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- W4244725056 abstract "This chapter describes the molecular structure, functions, and primary structure of collagen type XI. This collagen is a quantitatively minor fibrillar collagen and forms heterotypic fibrils with types II and IX collagens mainly in cartilaginous tissues. However, it is also expressed by nonchondrogenic tissues, particularly during embryonic development. In nonchondrogenic tissues, cross-type heterotrimers of types V and XI collagens frequently exist. Type XI collagen is synthesized as a heterotrimeric procollagen comprising three distinct elements—proα1(XI), proα2(XI), and proα3(XI) chains, although alternative assemblies may exist. The proα1(XI) chain is not cleaved by N-proteinase or mammalian collagenase, suggesting differences between the two chains in either amino acid sequence or enzyme accessibility. The procollagen forms are processed extracellularly at the carboxylic acid terminus, but only partial processing occurs at the NH2 terminus for the proα1(XI) and proα2(XI) chains. The chapter also presents information on the gene structure and the structural and functional sites of type XI collagen." @default.
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- W4244725056 date "1998-01-01" @default.
- W4244725056 modified "2023-09-27" @default.
- W4244725056 title "Collagen type XI" @default.
- W4244725056 doi "https://doi.org/10.1016/b978-012068911-8/50116-0" @default.
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