A 92 kDa gelatinase (MMP-9) cleavage site in native type V collagen.
Native type V collagen molecules resist mammalian collagenase but are cleaved by certain gelatinases. We report a prominent site of cleavage within the collagen type V molecules by 92 kDa gelatinase (MMP-9). The enzyme was purified from conditioned medium of a rabbit synovial cell line (HIG-82). It cleaved native type V collagen from bovine bone in solution at two molecular sites, one near the amino-terminus, the other producing a 3/5 C-terminal fragment. Amino-terminal sequence analysis of the individual alpha chains from this latter fragment showed that MMP-9 had cleaved between residues Gly439-Val in both alpha 1(V) and alpha (XI) and between residues Gly445-Leu in the alpha 2(V) chain. These sites are close to the previously reported trypsin-cleavage site. The findings imply that gelatinases may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen.
Niyibizi
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Department of Orthopaedic Surgery, University of Pittsburgh School of Medicine, PA 15261.
Chan
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R
Wu
J J
JJ
Eyre
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D
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000737:chemistry / Q000378:metabolism; D017364:Collagenases / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D020780:Matrix Metalloproteinase 9; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010449:Peptide Mapping; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013583:Synovial Membrane / Q000201:enzymology
D010446:Peptide Fragments; D003094:Collagen; D017364:Collagenases; D020780:Matrix Metalloproteinase 9