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PMID: 1649600 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).

The Biochemical journal ·Vol. 277 ( Pt 1) ·1991-07-01 ·Pages 277-9

Murphy G, Cockett MI, Ward RV, Docherty AJ

Abstract

The abilities of the matrix metalloproteinases 95 kDa and 72 kDa gelatinases (type IV collagenases), stromelysins-1 and -2 and punctuated metalloproteinase (PUMP) to degrade insoluble elastin, type IV collagen films and proteoglycan have been compared. The gelatinases and PUMP were markedly more active in the degradation of elastin than were the stromelysins. PUMP and the stromelysins were more potent proteoglycan-degrading enzymes. All of the enzymes studied degraded soluble native type IV collagen, but the gelatinases were more effective at higher temperatures. These quantitative data allow an analysis of the potential relative roles of these metalloproteinases in the breakdown of the key components of connective tissue matrices.

MeSH Terms
Cell Line Collagen/metabolism Elastin/metabolism Extracellular Matrix/enzymology Fibroblasts/enzymology Gelatinases Gingiva/enzymology Humans Kinetics Matrix Metalloproteinase 3 Matrix Metalloproteinase 7 Metalloendopeptidases/metabolism Molecular Weight Pepsin A/metabolism Proteoglycans/metabolism Recombinant Proteins/metabolism Substrate Specificity
Chemicals
Proteoglycans Recombinant Proteins Collagen Elastin Pepsin A Gelatinases Metalloendopeptidases Matrix Metalloproteinase 3 MMP7 protein, human Matrix Metalloproteinase 7
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Murphy G
Strangeways Research Laboratory, Worts' Causeway, Cambridge, U.K.
Cockett M I
Ward R V
Docherty A J
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1991-07-01
Pages
277-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1151220
Subset
IM
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