Cartilage type IX collagen is cross-linked by hydroxypyridinium residues |
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Authors: | J J Wu D R Eyre |
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Institution: | Laboratory for Skeletal Disorders, Children''s Hospital and Harvard Medical School, Boston, MA 02115, USA |
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Abstract: | Type IX collagen, a recently discovered, unusual protein of cartilage, has a segmented triple-helical structure containing interchain disulfides. Its polymeric form and function are unknown. When prepared by pepsin from bovine articular cartilage, type IX collagen was found to contain a high concentration of hydroxypyridinium cross-links, similar to that in type II collagen. Fluorescence spectroscopy located the hydroxylysyl pyridinoline and lysyl pyridinoline cross-linking residues exclusively in the high-molecular-weight collagen fraction, from which they were recovered predominantly in a single CNBr-derived peptide. The results point to a structural role for type IX collagen in cartilage matrix, possibly as an adhesion material to type II collagen fibrils. |
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Keywords: | HP hydroxylysyl pyridinoline LP lysyl pyridinoline HMW high molecular fragments of type IX collagen LMW low molecular weight fragments of type IX collagen CNBr cyanogen bromide SDS sodium dodecyl sulfate DTT dithiothreiotol |
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