MassIVE MSV000091002

Complete Public PXD039221

Tissue-regulated collagen hydroxylation at GEP/GDP motifs mediated by P4HA2

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Description

Collagen, the most abundant organic compound of vertebrate organisms, is a supramolecular protein-made polymer. Details of its subtle post-translational maturation largely determine the mechanical properties of connective tissues. Its assembly requires massive, heterogeneous prolyl-4-hydroxylation (P4H), catalyzed by Prolyl-4-hydroxylases (P4HA1-3), providing thermostability to its elemental, triple helical building block. So far, there was no evidence of tissue-specific regulation of P4H, nor of a differential substrate repertoire of P4HAs. Here, the positional P4H profiles of collagen extracted from bone, skin, and tendon were compared, revealing lower hydroxylation of most GEP/GDP motifs in the tendon, across homeotherms. P4HA2 mRNA was found low in tendon. Invalidation of P4HA2, unlike decreased, generalized P4H activity, in the ATDC5 cellular model of collagen assembly, mimicked the tendon-related P4H profile. Therefore, P4HA2 has a better ability than other P4HAs to hydroxylate GEP/GDP motifs and the differential expression of P4HAs in tissues dictates the positional P4H profile of collagen, which participates in determining tissue specificities of its assembly. [doi:10.25345/C5GX4544G] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: type I collagen ; 4-hydroxyproline ; prolyl-4-hydroxylase ; tendon

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Principal Investigators:
(in alphabetical order) 		vincourt, IMoPA UMR 7365 CNRS UL, FRANCE
Submitting User: jbvincourt
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