Biosynthesis of collagen crosslinks in rabbit articular cartilage in vivo |
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Authors: | F Shapiro D Brickley-Parsons M J Glimcher |
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Affiliation: | Department of Orthopaedic Surgery, Harvard Medical School, Children''s Hospital Medical Center, Boston, Massachusetts 02115 USA |
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Abstract: | The biosynthesis in vivo of the two reducible aldimine crosslinks of immature rabbit articular collagen, hydroxylysinohydroxynorleucine and hydroxylysinonorleucine, is demonstrated. The peak amount of crosslink was detected 1–2 weeks following labeling of the cartilage with [14C]lysine. The subsequent diminution which occurred was due primarily to a decrease in the amount of hydroxylysinohydroxynorleucine. Natural reduction of the aldimine crosslinks in vivo did not occur. Glucosylgalactosyl hydroxylysine and galactosylhydroxylysine, in a ratio, were synthesized. Seventy-three percent of the hydroxylysine residues were glycosylated. [3H]NaBH4 reduction of non-14C-labeled cartilage showed diminished amounts of reducible crosslink with time and the presence of hexosyl lysines and hexosyl hydroxylysines in mature articular cartilage. |
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