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Articular cartilage and changes in Arthritis: Collagen of articular cartilage
The extracellular framework and two-thirds of the dry mass of adult articular cartilage are polymeric collagen. Type II collagen is the principal molecular component in mammals, but collagens III, VI, IX, X, XI, XII and XIV all contribute to the mature matrix. In developing cartilage, the core fibri...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2002
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC128915/ https://www.ncbi.nlm.nih.gov/pubmed/11879535 http://dx.doi.org/10.1186/ar380 |
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author | Eyre, David |
author_facet | Eyre, David |
author_sort | Eyre, David |
collection | PubMed |
description | The extracellular framework and two-thirds of the dry mass of adult articular cartilage are polymeric collagen. Type II collagen is the principal molecular component in mammals, but collagens III, VI, IX, X, XI, XII and XIV all contribute to the mature matrix. In developing cartilage, the core fibrillar network is a cross-linked copolymer of collagens II, IX and XI. The functions of collagens IX and XI in this heteropolymer are not yet fully defined but, evidently, they are critically important since mutations in COLIX and COLXI genes result in chondrodysplasia phenotypes that feature precocious osteoarthritis. Collagens XII and XIV are thought also to be bound to fibril surfaces but not covalently attached. Collagen VI polymerizes into its own type of filamentous network that has multiple adhesion domains for cells and other matrix components. Collagen X is normally restricted to the thin layer of calcified cartilage that interfaces articular cartilage with bone. |
format | Text |
id | pubmed-128915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-1289152002-10-29 Articular cartilage and changes in Arthritis: Collagen of articular cartilage Eyre, David Arthritis Res Review The extracellular framework and two-thirds of the dry mass of adult articular cartilage are polymeric collagen. Type II collagen is the principal molecular component in mammals, but collagens III, VI, IX, X, XI, XII and XIV all contribute to the mature matrix. In developing cartilage, the core fibrillar network is a cross-linked copolymer of collagens II, IX and XI. The functions of collagens IX and XI in this heteropolymer are not yet fully defined but, evidently, they are critically important since mutations in COLIX and COLXI genes result in chondrodysplasia phenotypes that feature precocious osteoarthritis. Collagens XII and XIV are thought also to be bound to fibril surfaces but not covalently attached. Collagen VI polymerizes into its own type of filamentous network that has multiple adhesion domains for cells and other matrix components. Collagen X is normally restricted to the thin layer of calcified cartilage that interfaces articular cartilage with bone. BioMed Central 2002 2001-10-05 /pmc/articles/PMC128915/ /pubmed/11879535 http://dx.doi.org/10.1186/ar380 Text en Copyright © 2001 BioMed Central Ltd |
spellingShingle | Review Eyre, David Articular cartilage and changes in Arthritis: Collagen of articular cartilage |
title | Articular cartilage and changes in Arthritis: Collagen of articular cartilage |
title_full | Articular cartilage and changes in Arthritis: Collagen of articular cartilage |
title_fullStr | Articular cartilage and changes in Arthritis: Collagen of articular cartilage |
title_full_unstemmed | Articular cartilage and changes in Arthritis: Collagen of articular cartilage |
title_short | Articular cartilage and changes in Arthritis: Collagen of articular cartilage |
title_sort | articular cartilage and changes in arthritis: collagen of articular cartilage |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC128915/ https://www.ncbi.nlm.nih.gov/pubmed/11879535 http://dx.doi.org/10.1186/ar380 |
work_keys_str_mv | AT eyredavid articularcartilageandchangesinarthritiscollagenofarticularcartilage |