Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins
Normal and pathological turnover of proteoglycans in articular cartilage involves its cleavage close to the N-terminal G1 domain responsible for aggregation. A fragment containing G1 and G2 N-terminal domains of pig cartilage proteoglycans was therefore used as a substrate to investigate its degrada...
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Published in | The Journal of biological chemistry Vol. 266; no. 24; pp. 15579 - 15582 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
25.08.1991
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Subjects | |
Online Access | Get full text |
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Summary: | Normal and pathological turnover of proteoglycans in articular cartilage involves its cleavage close to the N-terminal G1
domain responsible for aggregation. A fragment containing G1 and G2 N-terminal domains of pig cartilage proteoglycans was
therefore used as a substrate to investigate its degradation by the metalloproteinase stromelysin and related recombinant
stromelysin enzymes. The stromelysins produced an apparent single cleavage yielding a G1 fragment of 56 kDa and a G2 fragment
of 110 kDa. Rabbit bone stromelysin was much more active against the G1-G2 fragment and against proteoglycan aggregates than
recombinant human stromelysin-1 and stromelysin-2. All metalloproteinase preparations were active against proteoglycan and
the G1-G2 fragment at acid (pH 5.5) and neutral pH (7.4). N-terminal sequencing of the G2 fragment derived from the action
of recombinant human stromelysin-1 revealed that cleavage between G1 and G2 occurred at the N-terminal end of the interglobular
domain, close to the last cysteine in G1. The specific cleavage site was between an asparagine and a pair of phenylalanine
residues, where the asparagine corresponds to residue 341 in human and rat mature core protein sequence. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(18)98442-5 |