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- W2017316218 endingPage "531" @default.
- W2017316218 startingPage "515" @default.
- W2017316218 abstract "The fibrillar collagens are the most abundant proteins of extracellular matrices. Among them, collagens V and XI are quantitatively minor components which participate in the formation of the fibrillar collagen network. Since these collagens were discovered, studies have demonstrated that they may play a fundamental role in the control of fibrillogenesis, probably by forming a core within the fibrils. Another characteristic of these collagens is the partial retention of their N-propeptide extensions in tissue forms, an unusual observation in comparison to the other known fibrillar collagens. The tissue locations of collagens V and XI are different, but their structural and biological properties seem to be closely related. It has been shown that their primary structures are highly conserved at both the gene and protein levels, and that these conserved features are the bases of their similar biological properties. In particular, they are both resistant to mammalian collagenases, and surprisingly sensitive to trypsin treatment. Collagens V and XI are usually buried within the major collagen fibrils, although they have both cell adhesion and heparin binding sites which could be of crucial importance in physiological processes such as development and wound healing. It has became evident that several molecules are in fact heterotypic associations of chains from both collagens V and XI, demonstrating that these two collagens are not distinct types but a single type which can be called collagen V/XI." @default.
- W2017316218 created "2016-06-24" @default.
- W2017316218 creator A5030958164 @default.
- W2017316218 creator A5054976883 @default.
- W2017316218 creator A5090290848 @default.
- W2017316218 date "1995-07-01" @default.
- W2017316218 modified "2023-09-25" @default.
- W2017316218 title "Another look at collagen V and XI molecules" @default.
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