Stallion epididymal fluid proteome: qualitative and quantitative characterization, secretion and dynamic changes of major proteins - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Access content directly
Journal Articles Biology of Reproduction Year : 2000

Stallion epididymal fluid proteome: qualitative and quantitative characterization, secretion and dynamic changes of major proteins

Abstract

Proteins present in and secreted into the lumen of various regions of the stallion epididymis were characterized qualitatively and quantitatively by two-dimensional electrophoresis. Using this proteomic approach, 201 proteins were found in the lumen and 117 were found that were secreted by the epithelium in various parts of the organ. Eighteen proteins made up 92.6% of the total epididymal secretory activity, lactoferrin (41.2%) and clusterin (24.8%) being the most abundant. Procathepsin D, HE1/CTP (cholesterol transfer protein), GPX (glutathione peroxidase), beta-N-acetyl-hexosaminidase, and PGDS (prostaglandin D2 synthase) were the other major compounds secreted. The most abundant proteins found in the luminal fluid were albumin and the secreted proteins: lactoferrin, PGDS, GPX, HE1/CTP, and hexosaminidase. Three main secretory epididymal regions were identified from the protein pattern, i.e., regions E0-E2, E3-E5, and E6-E9. Region E0-E2 was characterized by the secretion of clusterin (53%), PGDS (44%), and GPX (6%). Region E3-E5 had the highest number of secreted proteins, the highest protein concentrations (60-80 mg/ml), and the highest spermatocrit value (85%). Lactoferrin (60% in E4), clusterin (29% in E3), hexosaminidase (10% in E3), and procathepsin D (6.9% in E4) were the mast abundant proteins in this region. Region E6-E9, in which few region-specific secreted compounds were found, was characterized by a high quantity of lactoferrin in the luminal fluid (2-14 mg/ml). Comparison between the secretion of the major proteins and their concentrations in the lumen throughout the organ showed that the behavior of each protein is specific, in particular for the three isoforms of clusterin.
Fichier principal
Vignette du fichier
2002_Fouchecourt_BiolReprod_62_1790_freeaccess_1.pdf (2.3 Mo) Télécharger le fichier
Origin : Publisher files allowed on an open archive
Loading...

Dates and versions

hal-02697075 , version 1 (01-06-2020)

Identifiers

Cite

Sophie Fouchécourt, Sonia Metayer, Aude Locatelli, Françoise Dacheux, J.L. Dacheux. Stallion epididymal fluid proteome: qualitative and quantitative characterization, secretion and dynamic changes of major proteins. Biology of Reproduction, 2000, 62 (6), pp.1790-1803. ⟨10.1095/biolreprod62.6.1790⟩. ⟨hal-02697075⟩
13 View
58 Download

Altmetric

Share

Gmail Facebook X LinkedIn More