. Gygi, G. L. Corthals, Y. Zhang, Y. Rochon, and R. Aebersold, Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology, Proc. Natl. Acad. Sci, vol.97, pp.9390-9395, 2000.

M. Hamdan, Biomarkers: Analytical Techniques for Discovery, 2007.

R. M. Hamill, J. Mcbryan, C. Mcgee, A. M. Mullen, T. Sweeney et al., Functional analysis of muscle gene expression profiles associated with tenderness and intramuscular fat content in pork, Meat Sci, vol.92, pp.440-450, 2012.

S. Hansen, M. Therkildsen, and D. V. Byrne, Effects of a compensatory growth strategy on sensory and physical properties of meat from young bulls, Meat Sci, vol.74, pp.628-643, 2006.

?. Hanzelková, J. Simeonovová, D. Hampel, A. Dufek, and J. ?ubrt, The effect of breed, sex and aging time on tenderness of beef meat, Acta Vet. Brno, vol.80, pp.191-196, 2011.

G. S. Harper, P. G. Allingham, L. Feuvre, and R. P. , Changes in connective tissue of M. semitendinosus as a response to different growth paths in steers, Meat Sci, vol.53, pp.107-121, 1999.

. Hébel, Evolution de la consommation de viande en France: les nouvelles données de l'enquête "comportements et consommations alimentaires en france" (CCAF), 2012.

W. M. Henne, N. J. Buchkovich, and S. D. Emr, The ESCRT Pathway, Dev. Cell, vol.21, pp.77-91, 2011.

W. M. Henne, H. Stenmark, and S. D. Emr, Molecular mechanisms of the membrane sculpting ESCRT pathway, Cold Spring Harb. Perspect. Biol, vol.5, 2013.

A. K. Henning, D. Albrecht, K. Riedel, T. C. Mettenleiter, and A. Karger, An alternative method for serum protein depletion/enrichment by precipitation at mildly acidic pH values and low ionic strength, Proteomics, vol.15, pp.1935-1940, 2015.

J. Henningsen, K. Rigbolt, B. Blagoev, B. K. Pedersen, and I. Kratchmarova, Dynamics of the Skeletal Muscle Secretome during Myoblast Differentiation, Mol. Cell. Proteomics, vol.9, pp.2482-2496, 2010.

T. Henriksen, C. Green, K. Pedersen, and B. , Myokines in Myogenesis and Health: Ingenta Connect, Recent Pat. Biotechnol, vol.6, issue.5, pp.167-171, 2012.

C. H. Herrera-mendez, S. Becila, X. Blanchet, P. Pelissier, D. Delourme et al., Inhibition of human initiator caspase 8 and effector caspase 3 by cross-class inhibitory bovSERPINA3-1 and A3-3, FEBS Lett, vol.583, pp.2743-2748, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02661888

C. H. Herrera-mendez, L. Brémaud, G. Coulis, P. Pélissier, M. A. Sentandreu et al., Purification of the skeletal muscle protein Endopin 1B and characterization of the genes encoding Endopin 1A and 1B isoforms, FEBS Lett, vol.580, pp.3477-3484, 2006.
URL : https://hal.archives-ouvertes.fr/hal-01211871

N. Herrera, E. Kunze, K. Domenech-perez, F. Ribeiro, M. Chao et al., The Relationship between Marbling, Superoxide Dismutase, and Beef Tenderness, Meat Muscle Biol, vol.1, pp.169-169, 2017.

N. P. Hessvik, A. Øverbye, A. Brech, M. L. Torgersen, I. S. Jakobsen et al., PIKfyve inhibition increases exosome release and induces secretory autophagy, Cell. Mol. Life Sci, vol.73, pp.4717-4737, 2016.

T. Hoch, C. Begon, C. Malek, I. Picard, B. Savary-auzeloux et al., , 2003.

J. Hocquette, I. Cassar-malek, A. Listrat, C. Jurie, R. Jailler et al., Evolution des recherches sur le muscle des bovins et la qualité sensorielle de leur viande, 2005.

J. F. Hocquette, I. Ortigues-marty, D. Pethick, P. Herpin, and X. Fernandez, Nutritional and hormonal regulation of energy metabolism in skeletal muscles of meat-producing animals, Livest. Prod. Sci, vol.56, pp.115-143, 1998.
URL : https://hal.archives-ouvertes.fr/hal-02769758

J. Holdstock, J. L. Aalhus, B. A. Uttaro, Ó. López-campos, I. L. Larsen et al., The impact of ultimate pH on muscle characteristics and sensory attributes of the longissimus thoracis within the dark cutting (Canada B4) beef carcass grade, Meat Sci, vol.98, pp.842-849, 2014.

L. Holmgren, A. Szeles, E. Rajnavölgyi, J. Folkman, G. Klein et al., Apoptotic_body_EBV-transfer_Blood1999, vol.93, pp.3956-3963, 1999.

K. Honda, Y. Hayashida, T. Umaki, T. Okusaka, T. Kosuge et al., Possible detection of pancreatic cancer by plasma protein profiling, Cancer Res, vol.65, pp.10613-10622, 2005.

G. L. Hortin and D. Sviridov, The dynamic range problem in the analysis of the plasma proteome, J. Proteomics, vol.73, pp.629-636, 2010.

P. Horvatovich, L. Franke, and R. Bischoff, Proteomic Studies Related to Genetic Determinants of Variability in Protein Concentrations, J. Proteome Res, vol.13, pp.5-14, 2014.

D. Hoshino, K. C. Kirkbride, K. Costello, E. S. Clark, S. Sinha et al., Exosome secretion is enhanced by invadopodia and drives invasive behavior, Cell Rep, vol.5, pp.1159-1168, 2013.

R. S. Hotchkiss, A. Strasser, J. E. Mcdunn, and P. E. Swanson, Cell death. N. Engl. J. Med, vol.361, pp.1570-83, 2009.

M. Hristov, W. Erl, S. Linder, and P. C. Weber, Apoptotic bodies from endothelial cells enhance the number and initiate the differentiation of human endothelial progenitor cells in vitro, Blood, vol.104, pp.2761-2766, 2004.

I. Hrynaszkiewicz, A call for BMC Research Notes contributions promoting best practice in data standardization, sharing and publication, BMC Res. Notes, vol.3, p.235, 2010.

C. Hsu, Y. Morohashi, S. I. Yoshimura, N. Manrique-hoyos, J. Sy et al., Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A-C, J. Cell Biol, vol.189, pp.223-232, 2010.

G. Hu, K. M. Drescher, and X. M. Chen, Exosomal miRNAs: Biological properties and therapeutic potential, Front. Genet, vol.3, 2012.

E. Huff-lonergan and S. M. Lonergan, Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes, Meat Sci, vol.71, pp.194-204, 2005.

E. Huff-lonergan, W. Zhang, and S. M. Lonergan, Biochemistry of postmortem muscle -Lessons on mechanisms of meat tenderization, Meat Sci, vol.86, pp.184-195, 2010.

B. Hugel, M. C. Martínez, C. Kunzelmann, and J. M. Freyssinet, Membrane microparticles: Two sides of the coin, Physiology, vol.20, pp.22-27, 2005.

J. A. Huntington, Serpin structure, function and dysfunction, J. Thromb. Haemost, vol.9, pp.26-34, 2011.

J. A. Huntington and R. W. Carrell, The Serpins: Nature's Molecular Mousetraps, Sci. Prog, vol.84, pp.125-136, 2001.

J. A. Huntington, R. J. Read, and R. W. Carrell, Structure of a serpin-protease complex shows inhibition by deformation, Nature, vol.407, pp.923-926, 2000.

J. Huotari and A. Helenius, Endosome maturation, EMBO J, vol.30, pp.3481-500, 2011.

S. N. Hurwitz, M. M. Conlon, M. A. Rider, N. C. Brownstein, and D. G. Meckes, Nanoparticle analysis sheds budding insights into genetic drivers of extracellular vesicle biogenesis, J. Extracell. Vesicles, vol.5, p.31295, 2016.

R. J. Isfort, F. Wang, K. D. Greis, Y. Sun, T. W. Keough et al., Proteomic analysis of rat soleus muscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy, Proteomics, vol.2, pp.543-550, 2002.

V. Jesenberger and S. Jentsch, Deadly encounter: ubiquitin meets apoptosis, Nat. Rev. Mol. Cell Biol, vol.3, pp.112-121, 2002.

X. Jia, M. Ekman, H. Grove, E. M. Faergestad, L. Aass et al., Proteome Changes in Bovine Longissimus Thoracis Muscle During the Early Postmortem Storage Period, J. Proteome Res, vol.6, pp.2720-2731, 2007.

X. Jia, K. I. Hildrum, F. Westad, E. Kummen, L. Aass et al., Changes in enzymes associated with energy metabolism during the early post mortem period in Longissimus thoracis bovine muscle analyzed by proteomics, J. Proteome Res, vol.5, pp.1763-1769, 2006.

X. Jia, K. Hollung, M. Therkildsen, K. I. Hildrum, and E. Bendixen, Proteome analysis of early postmortem changes in two bovine muscle types:M. longissimus dorsi andM. semitendinosis, Proteomics, vol.6, pp.936-944, 2006.

S. Jiang, Y. Liu, Z. Shen, B. Zhou, and Q. W. Shen, Acetylome profiling reveals extensive involvement of lysine acetylation in the conversion of muscle to meat, J. Proteomics, vol.205, p.103412, 2019.

S. T. Jiang, Contribution of muscle proteinases to meat tenderization, Proc. Natl. Sci. Counc. Repub. China. B, vol.22, pp.97-107, 1998.

B. C. Johnston, D. Zeraatkar, M. A. Han, R. Vernooij, C. Valli et al., Unprocessed Red Meat and Processed Meat Consumption: Dietary Guideline Recommendations From the Nutritional Recommendations (NutriRECS) Consortium, Ann. Intern. Med, 2019.

R. M. Johnstone, M. Adam, J. R. Hammond, L. Orr, and C. Turbide, Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes), J. Biol. Chem, vol.262, pp.9412-9432, 1987.

R. M. Johnstone, A. Mathew, A. B. Mason, and K. Teng, Exosome formation during maturation of mammalian and avian reticulocytes: Evidence that exosome release is a major route for externalization of obsolete membrane proteins, J. Cell. Physiol, vol.147, pp.27-36, 1991.

S. J. Jones, D. L. Starkey, C. R. Calkins, and J. D. Crouse, Myofibrillar protein turnover in feed-restricted and realimented beef cattle, J. Anim. Sci, vol.68, p.2707, 1990.

D. Jong, O. G. , V. Balkom, B. Gremmels, H. Verhaar et al., Exosomes from hypoxic endothelial cells have increased collagen crosslinking activity through up-regulation of lysyl oxidase-like 2, J. Cell. Mol. Med, vol.20, pp.342-350, 2016.

P. Joseph, S. P. Suman, G. Rentfrow, S. Li, and C. M. Beach, Proteomics of Muscle-Specific Beef Color Stability, J. Agric. Food Chem, vol.60, pp.3196-3203, 2012.

J. Jung, J. Kim, S. H. Roh, I. Jun, R. D. Sampson et al., The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion, Nat. Commun, vol.7, p.11386, 2016.

C. Jurie, J. Martin, A. Listrat, R. Jailler, J. Culioli et al., Effects of age and breed of beef bulls on growth parameters, carcass and muscle characteristics, Anim. Sci, vol.80, pp.257-263, 2005.
URL : https://hal.archives-ouvertes.fr/hal-02680500

C. Jurie, I. Ortigues-marty, B. Picard, D. Micol, and J. F. Hocquette, The separate effects of the nature of diet and grazing mobility on metabolic potential of muscles from Charolais steers, Livest. Sci, vol.104, pp.182-192, 2006.
URL : https://hal.archives-ouvertes.fr/hal-02659289

C. Jurie, B. Picard, and Y. Geay, Changes in the metabolic and contractile characteristics of muscle in male cattle between 10 and 16 months of age, Histochem. J, vol.31, pp.117-122, 1999.
URL : https://hal.archives-ouvertes.fr/hal-02687290

C. Jurie, J. Robelin, B. Picard, and Y. Geay, Post-natal changes in the biological characteristics of Semitendinosus muscle in male Limousin cattle, Meat Sci, vol.41, pp.125-135, 1995.
URL : https://hal.archives-ouvertes.fr/hal-02711835

T. Kajimoto, T. Okada, S. Miya, L. Zhang, and S. I. Nakamura, Ongoing activation of sphingosine 1-phosphate receptors mediates maturation of exosomal multivesicular endosomes, Nat. Commun, vol.4, 2013.

S. Keerthikumar, A catalogue of human secreted proteins and its implications, AIMS Biophys, vol.3, pp.563-570, 2016.

R. Kelly, Pathways of protein secretion in eukaryotes. Science (80-. ), vol.230, pp.25-32, 1985.

C. M. Kemp and T. Parr, Advances in apoptotic mediated proteolysis in meat tenderisation, Meat Sci, vol.92, pp.252-259, 2012.

C. M. Kemp and T. L. Wheeler, Effects of manipulation of the caspase system on myofibrillar protein degradation in vitro12, J. Anim. Sci, vol.89, pp.3262-3271, 2011.

J. F. Kerr, A. H. Wyllie, and A. R. Currie, Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics, Br. J. Cancer, vol.26, pp.239-57, 1972.

J. Kerry, ). Microbiologist, and D. Ledward, Improving the sensory and nutritional quality of fresh meat, vol.664, 2009.

P. Kharaziha, S. Ceder, Q. Li, and T. Panaretakis, Tumor cell-derived exosomes: A message in a bottle, Biochim. Biophys. Acta -Rev. Cancer, vol.1826, pp.103-111, 2012.

G. Kim, Y. , H. Jeong, and J. , Comparison of Characteristics of Myosin Heavy Chain-based Fiber and Meat Quality among Four Bovine Skeletal Muscles, Korean J. food Sci. Anim. Resour, vol.36, pp.819-828, 2016.

J. Kim, S. H. Noh, H. Piao, D. H. Kim, K. Kim et al., Monomerization and ER Relocalization of GRASP Is a Requisite for Unconventional Secretion of CFTR, Traffic, vol.17, pp.733-753, 2016.

N. K. Kim, S. Cho, S. H. Lee, H. R. Park, C. S. Lee et al., Proteins in longissimus muscle of Korean native cattle and their relationship to meat quality, Meat Sci, vol.80, pp.1068-1073, 2008.

S. F. Kingsmore, Multiplexed protein measurement: technologies and applications of protein and antibody arrays, Nat. Rev. Drug Discov, vol.5, pp.310-321, 2006.

M. Kiran, B. M. Naveena, K. S. Reddy, M. Shashikumar, V. R. Reddy et al., Muscle-Specific Variation in Buffalo ( B ubalus bubalis ) Meat Texture: Biochemical, Ultrastructural and Proteome Characterization, J. Texture Stud, vol.46, pp.254-261, 2015.

Y. Kitamura, R. Usami, S. Ichihara, H. Kida, M. Satoh et al., Plasma protein profiling for potential biomarkers in the early diagnosis of Alzheimer's disease, Neurol. Res, vol.39, pp.231-238, 2017.

R. E. Klont, V. M. Barnier, A. Van-dijk, F. J. Smulders, A. H. Hoving-bolink et al., Effects of rate of pH fall, time of deboning, aging period, and their interaction on veal quality characteristics, J. Anim. Sci, vol.78, p.1845, 2000.

S. Kojic, E. Medeot, E. Guccione, H. Krmac, Z. I. Martinelli et al., The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle, J. Mol. Biol, vol.339, pp.313-325, 2004.

S. Kojic, D. Radojkovic, and G. Faulkner, Muscle ankyrin repeat proteins: Their role in striated muscle function in health and disease, Crit. Rev. Clin. Lab. Sci, vol.48, pp.269-294, 2011.

M. Koohmaraie, M. P. Kent, S. D. Shackelford, E. Veiseth, and T. L. Wheeler, Meat tenderness and muscle growth: is there any relationship?, Meat Sci, vol.62, pp.345-352, 2002.

E. E. Kooijman, V. Chupin, B. De-kruijff, and K. Burger, Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid, Traffic, vol.4, pp.162-174, 2003.

J. Kowal, G. Arras, M. Colombo, M. Jouve, J. P. Morath et al., Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes, Proc. Natl. Acad. Sci. U. S. A, vol.113, pp.968-977, 2016.
URL : https://hal.archives-ouvertes.fr/inserm-02450678

G. Kroemer, L. Galluzzi, P. Vandenabeele, J. Abrams, E. S. Alnemri et al., Classification of cell death: recommendations of the Nomenclature Committee on Cell Death, Cell Death Differ, vol.16, pp.3-11, 2009.
URL : https://hal.archives-ouvertes.fr/hal-00407686

G. Kroemer and J. C. Reed, Mitochondrial control of cell death, Nat. Med, vol.6, pp.513-519, 2000.

N. T. Ktistakis and S. A. Tooze, Digesting the Expanding Mechanisms of Autophagy, Trends Cell Biol, vol.26, pp.624-635, 2016.

A. Lakkaraju and E. Rodriguez-boulan, Itinerant exosomes: emerging roles in cell and tissue polarity, Trends Cell Biol, vol.18, pp.199-209, 2008.

R. Lametsch, A. Karlsson, K. Rosenvold, H. J. Andersen, P. Roepstorff et al., Postmortem Proteome Changes of Porcine Muscle Related to Tenderness, J. Agric. Food Chem, vol.51, pp.6992-6997, 2003.

R. Lametsch, P. Roepstorff, H. Møller, and E. Bendixen, Identification of myofibrillar substrates for ?calpain, Meat Sci, vol.68, pp.515-521, 2004.

J. Lan, N. Galindo, A. Doecke, J. Fowler, C. Martins et al., Systematic Evaluation of the Use of Human Plasma and Serum for Mass-Spectrometry-Based Shotgun Proteomics, J. Proteome Res, vol.17, pp.1426-1435, 2018.

M. Laporte, La viande voit rouge, 2012.

C. Larzul, L. Lefaucheur, P. Ecolan, J. Gogué, A. Talmant et al., Phenotypic and genetic parameters for longissimus muscle fiber characteristics in relation to growth, carcass, and meat quality traits in large white pigs, J. Anim. Sci, vol.75, p.3126, 1997.
URL : https://hal.archives-ouvertes.fr/hal-02685236

S. Lata, G. Schoehn, J. Solomons, R. Pires, H. G. Göttlinger et al., Structure and function of ESCRT-III, Biochem. Soc. Trans, vol.37, pp.156-160, 2009.

E. Laville, T. Sayd, M. Morzel, S. Blinet, C. Chambon et al., Proteome Changes during Meat Aging in Tough and Tender Beef Suggest the Importance of Apoptosis and Protein Solubility for Beef Aging and Tenderization, J. Agric. Food Chem, vol.57, pp.10755-10764, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02663751

R. Law, Q. Zhang, S. Mcgowan, A. M. Buckle, G. A. Silverman et al., An overview of the serpin superfamily, Genome Biol, vol.7, p.216, 2006.

D. A. Lawrence, D. Ginsburg, D. E. Day, M. B. Berkenpas, I. M. Verhamme et al., Serpin-protease complexes are trapped as stable acyl-enzyme intermediates, J. Biol. Chem, vol.270, pp.25309-25321, 1995.

D. A. Lawrence, S. T. Olson, S. Muhammad, D. E. Day, J. O. Kvassman et al., Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A, J. Biol. Chem, vol.275, pp.5839-5883, 2000.

L. G. Leal, M. A. Lopes, and M. L. Batista, Physical exercise-induced myokines and muscle-adipose tissue crosstalk: A review of current knowledge and the implications for health and metabolic diseases, Front. Physiol, vol.9, 2018.

R. J. Leatherbarrow and P. D. Dean, Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A, Biochem. J, vol.189, pp.27-34, 1980.

B. Lebret and B. Picard, Les principales composantes de la qualité des carcasses et des viandes dans les différentes espèces animales, 2015.

J. Lee, S. Takahama, G. Zhang, S. I. Tomarev, and Y. Ye, Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells, Nat. Cell Biol, vol.18, pp.765-776, 2016.

J. H. Lee and H. S. Jun, Role of myokines in regulating skeletal muscle mass and function, Front. Physiol, 2019.

P. Y. Lee, J. Osman, T. Y. Low, and R. Jamal, Plasma/serum proteomics: Depletion strategies for reducing high-abundance proteins for biomarker discovery, Bioanalysis, vol.11, pp.1799-1812, 2019.

. Legifrance, Arrêté du 13 octobre 2008 portant homologation du cahier des charges de l'indication géographique protégée (IGP) « Génisse fleur d'Aubrac » | Legifrance, 2008.

. Lepetit, Rôle des tissus conjonctifs dans le déterminisme de la tendreté de la viande, In: 10èmes Journées des Sciences du Muscle et Technologies de la Viande, pp.15-25, 2004.

J. Lepetit and J. Culioli, Mechanical properties of meat, Meat Sci, vol.36, pp.203-237, 1994.
URL : https://hal.archives-ouvertes.fr/hal-02701871

B. Levine and J. Yuan, Autophagy in cell death: an innocent convict?, J. Clin. Invest, vol.115, pp.2679-2688, 2005.

H. Li, H. Zhu, C. Xu, and J. Yuan, Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis, Cell, vol.94, pp.491-501, 1998.

L. Li, Dynamic range compression with proteominer TM : Principles and examples, Methods in Molecular Biology, pp.99-107, 2015.

P. Li, D. Nijhawan, and X. Wang, Mitochondrial activation of apoptosis, Cell, vol.116, p.59, 2004.

S. Li, Y. He, Z. Lin, S. Xu, R. Zhou et al., Digging More Missing Proteins Using an Enrichment Approach with ProteoMiner, J. Proteome Res, vol.16, pp.4330-4339, 2017.

Z. Li, E. Rodriguez, S. Azaria, A. Pekarek, and D. S. Hage, Affinity monolith chromatography: A review of general principles and applications, Electrophoresis, vol.38, pp.2837-2850, 2017.

L. C. Lim, M. L. Looi, S. Z. Syed-zakaria, I. Sagap, I. M. Rose et al., Identification of Differentially Expressed Proteins in the Serum of Colorectal Cancer Patients Using 2D-DIGE Proteomics Analysis, Pathol. Oncol. Res, vol.22, pp.169-177, 2016.

K. J. Linton, Structure and Function of ABC Transporters, Physiology, vol.22, pp.122-130, 2007.

A. Listrat, B. Lebret, I. Louveau, T. Astruc, M. Bonnet et al., Comment la structure et la composition du muscle déterminent la qualité des viandes ou chairs, vol.28, pp.125-136, 2015.

A. Listrat, B. Lebret, I. Louveau, T. Astruc, M. Bonnet et al., How Muscle Structure and Composition Influence Meat and Flesh Quality, Sci. World J, vol.2016, pp.1-14, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01285897

A. Listrat, C. Lethias, J. F. Hocquette, G. Renand, F. Ménissier et al., Age-related Changes and Location of Types I, III, XII and XIV Collagen During Development of Skeletal Muscles from Références bibliographiques, 2000.

, Genetically Different Animals. Histochem. J, vol.32, pp.349-356

A. Listrat, N. Rakadjiyski, C. Jurie, B. Picard, C. Touraille et al., Effect of the type of diet on muscle characteristics and meat palatability of growing Salers bulls, Meat Sci, vol.53, pp.115-124, 1999.

G. Liu, Y. Zhao, A. A. Hamuro, L. L. Arnold, M. E. Shen et al., A novel and cost effective method of removing excess albumin from plasma/serum samples and its impacts on LC-MS/MS bioanalysis of therapeutic proteins, Anal. Chem, vol.86, pp.8336-8343, 2014.

Q. Liu, M. C. Lanari, and D. M. Schaefer, A review of dietary vitamin E supplementation for improvement of beef quality, J. Anim. Sci, vol.73, p.3131, 1995.

X. Liu, C. N. Kim, J. Yang, R. Jemmerson, and X. Wang, Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c, Cell, vol.86, pp.147-57, 1996.

Z. Liu, S. Fan, H. Liu, J. Yu, R. Qiao et al., Enhanced Detection of Low-Abundance Human Plasma Proteins by Integrating Polyethylene Glycol Fractionation and Immunoaffinity Depletion, PLoS One, vol.11, p.166306, 2016.

G. Liumbruno, D. 'alessandro, A. Grazzini, G. Zolla, and L. , Blood-related proteomics, J. Proteomics, vol.73, pp.483-507, 2010.

R. J. Lobb, M. Becker, W. Wen, S. Wong, C. Wiegmans et al., Optimized exosome isolation protocol for cell culture supernatant and human plasma, J. Extracell. Vesicles, vol.4, p.27031, 2015.

D. Lomiwes, M. M. Farouk, E. Wiklund, and O. A. Young, Small heat shock proteins and their role in meat tenderness: A review, Meat Sci, vol.96, pp.26-40, 2014.

, Lucidchart. Lucid Software Inc. Structure de base de données et tutoriel de conception | Lucidchart

A. Ludwig and B. Giebel, Exosomes: Small vesicles participating in intercellular communication, Int. J. Biochem. Cell Biol, vol.44, pp.11-15, 2012.

J. Lunardi, J. Fauré, M. I. Monnier, and N. , Le récepteur de la ryanodine de type I, médecine/sciences, vol.24, pp.897-899, 2008.

Z. Ma and S. Ramakrishna, Electrospun regenerated cellulose nanofiber affinity membrane functionalized with protein A/G for IgG purification, J. Memb. Sci, vol.319, pp.23-28, 2008.

S. Maas, X. O. Breakefield, and A. M. Weaver, Extracellular Vesicles: Unique Intercellular Delivery Vehicles, Trends Cell Biol, vol.27, pp.172-188, 2017.

L. Maccatrozzo, M. Patruno, L. Toniolo, C. Reggiani, and F. Mascarello, Myosin heavy chain 2B isoform is expressed in specialized eye muscles but not in trunk and limb muscles of cattle, Eur. J. Histochem, vol.48, pp.357-66, 2004.

L. M. Maclean, P. J. O'toole, M. Stark, J. Marrison, C. Seelenmeyer et al., Trafficking and release of Leishmania metacyclic HASPB on macrophage invasion, Cell. Microbiol, vol.14, pp.740-61, 2012.

A. A. Maddur, R. Swanson, G. Izaguirre, P. Gettins, and S. T. Olson, Kinetic intermediates en route to the final serpin-protease complex: studies of complexes of ?1-protease inhibitor with trypsin, J. Biol. Chem, vol.288, pp.32020-32055, 2013.

A. Mahn and M. Ismail, Depletion of highly abundant proteins in blood plasma by ammonium sulfate precipitation for 2D-PAGE analysis, J. Chromatogr. B Anal. Technol. Biomed. Life Sci, vol.879, pp.3645-3648, 2011.

J. M. Malheiros, C. P. Braga, R. A. Grove, F. A. Ribeiro, C. R. Calkins et al., Influence of oxidative damage to proteins on meat tenderness using a proteomics approach, Meat Sci, vol.148, pp.64-71, 2019.

C. Maltin, D. Balcerzak, R. Tilley, and M. Delday, Determinants of meat quality: tenderness, Proc. Nutr. Soc, vol.62, pp.337-384, 2003.

C. A. Maltin, C. C. Warkup, K. R. Matthews, C. M. Grant, A. D. Porter et al., Pig muscle fibre characteristics as a source of variation in eating quality, Meat Sci, vol.47, pp.237-248, 1997.

R. A. Mancini and M. C. Hunt, Current research in meat color, Meat Sci, vol.71, pp.100-121, 2005.

R. Manjithaya, C. Anjard, W. F. Loomis, and S. Subramani, Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation, J. Cell Biol, vol.188, pp.537-583, 2010.

R. Manjithaya and S. Subramani, Autophagy: a broad role in unconventional protein secretion?, Trends Cell Biol, vol.21, pp.67-73, 2011.

R. Marino, M. Albenzio, A. Della-malva, M. Caroprese, A. Santillo et al., Changes in meat quality traits and sarcoplasmic proteins during aging in three different cattle breeds, Meat Sci, vol.98, pp.178-186, 2014.

R. Marouga, S. David, and E. Hawkins, The development of the DIGE system: 2D fluorescence difference gel analysis technology, Anal. Bioanal. Chem, vol.382, pp.669-678, 2005.

S. Mathivanan, H. Ji, and R. J. Simpson, Exosomes: Extracellular organelles important in intercellular communication, J. Proteomics, vol.73, pp.1907-1920, 2010.

J. Matsubara, M. Ono, A. Negishi, H. Ueno, T. Okusaka et al., Identification of a predictive biomarker for hematologic toxicities of gemcitabine, J. Clin. Oncol, vol.27, pp.2261-2268, 2009.

C. Mazzeo, V. Calvo, R. Alonso, I. Mérida, and M. Izquierdo, Protein kinase D1/2 is involved in the maturation of multivesicular bodies and secretion of exosomes in T and B lymphocytes, Cell Death Differ, vol.23, pp.99-109, 2016.

. Mccormick, Collagen. In: In Applied Muscle. Biology and Meat Science. M. Du, pp.128-148, 2009.

R. Mccormick, Extracellular modifications to muscle collagen: implications for meat quality, Poult. Sci, vol.78, pp.785-791, 1999.

W. H. Mcdonald and J. R. Yates, Shotgun proteomics and biomarker discovery, Dis. Markers, vol.18, pp.99-105, 2002.

J. P. Mcgrath and A. Varshavsky, The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein, Nature, vol.340, pp.400-404, 1989.

H. T. Mcmahon and E. Boucrot, Membrane curvature at a glance, J. Cell Sci, vol.128, pp.1065-1070, 2015.

A. C. Mcpherron, A. M. Lawler, and S. Lee, Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member, Nature, vol.387, pp.83-90, 1997.

H. Mehrani, M. Ghanei, J. Aslani, and Z. Tabatabaei, Plasma proteomic profile of sulfur mustard exposed lung diseases patients using 2-dimensional gel electrophoresis, Clin. Proteomics, vol.8, 2011.

S. Mekchay, T. Teltathum, S. Nakasathien, and P. Pongpaichan, Proteomic Analysis of Tenderness Trait in Thai Native and Commercial Broiler Chicken Muscles, J. Poult. Sci, vol.47, pp.8-12, 2010.

I. Mellman and G. Warren, The road taken: past and future foundations of membrane traffic, Cell, vol.100, pp.99-112, 2000.

. Micol, Qualités sensorielles de la viande bovine. Impacts des facteurs d'élevage, Muscle et viande de ruminant., Quae éditi, pp.163-173, 2010.

E. A. Miller, T. H. Beilharz, P. N. Malkus, M. C. Lee, S. Hamamoto et al., Multiple Cargo Binding Sites on the COPII Subunit Sec24p Ensure Capture of Diverse Membrane Proteins into Transport Vesicles, Cell, vol.114, pp.497-509, 2003.

M. F. Miller, H. R. Cross, J. D. Crouse, and T. G. Jenkins, Effect of feed energy intake on collagen characteristics and muscle quality of mature cows, Meat Sci, vol.21, pp.287-294, 1987.

A. Mitsumoto, Y. Nakagawa, A. Takeuchi, K. Okawa, A. Iwamatsu et al., Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat, Free Radic. Res, vol.35, pp.301-310, 2001.

N. Mizushima, B. Levine, A. M. Cuervo, and D. J. Klionsky, Autophagy fights disease through cellular selfdigestion, Nature, vol.451, pp.1069-1075, 2008.

I. Moevi, La vente directe de viande bovine : Eléments d'information et de réflexion, Compte rendu de l'Institut de l'Elevage n°2033215, pp.1-114, 2003.

S. J. Moisá, S. S. Aly, T. W. Lehenbauer, W. J. Love, P. V. Rossitto et al., Association of plasma haptoglobin concentration and other biomarkers with bovine respiratory disease status in pre-weaned dairy calves, J. Vet. Diagnostic Investig, vol.31, pp.40-46, 2019.

K. Monastyrskaya, E. B. Babiychuk, and A. Draeger, The annexins: spatial and temporal coordination of signaling events during cellular stress, Cell. Mol. Life Sci, vol.66, pp.2623-2642, 2009.

G. Monin, Facteurs biologiques des qualités de la viande bovine, 1991.

F. Monsón, C. Sañudo, and I. Sierra, Influence of breed and ageing time on the sensory meat quality and consumer acceptability in intensively reared beef, Meat Sci, vol.71, pp.471-479, 2005.

J. L. Montgomery, F. C. Parrish, D. C. Beitz, R. L. Horst, E. J. Huff-lonergan et al., The use of vitamin D3 to improve beef tenderness, J. Anim. Sci, vol.78, p.2615, 2000.

Y. H. Moon, W. K. Cho, and S. S. Lee, Investigation of blood biomarkers related to meat quality and quantity in Hanwoo steers, Asian-Australasian J. Anim. Sci, vol.31, pp.1923-1929, 2018.

J. B. Morgan, J. W. Savell, D. S. Hale, R. K. Miller, D. B. Griffin et al., National beef tenderness survey, J. Anim. Sci, vol.69, p.3274, 1991.

C. Morganti, M. Bonora, L. Sbano, G. Morciano, G. Aquila et al., The mitochondrial permeability transition pore, Mitochondrial Biology and Experimental Therapeutics, pp.47-73, 2018.

D. S. Mottram, Flavour formation in meat and meat products: a review, Food Chem, vol.62, pp.415-424, 1998.

M. R. Muhsin-sharafaldine, S. C. Saunderson, A. C. Dunn, J. M. Faed, T. Kleffmann et al., Procoagulant and immunogenic properties of melanoma exosomes, microvesicles and apoptotic vesicles, Oncotarget, vol.7, pp.56279-56294, 2016.

A. M. Mullen, L. Pannier, and R. Hamill, New insights into the biology of meat quality from genomic and proteomic perspectives, with particular emphasis on beef, Improving the Sensory and Nutritional Quality of Fresh Meat, pp.199-224, 2009.

T. G. Nagaraja, S. K. Narayanan, G. C. Stewart, and M. M. Chengappa, Fusobacterium necrophorum infections in animals: Pathogenesis and pathogenic mechanisms, Anaerobe, vol.11, pp.239-246, 2005.

K. Nakanishi, M. Maruyama, T. Shibata, and N. Morishima, Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development, J. Biol. Chem, vol.276, pp.41237-41244, 2001.

B. M. Naveena, C. Faustman, N. Tatiyaborworntham, S. Yin, R. Ramanathan et al., Detection of 4-hydroxy-2-nonenal adducts of turkey and chicken myoglobins using mass spectrometry, Food Chem, vol.122, pp.836-840, 2010.

A. Negishi, M. Ono, Y. Handa, H. Kato, K. Yamashita et al., Large-scale quantitative clinical proteomics by label-free liquid chromatography and mass spectrometry, Cancer Sci, vol.100, pp.514-519, 2009.

K. G. Newton and G. Co, The microbiology of DFD fresh meats: A review, Meat Sci, vol.5, pp.223-232, 1981.

W. Nickel, The mystery of nonclassical protein secretion, Eur. J. Biochem, vol.270, pp.2109-2119, 2003.

W. Nickel and M. Seedorf, Unconventional Mechanisms of Protein Transport to the Cell Surface of Eukaryotic Cells, Annu. Rev. Cell Dev. Biol, vol.24, pp.287-308, 2008.

G. Van-niel, D. Angelo, G. Raposo, and G. , Shedding light on the cell biology of extracellular vesicles, Nat. Rev. Mol. Cell Biol, vol.19, pp.213-228, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02359760

T. Nishimura, Role of extracellular matrix in development of skeletal muscle and postmortem aging of meat, Meat Sci, vol.109, pp.48-55, 2015.

M. A. O'brien and K. R. , Apoptosis: A review of pro-apoptotic and anti-apoptotic pathways and dysregulation in disease, J. Vet. Emerg. Crit. Care, vol.18, pp.572-585, 2008.

P. H. O'farrell, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem, vol.250, pp.4007-4028, 1975.

T. G. O'quinn, J. F. Legako, J. C. Brooks, and M. F. Miller, Evaluation of the contribution of tenderness, 2018.

, juiciness, and flavor to the overall consumer beef eating experience1, Transl. Anim. Sci, vol.2, pp.26-36

T. D. Oberley, W. Zhong, L. I. Szweda, and L. W. Oberley, Localization of antioxidant enzymes and oxidative damage products in normal and malignant prostate epithelium, Prostate, vol.44, pp.144-55, 2000.

G. Offer, P. Knight, R. Jeacocke, R. Almond, T. Cousins et al., The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products, 1989.

K. Ohmine, K. Kawaguchi, S. Ohtsuki, F. Motoi, H. Ohtsuka et al., Quantitative Targeted Proteomics of Pancreatic Cancer: Deoxycytidine Kinase Protein Level Correlates to Progression-Free Survival of Patients Receiving Gemcitabine Treatment, Mol. Pharm, vol.12, pp.3282-3291, 2015.

S. Ohta, I. Ohsawa, K. Kamino, F. Ando, and H. Shimokata, Mitochondrial ALDH2 Deficiency as an Oxidative Stress, Mitochondrial Pathogenesis, pp.36-44, 2004.

. Olleta, Sensory evaluation of several european cattle breeds, Proc 2nd Seminar of the Scientific-Professional Network on Mediterranean Livestock Farming, 2006.
URL : https://hal.archives-ouvertes.fr/hal-02755515

G. S. Omenn, D. J. States, M. Adamski, T. W. Blackwell, R. Menon et al., Hanash SM. 2005. Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, vol.5, pp.3226-3245

S. Orrenius, V. Gogvadze, and B. Zhivotovsky, Calcium and mitochondria in the regulation of cell death, Biochem. Biophys. Res. Commun, vol.460, pp.72-81, 2015.

J. Osman, S. C. Tan, P. Y. Lee, T. Y. Low, and R. Jamal, Sudden Cardiac Death (SCD) -Risk stratification and prediction with molecular biomarkers, J. Biomed. Sci, vol.26, 2019.

M. Ostrowski, N. B. Carmo, S. Krumeich, I. Fanget, G. Raposo et al., Rab27a and Rab27b control different steps of the exosome secretion pathway, Nat. Cell Biol, vol.12, pp.19-30, 2010.

S. Otte and C. Barlowe, Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles, Nat. Cell Biol, vol.6, pp.1189-1194, 2004.

A. Ouali, Meat Tenderization: Possible Causes and Mechanisms. a, Review. J. Muscle Foods, vol.1, pp.129-165, 1990.
URL : https://hal.archives-ouvertes.fr/hal-02715942

A. Ouali, Sensory quality of meat as affected by muscle biochemistry and modern technologies, Animal Biotechnology and the Quality of Meat Production, pp.85-105, 1991.
URL : https://hal.archives-ouvertes.fr/hal-02778894

A. Ouali, M. Gagaoua, Y. Boudida, S. Becila, A. Boudjellal et al., Références bibliographiques, p.150, 2013.

, Biomarkers of meat tenderness: Present knowledge and perspectives in regards to our current understanding of the mechanisms involved, Meat Sci, vol.95, pp.854-870

A. Ouali, C. H. Herrera-mendez, G. Coulis, S. Becila, A. Boudjellal et al., Revisiting the conversion of muscle into meat and the underlying mechanisms, Meat Sci, vol.74, pp.44-58, 2006.

A. Ouali and A. Talmant, Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles, Meat Sci, vol.28, pp.331-348, 1990.
URL : https://hal.archives-ouvertes.fr/hal-02715661

M. Oury, R. Dumont, C. Jurie, J. Hocquette, and B. Picard, Specific fibre composition and metabolism of the rectus abdominis muscle of bovine Charolais cattle, BMC Biochem, vol.11, p.12, 2010.
URL : https://hal.archives-ouvertes.fr/hal-02665325

M. P. Oury, J. Agabriel, C. Agabriel, D. Micol, B. Picard et al., Relationship between rearing practices and eating quality traits of the muscle rectus abdominis of Charolais heifers, Livest. Sci, vol.111, pp.242-254, 2007.
URL : https://hal.archives-ouvertes.fr/hal-02146987

G. Palade, Intracellular aspects of the process of protein synthesis. Science (80-. ), vol.189, pp.347-358, 1975.

T. Palzkill and . Kluwer, Proteomics, Proteomics, 2002.

I. Parolini, C. Federici, C. Raggi, L. Lugini, S. Palleschi et al., Microenvironmental pH is a key factor for exosome traffic in tumor cells, J. Biol. Chem, vol.284, pp.34211-34222, 2009.

T. Pas, M. Hoekman, A. Smits, and M. , Biomarkers as management tools for industries in the pork production chain, J. Chain Netw. Sci, vol.11, pp.155-166, 2011.

M. Patron, A. Raffaello, V. Granatiero, A. Tosatto, G. Merli et al., The mitochondrial calcium uniporter (MCU): molecular identity and physiological roles, J. Biol. Chem, vol.288, pp.10750-10758, 2013.

B. K. Pedersen, Muscle as a Secretory Organ, Comprehensive Physiology, pp.1337-1362, 2013.

B. K. Pedersen, T. Åkerström, A. R. Nielsen, and C. P. Fischer, Role of myokines in exercise and metabolism, J. Appl. Physiol, vol.103, pp.1093-1098, 2007.

B. K. Pedersen and M. A. Febbraio, Muscles, exercise and obesity: skeletal muscle as a secretory organ, Nat. Rev. Endocrinol, vol.8, pp.457-465, 2012.

H. R. Pelham, SNAREs and the specificity of membrane fusion, Trends Cell Biol, vol.11, pp.99-101, 2001.

H. R. Pelham and J. E. Rothman, The debate about transport in the Golgi--two sides of the same coin, Cell, vol.102, pp.713-722, 2000.

P. Pelissier, D. Delourme, A. Germot, X. Blanchet, S. Becila et al., An original SERPINA3 gene cluster: Elucidation of genomic organization and gene expression in the Bos taurus 21q24 region, BMC Genomics, vol.9, p.151, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01211893

S. R. Pfeffer, Unsolved Mysteries in Membrane Traffic, Annu. Rev. Biochem, vol.76, pp.629-645, 2007.

P. A. , Caspases: potential targets for regulating cell death, J. Cell. Mol. Med, vol.8, pp.432-476, 2004.

B. Picard, S. Allais, C. Jurie, H. Levéziel, L. Journaux et al., , 2009.

B. Picard, C. Berri, L. Lefaucheur, C. Molette, T. Sayd et al., Skeletal muscle proteomics in livestock production, Briefings Funct. Genomics Proteomics, vol.9, pp.259-278, 2010.
URL : https://hal.archives-ouvertes.fr/hal-02664698

B. Picard and I. Cassar-malek, Evidence for expression of IIb myosin heavy chain isoform in some skeletal muscles of Blonde d'Aquitaine bulls, Meat Sci, vol.82, pp.30-36, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02665867

B. Picard and M. Gagaoua, Meta-proteomics for the discovery of protein biomarkers of beef tenderness: An overview of integrated studies, Food Res. Int, vol.127, p.108739, 2020.
URL : https://hal.archives-ouvertes.fr/hal-02627755

B. Picard and M. Gagaoua, Proteomic Investigations of Beef Tenderness, Proteomics in Food Science, pp.177-197, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01580641

B. Picard and M. Gagaoua, Proteomic Investigations of Beef Tenderness, Proteomics Food Sci, pp.177-197, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01580641

B. Picard, M. Gagaoua, A. , M. , D. Koning et al., Beef tenderness and intramuscular fat proteomic biomarkers: muscle type effect, PeerJ, vol.6, p.4891, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01818264

B. Picard, M. Gagaoua, and K. Hollung, Gene and Protein Expression as a Tool to Explain/Predict Meat (and Fish) Quality. In: New Aspects of Meat Quality, pp.321-354, 2017.

B. Picard, M. Gagaoua, A. Jammas, M. Bonnet, and M. , Beef tenderness and intramuscular fat proteomic biomarkers: Effect of gender and rearing practices, J. Proteomics, vol.200, pp.1-10, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02627558

B. Picard, M. Kammoun, M. Gagaoua, C. Barboiron, B. Meunier et al., Calcium homeostasis and muscle energy metabolism are modified in HspB1-null mice, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02639482

B. Picard and A. Kondjoyan, La viande : de l'e?evage a? l'assiette, Presses Un, 2019.

B. Picard, B. Lebret, I. Cassar-malek, L. Liaubet, C. Berri et al., Recent advances in omic technologies for meat quality management, Meat Sci, vol.109, pp.18-26, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02740130

B. Picard, F. Lefèvre, B. Lebret, F. Lefevre, and B. Lebret, Meat and fish flesh quality improvement with proteomic applications, Anim. Front, vol.2, pp.18-25, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01210384

B. Picard, J. Robelin, and Y. Geay, Influence of castration and postnatal energy restriction on the contractile and metabolic characteristics of bovine muscle, 1995.
URL : https://hal.archives-ouvertes.fr/hal-00889189

L. Picard, C. Malek, . Liaubet, . Berri, L. Bihan-duval et al., Des marqueurs génomiques au service de la qualité de la viande, 2015.

P. Picotti and R. Aebersold, Selected reaction monitoring-based proteomics: Workflows, potential, Références bibliographiques 152 pitfalls and future directions, Nat. Methods, vol.9, pp.555-566, 2012.

S. Piovesana, A. L. Capriotti, G. Caruso, C. Cavaliere, L. Barbera et al., Labeling and label free shotgun proteomics approaches to characterize muscle tissue from farmed and wild gilthead sea bream (Sparus aurata), J. Chromatogr. A, vol.1428, pp.193-201, 2016.

R. C. Piper and D. J. Katzmann, Biogenesis and Function of Multivesicular Bodies, Annu. Rev. Cell Dev. Biol, vol.23, pp.519-547, 2007.

S. Pisanu, G. Biosa, L. Carcangiu, S. Uzzau, and D. Pagnozzi, Comparative evaluation of seven commercial products for human serum enrichment/depletion by shotgun proteomics, Talanta, vol.185, pp.213-220, 2018.

P. Plomgaard, P. A. Halban, and K. Bouzakri, Bimodal impact of skeletal muscle on pancreatic ?-cell function in health and disease, Diabetes, Obes. Metab, vol.14, pp.78-84, 2012.

V. Polaskova, A. Kapur, A. Khan, M. P. Molloy, and M. S. Baker, High-abundance protein depletion: Comparison of methods for human plasma biomarker discovery, Electrophoresis, vol.31, pp.471-482, 2010.

R. Polati, M. Menini, E. Robotti, R. Millioni, E. Marengo et al., Proteomic changes involved in tenderization of bovine Longissimus dorsi muscle during prolonged ageing, Food Chem, vol.135, pp.2052-2069, 2012.

C. Praillet, J. Grimaud, and H. Lortat-jacob, Les protéoglycanes. (I) Molécules aux multiples fonctions, futures molécules thérapeutiques ? médecine/sciences, vol.14, p.412, 1998.

D. J. Pulford, P. Dobbie, F. Vazquez, S. Fraser-smith, E. Frost et al., Variation in bull beef quality due to ultimate muscle pH is correlated to endopeptidase and small heat shock protein levels, Meat Sci, vol.83, pp.1-9, 2009.

D. J. Pulford, F. Vazquez, S. Frost, D. F. Fraser-smith, E. Dobbie et al., The intracellular distribution of small heat shock proteins in post-mortem beef is determined by ultimate pH, Meat Sci, vol.79, pp.623-630, 2008.

P. P. Purslow, Intramuscular connective tissue and its role in meat quality, Meat Sci, vol.70, pp.435-447, 2005.

M. A. Puthenveedu, C. Bachert, S. Puri, F. Lanni, and A. D. Linstedt, GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution, Nat. Cell Biol, vol.8, pp.238-248, 2006.

V. N. Puttamallesh, S. K. Sreenivasamurthy, P. Singh, H. C. Harsha, A. Ganjiwale et al., Proteomic profiling of serum samples from chikungunya-infected patients provides insights into host response, Clin. Proteomics, vol.10, p.14, 2013.

T. Rabilloud, M. Chevallet, S. Luche, and C. Lelong, Two-dimensional gel electrophoresis in proteomics: Past, present and future, J. Proteomics, vol.73, pp.2064-2077, 2010.
URL : https://hal.archives-ouvertes.fr/hal-00509715

C. Rabouille, Pathways of Unconventional Protein Secretion, Trends Cell Biol, vol.27, pp.230-240, 2017.

C. Rabouille and J. Klumperman, The maturing role of COPI vesicles in intra-Golgi transport, Nat. Rev. Mol. Cell Biol, vol.6, pp.812-817, 2005.

C. Rabouille and A. D. Linstedt, GRASP: A Multitasking Tether. Front. Cell Dev. Biol, vol.4, p.1, 2016.

C. Rabouille, V. Malhotra, and W. Nickel, Diversity in unconventional protein secretion, Références bibliographiques, vol.125, 2012.

G. Raposo and W. Stoorvogel, Extracellular vesicles: Exosomes, microvesicles, and friends, J. Cell Biol, vol.200, pp.373-383, 2013.

Z. El-rassi and C. Puangpila, Liquid-phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis-An update covering the period, Electrophoresis, vol.38, pp.150-161, 2014.

J. Ratajczak, M. Wysoczynski, F. Hayek, A. Janowska-wieczorek, and M. Z. Ratajczak, Membrane-derived microvesicles: important and underappreciated mediators of cell-to-cell communication, Leukemia, vol.20, pp.1487-1495, 2006.

;. Raude and . Français, , vol.43, pp.19-28, 2008.

M. Rechsteiner and C. P. Hill, Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors, Trends Cell Biol, vol.15, pp.27-33, 2005.

D. Rémond, M. Peyron, and I. Savary-auzeloux, Viande et nutrition protéique, 2010.

G. Renand, B. Picard, C. Touraille, P. Berge, and J. Lepetit, Relationships between muscle characteristics and meat quality traits of young Charolais bulls, Meat Sci, vol.59, pp.49-60, 2001.
URL : https://hal.archives-ouvertes.fr/hal-02675972

M. Renerre, Effect of age and slaughter weight on the color of young bull meat (Friesian and Charolais breeds), Sci. Aliments, 1982.

M. Renerre, Factors involved in the discoloration of beef meat, IInternational J. Food Sci. Technol, vol.25, pp.613-630, 1990.
URL : https://hal.archives-ouvertes.fr/hal-02713562

M. Renerre, A. M. Gatellier, and P. , Autoxidation of purified myoglobin from two bovine muscles, Meat Sci, vol.32, pp.331-342, 1992.
URL : https://hal.archives-ouvertes.fr/hal-02706735

S. J. Rice, X. Liu, B. Miller, M. Joshi, J. Zhu et al., Proteomic profiling of human plasma identifies apolipoprotein E as being associated with smoking and a marker for squamous metaplasia of the lung, Proteomics, vol.15, pp.3267-3277, 2015.

N. Rifai, M. A. Gillette, and S. A. Carr, Protein biomarker discovery and validation: the long and uncertain path to clinical utility, Nat. Biotechnol, vol.24, pp.971-983, 2006.

P. G. Righetti and E. Boschetti, Sample treatment methods involving combinatorial peptide ligand libraries for improved proteomes analyses, Methods Mol. Biol, vol.1243, pp.55-82, 2015.

P. G. Righetti, G. Candiano, A. Citterio, and E. Boschetti, Combinatorial peptide ligand libraries as a "trojan horse" in deep discovery proteomics, Anal. Chem, vol.87, pp.293-305, 2015.

J. Robelin and L. Casteilla, Différenciation, croissance et développement du tissu adipeux, Prod. Anim, vol.3, pp.243-252, 1990.

S. Roche, L. Tiers, M. Provansal, M. Seveno, M. T. Piva et al., Depletion of one, six, twelve or twenty major blood proteins before proteomic analysis: The more the better?, J. Proteomics, vol.72, pp.945-951, 2009.
URL : https://hal.archives-ouvertes.fr/hal-00410072

R. Pharmacy and A. P. , The definition of exosome and extracellular vesicles (EV), 2019.

D. P. Romancino, G. Paterniti, Y. Campos, D. Luca, A. et al., Identification and characterization of the nano-sized vesicles released by muscle cells, FEBS Lett, vol.587, pp.1379-1384, 2013.

H. Rottenberg and J. B. Hoek, The path from mitochondrial ROS to aging runs through the mitochondrial permeability transition pore, Aging Cell, vol.16, pp.943-955, 2017.

L. J. Rowe, K. R. Maddock, S. M. Lonergan, and E. Huff-lonergan, Oxidative environments decrease tenderization of beef steaks through inactivation of ??-calpain, J. Anim. Sci, vol.82, pp.3254-3266, 2004.

W. Ruan and M. Lai, Actin, a reliable marker of internal control?, Clin. Chim. Acta, vol.385, pp.1-5, 2007.

J. Rung and A. Brazma, Reuse of public genome-wide gene expression data, Nat. Rev. Genet, vol.14, pp.1-11, 2013.

S. K. Rupinder, A. K. Gurpreet, and S. Manjeet, Cell suicide and caspases, Vascul. Pharmacol, vol.46, pp.383-393, 2007.

E. Ruusuvuori and K. Kaila, Carbonic Anhydrases and Brain pH in the Control of Neuronal Excitability, Sub-cellular biochemistry, pp.271-290, 2014.

X. Saelens, N. Festjens, L. Walle, . Vande, M. Gurp et al., Toxic proteins released from mitochondria in cell death, Oncogene, vol.23, pp.2861-2874, 2004.

K. Saha, F. Bender, and E. Gizeli, Comparative study of IgG binding to proteins G and A: Nonequilibrium kinetic and binding constant determination with the acoustic waveguide device, Anal. Chem, vol.75, pp.835-842, 2003.

K. Salimi, D. D. Usta, ?. Koçer, E. Çelik, and A. Tuncel, Protein A and protein A/G coupled magnetic SiO2 microspheres for affinity purification of immunoglobulin G, Int. J. Biol. Macromol, vol.111, pp.178-185, 2018.

A. M. Salter, Impact of consumption of animal products on cardiovascular disease, diabetes, and cancer in developed countries, Anim. Front, vol.3, pp.20-27, 2013.

J. G. Salway, Metabolism at a glance, vol.125, 2004.

A. Samali and T. G. Cotter, Heat Shock Proteins Increase Resistance to, Apoptosis. Exp. Cell Res, vol.223, pp.163-170, 1996.

L. Santucci, G. Candiano, A. Petretto, C. Lavarello, M. Bruschi et al., Combinatorial ligand libraries as a two-dimensional method for proteome analysis, J. Chromatogr. A, vol.1297, pp.106-112, 2013.

A. Sarin, M. Clerici, S. P. Blatt, C. W. Hendrix, G. M. Shearer et al., Inhibition of activationinduced programmed cell death and restoration of defective immune responses of HIV+ donors by cysteine protease inhibitors, J. Immunol, vol.153, pp.862-72, 1994.

K. Satoh, T. Maniwa, T. Oda, K. Matsumoto, and . Ichi, Proteomic profiling for the identification of serum diagnostic biomarkers for abdominal and thoracic aortic aneurysms, Proteome Sci, vol.11, 2013.

S. Sauer and T. Luge, Nutriproteomics: Facts, concepts, and perspectives, Proteomics, vol.15, pp.997-1013, 2015.

D. Sauvant, M. Letourneau-montminy, P. Schmidely, M. Boval, C. Loncke et al., Use and misuse Références bibliographiques 155 of meta-analysis in Animal Science, 2019.

D. Sauvant, P. Schmidely, and J. J. Daudin, Les méta-analyses des données expérimentales : applications en nutrition animale, Prod. Anim, vol.1, issue.18, pp.63-73, 2005.

A. Savina, C. M. Fader, M. T. Damiani, and M. I. Colombo, Rab11 promotes docking and fusion of multivesicular bodies in a calcium-dependent manner, Traffic, vol.6, pp.131-143, 2005.

A. Savina, M. Furlán, M. Vidal, and M. I. Colombo, Exosome release is regulated by a calcium-dependent mechanism in K562 cells, J. Biol. Chem, vol.278, pp.20083-90, 2003.

J. C. Sawdy, S. A. Kaiser, N. R. St-pierre, and M. P. Wick, Myofibrillar 1-D fingerprints and myosin heavy chain MS analyses of beef loin at 36 h postmortem correlate with tenderness at 7 days, Meat Sci, vol.67, pp.421-426, 2004.

Y. Saylan and A. Denizli, Supermacroporous composite cryogels in biomedical applications, Gels 5, 2019.

T. Schäfer, H. Zentgraf, C. Zehe, B. Brügger, J. Bernhagen et al., Unconventional Secretion of Fibroblast Growth Factor 2 Is Mediated by Direct Translocation across the Plasma Membrane of Mammalian Cells, J. Biol. Chem, vol.279, pp.6244-6251, 2004.

, Sensory analysis ISO 6658, 2017.

M. Sentandreu, G. Coulis, and A. Ouali, Role of muscle endopeptidases and their inhibitors in meat tenderness, Trends Food Sci. Technol, vol.13, pp.400-421, 2002.

S. D. Shackelford, M. Koohmaraie, M. F. Miller, J. D. Crouse, and J. O. Reagan, An evaluation of tenderness of the longissimus muscle of Angus by Hereford versus Brahman crossbred heifers, J. Anim. Sci, vol.69, pp.171-177, 1991.

V. Sierra and M. Oliván, Role of mitochondria on muscle cell death and meat tenderization, Recent Pat. Endocr. Metab. Immune Drug Discov, vol.7, pp.120-129, 2013.

C. Sihlbom, I. Kanmert, . Bahr-h-von, and P. Davidsson, Evaluation of the Combination of Bead Technology with SELDI-TOF-MS and 2-D DIGE for Detection of Plasma Proteins, J. Proteome Res, vol.7, pp.4191-4198, 2008.

G. A. Silverman, P. I. Bird, R. W. Carrell, F. C. Church, P. B. Coughlin et al., The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature, J. Biol. Chem, vol.276, pp.33293-33299, 2001.

R. J. Simes, Publication bias: the case for an international registry of clinical trials, J. Clin. Oncol, vol.4, pp.1529-1541, 1986.

K. D. Sinclair, G. E. Lobley, G. W. Horgan, D. J. Kyle, A. D. Porter et al., Factors influencing beef eating quality 1. Effects of nutritional regimen and genotype on Références bibliographiques 156 organoleptic properties and instrumental texture, Anim. Sci, vol.72, pp.269-277, 2001.

S. Sinha, D. Hoshino, N. H. Hong, K. C. Kirkbride, N. E. Grega-larson et al., Cortactin promotes exosome secretion by controlling branched actin dynamics, J. Cell Biol, vol.214, pp.197-213, 2016.

T. Skotland, K. Sandvig, and A. Llorente, Lipids in exosomes: Current knowledge and the way forward, Prog. Lipid Res, vol.66, pp.30-41, 2017.

M. Smith, S. L. Wood, A. Zougman, J. Ho, J. Peng et al., A systematic analysis of the effects of increasing degrees of serum immunodepletion in terms of depth of coverage and other key aspects in top-down and bottom-up proteomic analyses, Proteomics, vol.11, pp.2222-2235, 2011.

V. L. Smith, L. Jackson, and J. S. Schorey, Ubiquitination as a Mechanism To Transport Soluble Mycobacterial and Eukaryotic Proteins to Exosomes, J. Immunol, vol.195, pp.2722-2730, 2015.

F. Smulders, P. Hofbauer, and G. H. Geesink, The Conversion of Muscle to Meat, Meat Inspection and Control in the Slaughterhouse, pp.399-421, 2014.

S. Sorbolini, G. Marras, G. Gaspa, C. Dimauro, M. Cellesi et al., Detection of selection signatures in Piemontese and Marchigiana cattle, two breeds with similar production aptitudes but different selection histories, Genet. Sel. Evol, p.47, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01336308

J. Soulat, Pilotage conjoint, à partir des pratiques d'élevage, des caractéristiques de la carcasse et de la viande de bovins, 2017.

J. Soulat, B. Picard, S. Léger, M. Ellies-oury, and V. Monteils, Preliminary Study to Determinate the Effect of the Rearing Managements Applied during Heifers' Whole Life on Carcass and Flank Steak Quality, vol.7, p.160, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02621787

M. Squier, A. Miller, A. M. Malkinson, and J. J. Cohen, Calpain activation in apoptosis, J. Cell. Physiol, vol.159, pp.229-237, 1994.

P. R. Srinivas, M. Verma, Y. Zhao, and S. Srivastava, Proteomics for cancer biomarker discovery, Clin. Chem, vol.48, pp.1160-1169, 2002.

J. Staal, T. Bekaert, and R. Beyaert, Regulation of NF-?B signaling by caspases and MALT1 paracaspase, Cell Res, vol.21, pp.40-54, 2011.

D. J. States, G. S. Omenn, T. W. Blackwell, D. Fermin, J. Eng et al., Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study, Nat. Biotechnol, vol.24, pp.333-338, 2006.

S. Stefanovic and R. S. Hegde, Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER, Cell, vol.128, pp.1147-1159, 2007.

H. Stenmark, Rab GTPases as coordinators of vesicle traffic, Nat. Rev. Mol. Cell Biol, vol.10, pp.513-525, 2009.

H. Stennicke and G. Salvesen, Catalytic properties of the caspases, Cell Death Differ, vol.6, pp.1054-1059, 1999.

H. R. Stennicke and G. S. Salvesen, Caspase Assays. Methods Enzymol, vol.322, pp.91-100, 2000.

J. P. Steringer, H. Müller, and W. Nickel, Unconventional Secretion of Fibroblast Growth Factor 2-A Novel Type of Protein Translocation across Membranes?, J. Mol. Biol, vol.427, pp.1202-1210, 2015.

K. Strimbu and J. A. Tavel, What are biomarkers?, Curr. Opin. HIV AIDS, vol.5, pp.463-466, 2010.

S. Stuffers, A. Brech, and H. Stenmark, ESCRT proteins in physiology and disease, Exp. Cell Res, vol.315, pp.1619-1626, 2009.

S. Stuffers, S. Wegner, C. Stenmark, H. Brech, and A. , Multivesicular Endosome Biogenesis in the Absence of ESCRTs, Traffic, vol.10, pp.925-937, 2009.

D. Sun, H. Zhang, D. Guo, A. Sun, and H. Wang, Shotgun Proteomic Analysis of Plasma from Dairy Cattle Suffering from Footrot: Characterization of Potential Disease-Associated Factors, PLoS One, vol.8, 2013.

D. Sun, X. Zhuang, S. Zhang, Z. Deng, . Bin et al., Exosomes are endogenous nanoparticles that can deliver biological information between cells, Adv. Drug Deliv. Rev, vol.65, pp.342-347, 2013.

X. Sun, M. Butterworth, M. Macfarlane, W. Dubiel, A. Ciechanover et al., Caspase Activation Inhibits Proteasome Function during Apoptosis, Mol. Cell, vol.14, pp.81-93, 2004.

S. K. Pedersen, ?. , J. L. Harry, ?. , L. Sebastian et al., Unseen Proteome: Mining Below the Tip of the Iceberg To Find Low Abundance and Membrane Proteins, 2003.

S. S. Swanek, J. B. Morgan, F. N. Owens, D. R. Gill, C. A. Strasia et al., Vitamin D3 supplementation of beef steers increases longissimus tenderness, J. Anim. Sci, vol.77, p.874, 1999.

J. Takano, M. Tomioka, S. Tsubuki, M. Higuchi, N. Iwata et al., Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice, J. Biol. Chem, vol.280, pp.16175-84, 2005.

E. Tamahkar, C. Babaç, T. Kutsal, E. Pi?kin, and A. Denizli, Bacterial cellulose nanofibers for albumin depletion from human serum, Process Biochem, vol.45, pp.1713-1719, 2010.

C. Tassy, C. H. Herrera-mendez, M. A. Sentandreu, A. L. Brémaud, L. Pélissier et al., Muscle endopin 1, a muscle intracellular serpin which strongly inhibits elastase: purification, characterization, cellular localization and tissue distribution, Biochem. J, vol.388, pp.273-280, 2005.
URL : https://hal.archives-ouvertes.fr/hal-01211896

K. Temmerman, A. D. Ebert, H. Müller, I. Sinning, I. Tews et al., A Direct Role for Phosphatidylinositol-4,5-bisphosphate in Unconventional Secretion of Fibroblast Growth Factor 2, Traffic, vol.9, pp.1204-1217, 2008.

S. Teoh, J. C. Whisstock, and P. I. Bird, Maspin (SERPINB5) is an obligate intracellular serpin, J. Biol. Chem, vol.285, pp.10862-10871, 2010.

C. Terlouw, Stress reactivity, stress at slaughter and meat quality, In: In Meat Quality: Genetic and Environmental Factors, p.105, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02792925

C. Terlouw, A. Berne, and T. Astruc, Effect of rearing and slaughter conditions on behaviour, physiology and meat quality of Large White and Duroc-sired pigs, Livest. Sci, vol.122, pp.199-213, 2009.
URL : https://hal.archives-ouvertes.fr/hal-02666985

C. Théry, S. Amigorena, G. Raposo, and C. A. , Isolation and Characterization of Exosomes from Cell Culture Supernatants and Biological Fluids, Curr. Protoc. Cell Biol, vol.30, 2006.

C. Théry, M. Ostrowski, and E. Segura, Membrane vesicles as conveyors of immune responses, Nat. Rev. Immunol, vol.9, pp.581-593, 2009.

K. J. Thomas, M. K. Mccoy, J. Blackinton, A. Beilina, M. Van-der-brug et al., DJ-1 acts in parallel to the PINK1/parkin pathway to control mitochondrial function and autophagy, Hum. Mol. Genet, vol.20, pp.40-50, 2011.

A. Thorburn, Death receptor-induced cell killing, Cell. Signal, vol.16, pp.139-144, 2004.

, Thou shalt share your data, Nat. Methods, vol.5, pp.209-209, 2008.

V. Thulasiraman, S. Lin, L. Gheorghiu, J. Lathrop, L. Lomas et al., Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands, Electrophoresis, vol.26, pp.3561-3571, 2005.

U. Tinggi, Selenium: its role as antioxidant in human health, Environ. Health Prev. Med, vol.13, pp.102-110, 2008.

E. Tornberg, Effects of heat on meat proteins -Implications on structure and quality of meat products, Meat Sci, vol.70, pp.493-508, 2005.

C. Touraille, Incidence des caractbristiques musculaires sur les qualites organoleptiques des viandes, Influence. Renc. Rech. Rumin, pp.169-176, 1994.

K. Trajkovic, C. Hsu, S. Chiantia, L. Rajendran, D. Wenzel et al., Ceramide Triggers Budding of Exosome Vesicles into Multivesicular Endosomes. Science (80-. ), vol.319, pp.1244-1247, 2008.

K. Trajkovic, C. Hsu, S. Chiantia, L. Rajendran, D. Wenzel et al., Ceramide triggers budding of exosome vesicles into multivesicular endosomes. Science (80-. ), vol.319, pp.1244-1247, 2008.

J. Travis, J. Bowen, D. Tewksbury, J. D. Pannell, and R. , Isolation of albumin from whole human plasma and fractionation of albumin depleted plasma, Biochem. J, vol.157, pp.301-306, 1976.

C. Tucher, K. Bode, P. Schiller, L. Claßen, C. Birr et al., Extracellular vesicle subtypes released from activated or apoptotic T-lymphocytes carry a specific and stimulus-dependent protein cargo, Front. Immunol, vol.9, 2018.

W. C. Tucker and E. R. Chapman, Role of synaptotagmin in Ca2+-triggered exocytosis, Biochem. J, vol.366, pp.1-13, 2002.

. Ueda-k, ABC Proteins Protect the Human Body and Maintain Optimal Health, Biosci. Biotechnol. Biochem, vol.75, pp.401-409, 2011.

K. R. Underwood, W. J. Means, and M. Du, Caspase 3 is not likely involved in the postmortem tenderization of beef muscle, J. Anim. Sci, vol.86, pp.960-966, 2008.

M. Valapala and J. K. Vishwanatha, Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2, J. Biol. Chem, vol.286, pp.30911-30925, 2011.

G. Van-niel, S. Charrin, S. Simoes, M. Romao, L. Rochin et al., The Tetraspanin CD63 Regulates ESCRT-Independent and -Dependent Endosomal Sorting during Melanogenesis, Dev. Cell, vol.21, pp.708-721, 2011.

M. Vaudel, K. Verheggen, A. Csordas, H. Raeder, F. S. Berven et al., Exploring the potential of public proteomics data, Proteomics, vol.16, pp.214-225, 2016.

L. Venuta, G. Zeitler, M. Steringer, J. P. Müller, H. Nickel et al., The Startling Properties of Fibroblast Growth Factor 2: How to Exit Mammalian Cells without a Signal Peptide at Hand, J. Biol. Chem, vol.290, pp.27015-27035, 2015.

W. Verbeke, L. Van-wezemael, M. D. De-barcellos, J. O. Kügler, J. Hocquette et al., European beef consumers' interest in a beef eating-quality guarantee, Appetite, vol.54, pp.289-296, 2010.
URL : https://hal.archives-ouvertes.fr/hal-02665282

F. Vercauteren, L. Arckens, and R. Quirion, Applications and current challenges of proteomic approaches, focusing on two-dimensional electrophoresis, Amino Acids, vol.33, pp.405-414, 2007.

R. P. Verma and C. Hansch, Matrix metalloproteinases (MMPs): Chemical-biological functions and (Q)SARs, Bioorg. Med. Chem, vol.15, pp.2223-2268, 2007.

X. Vignon, J. Beaulaton, and A. Ouali, Ultrastructural localization of calcium in post-mortem bovine muscle: a cytochemical and X-ray microanalytical study, Histochem. J, vol.21, pp.403-414, 1989.
URL : https://hal.archives-ouvertes.fr/hal-02723710

C. Villarroya-beltri, F. Baixauli, C. Gutiérrez-vázquez, F. Sánchez-madrid, and M. Mittelbrunn, Sorting it out: Regulation of exosome loading, Semin. Cancer Biol, vol.28, pp.3-13, 2014.

C. Villarroya-beltri, F. Baixauli, M. Mittelbrunn, I. Fernández-delgado, D. Torralba et al., ISGylation controls exosome secretion by promoting lysosomal degradation of MVB proteins, Nat. Commun, vol.7, 2016.

F. Vitzthum, F. Behrens, N. L. Anderson, and J. H. Shaw, Proteomics: From Basic Research to Diagnostic Application. A Review of Requirements & Needs ?, J. Proteome Res, vol.4, pp.1086-1097, 2005.

J. Volatier, A. 2. Dufour, and L. Française,

P. Walter and G. Blobel, Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum, Nature, vol.299, pp.691-698, 1982.

K. K. Wang, Calpain and caspase: can you tell the difference?, Trends Neurosci, vol.23, pp.20-26, 2000.

K. Wang, R. Posmantur, R. Nadimpalli, R. Nath, P. Mohan et al., Caspase-Mediated Fragmentation of Calpain Inhibitor Protein Calpastatin during Apoptosis, Arch. Biochem. Biophys, vol.356, pp.187-196, 1998.

S. E. Warder, L. A. Tucker, T. J. Strelitzer, E. M. Mckeegan, J. L. Meuth et al., Reducing agent-mediated precipitation of high-abundance plasma proteins, Anal. Biochem, vol.387, pp.184-193, 2009.

N. J. Wewer-albrechtsen, P. E. Geyer, S. Doll, P. V. Treit, K. N. Bojsen-møller et al., Plasma Proteome Profiling Reveals Dynamics of Inflammatory and Lipid Homeostasis Markers after Roux-En-Y Gastric Bypass Surgery, Cell Syst, vol.7, pp.601-612, 2018.

J. C. Whisstock and S. P. Bottomley, Molecular gymnastics: serpin structure, folding and misfolding, Curr. Opin. Struct. Biol, vol.16, pp.761-768, 2006.

M. Whitham, B. L. Parker, M. Friedrichsen, J. R. Hingst, M. Hjorth et al., Extracellular Vesicles Provide a Means for Tissue Crosstalk during Exercise, Cell Metab, vol.27, pp.237-251, 2018.

M. R. Wilkins, J. Sanchez, A. A. Gooley, R. D. Appel, I. Humphery-smith et al., Progress with Proteome Projects: Why all Proteins Expressed by a Genome Should be Identified and How To Do It, Biotechnol. Genet. Eng. Rev, vol.13, pp.19-50, 1996.

L. L. Wilson, C. L. Egan, W. R. Henning, E. W. Mills, and T. R. Drake, Effects of live animal performance and hemoglobin level on special-fed veal carcass characteristics, Meat Sci, vol.41, pp.89-96, 1995.

P. Wolf, The nature and significance of platelet products in human plasma, Br. J. Haematol, vol.13, pp.269-288, 1967.

D. E. Wood, A. Thomas, L. A. Devi, Y. Berman, R. C. Beavis et al., Bax cleavage is mediated by calpain during drug-induced apoptosis, Oncogene, vol.17, pp.1069-1078, 1998.

W. Wood, M. Turmaine, R. Weber, V. Camp, R. A. Maki et al., Mesenchymal cells engulf and clear apoptotic footplate cells in macrophageless PU.1 null mouse embryos, Development, vol.127, pp.5245-52, 2000.

W. Wu, Y. Fu, M. Therkildsen, X. Li, and R. Dai, Molecular Understanding of Meat Quality Through Application of, Proteomics. Food Rev. Int, vol.31, pp.13-28, 2015.

W. Wu, Q. Yu, Y. Fu, X. Tian, F. Jia et al., Towards muscle-specific meat color stability of Chinese Luxi yellow cattle: A proteomic insight into post-mortem storage, J. Proteomics, vol.147, pp.108-118, 2016.

H. Yamashita, A. S. Jiang, S. London, R. Van-veldhoven, P. P. Subramani et al., Characterization of Human and Murine PMP20 Peroxisomal Proteins That Exhibit Antioxidant Activity in Vitro, J. Biol. Chem, vol.274, pp.29897-29904, 1999.

W. Yan and S. S. Chen, Mass spectrometry-based quantitative proteomic profiling, Briefings Funct. Genomics Proteomics, vol.4, pp.27-38, 2005.

M. Yáñez-mó, P. Siljander, Z. Andreu, A. B. Zavec, F. E. Borràs et al., Biological properties of extracellular vesicles and their physiological functions, J. Extracell. Vesicles, vol.4, pp.1-60, 2015.

C. Yang, Y. R. Liu, Y. Zhang, J. Wang, L. L. Tian et al., Depletion of abundant human serum proteins by per se imprinted cryogels based on sample heterogeneity, Proteomics, vol.17, 2017.

H. H. Yang, K. H. Lu, Y. F. Lin, S. H. Tsai, S. Chakraborty et al., Depletion of albumin and immunoglobulin G from human serum using epitope-imprinted polymers as artificial antibodies, J. Biomed. Mater. Res. -Part A, vol.101, pp.1935-1942, 2013.

Y. Yang, J. Huang, B. Rabii, R. Rabii, and S. Hu, Quantitative proteomic analysis of serum proteins from oral cancer patients: Comparison of two analytical methods, Int. J. Mol. Sci, vol.15, pp.14386-14395, 2014.

W. Yeh, A. Itie, A. J. Elia, M. Ng, H. Shu et al., Requirement for Casper (c-FLIP) in Regulation of Death Receptor-Induced Apoptosis and Embryonic Development, Immunity, vol.12, pp.633-642, 2000.

J. Yoo, B. D. Moyer, S. Bannykh, H. Yoo, J. R. Riordan et al., Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway, J. Biol. Chem, vol.277, pp.11401-11410, 2002.

F. Zamora, A. L. Sayd, T. Lepetit, J. Lebert, A. Sentandreu et al., Serine peptidase inhibitors, the best predictor of beef ageing amongst a large set of quantitative variables, Meat Sci, vol.71, pp.730-742, 2005.
URL : https://hal.archives-ouvertes.fr/hal-02680706

F. Zamora, E. Debiton, J. Lepetit, A. Lebert, E. Dransfield et al., Predicting variability of ageing and toughness in beef M. Longissimus lumborum et thoracis, Meat Sci, vol.43, pp.321-333, 1996.
URL : https://hal.archives-ouvertes.fr/hal-02695459

I. Zapata, H. N. Zerby, and M. Wick, Functional proteomic analysis predicts beef tenderness and the tenderness differential, J. Agric. Food Chem, vol.57, pp.4956-4963, 2009.

I. N. Zelko, T. J. Mariani, and R. J. Folz, Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic, Biol. Med, vol.33, pp.337-386, 2002.

A. Zernecke, K. Bidzhekov, H. Noels, E. Shagdarsuren, L. Gan et al., Delivery of microRNA-126 by apoptotic bodies induces CXCL12-dependent vascular protection, Sci. Signal, vol.2, 2009.

H. Zhang, A. Y. Liu, P. Loriaux, B. Wollscheid, Y. Zhou et al., Mass spectrometric detection of tissue proteins in plasma, Mol. Cell. Proteomics, vol.6, pp.64-71, 2007.

J. Zhang, M. Li, Q. Yu, L. Han, and Z. Ma, Effects of Lysosomal-Mitochondrial Apoptotic Pathway on Tenderness in Post-Mortem Bovine Longissimus Muscle, J. Agric. Food Chem, vol.67, pp.4578-4587, 2019.

M. Zhang, S. J. Kenny, L. Ge, K. Xu, and R. Schekman, Translocation of interleukin-1? into a vesicle intermediate in autophagy-mediated secretion, 2015.

Y. M. Zhao, U. Basu, M. Dodson, J. A. Basarb, and L. L. Guan, Proteome differences associated with fat accumulation in bovine subcutaneous adipose tissues, Proteome Sci, vol.8, p.14, 2010.

K. C. Zimmermann, C. Bonzon, and D. R. Green, The machinery of programmed cell death, Pharmacol. Ther, vol.92, pp.57-70, 2001.

N. Zolotarjova, J. Martosella, G. Nicol, J. Bailey, B. E. Boyes et al., Differences among techniques for high-abundant protein depletion, Proteomics, vol.5, pp.3304-3313, 2005.

R. Zwaal and A. J. Schroit, Pathophysiologic implications of membrane phospholipid asymmetry in blood cells, Blood, vol.89, pp.1121-1132, 1997.

M. H. Zweig and G. Campbell, Receiver-operating characteristic (ROC) plots: a fundamental evaluation tool in clinical medicine, Clin. Chem, vol.39, pp.561-77, 1993.