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Identification and characterization of the precursor of chicken matrix metalloprotease 2 (pro-MMP-2) in hen egg

Abstract : Using zymography and mass spectrometry, we identified for the first time the precursor of chicken matrix metalloprotease 2 (pro-MMP-2) as a complex with TIMP-2 (tissue inhibitor of metalloproteinases) in egg white and yolk. Real-time polymerase chain reaction confirmed that MMP-2 and its inhibitors TIMP-2 and TIMP-3 were expressed all along the oviduct and in the liver of laying hens. We also demonstrated that the processing of pro-MMP-2 into mature MMP-2 by serine proteases does not occur in vivo, although purified pro-MMP-2 undergoes proteolytic maturation by these proteases in vitro. Moreover, the relative pro-MMP-2 activity assessed by gelatin zymography was shown to decrease in egg white during the storage of unfertilized or fertilized eggs. However, the mature form of 62 kDa MMP-2 could not be detected. The fact that MMP-2 is found as a proform in fresh eggs suggests that the activity of this metalloprotease is regulated under specific conditions during embryonic development.
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Submitted on : Saturday, May 30, 2020 - 9:03:59 PM
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Sophie Réhault-Godbert, Joël Gautron, Valérie Labas, Maya Belghazi, Yves Nys. Identification and characterization of the precursor of chicken matrix metalloprotease 2 (pro-MMP-2) in hen egg. Journal of Agricultural and Food Chemistry, American Chemical Society, 2008, 56 (15), pp.6294-6303. ⟨10.1021/jf8003948⟩. ⟨hal-02660767⟩

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