All three chains of 1 alpha 2 alpha 3 alpha collagen from hyaline cartilage resist human collagenase |
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| Authors: | D R Eyre J J Wu D E Woolley |
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| Institution: | 1. Skeletal Diseases Laboratory, Children''s Hospital and Harvard Medical School Boston, MA 02115, U.S.A.;2. University Department of Medicine, University Hospital of South Manchester, Manchester, M20 BLR, U.K. |
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| Abstract: | A previous report that the 3 alpha collagen chain of hyaline cartilage was cleaved by human collagenase could not be confirmed when the 1 alpha 2 alpha 3 alpha collagen fraction was freed of all contaminating type II collagen. All three minor collagen chains, 1 alpha, 2 alpha and 3 alpha, were totally resistant to highly purified collagenases from both rheumatoid synovial and gastric mucosal tissues. This finding and CNBr-peptide patterns suggest that, despite the close homology with alpha 1 (II), the 3 alpha chain is a unique collagen component, possibly combined with 1 alpha and 2 alpha in heterotrimeric molecules. In contrast, a 3 alpha-like component from fibrocartilage was cleaved by collagenase and gave a CNBr-peptide pattern more typical of alpha 1 (II) than of the collagenase-resistant 3 alpha of hyaline cartilage. |
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| Keywords: | To whom reprint requests should be addressed |
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