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J. Biol. Chem., Vol. 266, Issue 24, 15579-15582, 08, 1991
AJ Fosang, PJ Neame, TE Hardingham, G Murphy and JA Hamilton
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.
Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins
University of Melbourne, Department of Medicine, Royal Melbourne Hospital, Parkville, Australia.
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