The synthesis of type X collagen by bovine and human growth-plate chondrocytes.
Chondrocytes were isolated from bovine growth-plate cartilage and cultured within type I collagen gels. A major collagen with chains of Mr 59,000, decreasing to 47,000 on pepsinization, was synthesized and identified as type X collagen. This collagen was cleaved at two sites by mammalian collagenase, resulting in a major triple-helical fragment with chains of Mr 32,000. The species of Mr 59,000, 47,000 and 32,000 were not detected by SDS-polyacrylamide gel electrophoresis before reduction, indicating the presence of disulphide bonds within the triple helix. In contrast, similar biosynthetic studies with human growth-plate cartilage in organ culture, indicated that human type X collagen does not contain disulphide bonds. A polyclonal antiserum was raised to bovine type X collagen and used in immunolocalization studies to provide direct evidence for the association of type X collagen with the hypertrophic chondrocytes in both bovine and human growth plates during development.
Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, UK.
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Marriott
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Ayad
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Grant
D000818:Animals; D002417:Cattle; D002478:Cells, Cultured; D003094:Collagen / Q000096:biosynthesis* / Q000737:chemistry; D046508:Culture Techniques; D005455:Fluorescent Antibody Technique; D006132:Growth Plate / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D008970:Molecular Weight; D011487:Protein Conformation
D003094:Collagen