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rdf:type |
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lifeskim:mentions |
umls-concept:C0009333,
umls-concept:C0013765,
umls-concept:C0025543,
umls-concept:C0033692,
umls-concept:C0172537,
umls-concept:C0182537,
umls-concept:C0243125,
umls-concept:C0392762,
umls-concept:C0441655,
umls-concept:C0623362,
umls-concept:C0699900,
umls-concept:C1707455
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pubmed:dateCreated |
1991-8-21
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2039471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2083684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2132731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2173721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2174891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2197998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2253219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2539808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2543625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2550050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2556414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2697298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2780323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2834383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2844164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-2930500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-3000628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-3095317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-3138995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-3182822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-3518704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-4204102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-4733239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-6086649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-6162199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-6215207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-6217835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-6347180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-7001953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-7030312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1649600-7041891
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Elastin,
http://linkedlifedata.com/resource/pubmed/chemical/Gelatinases,
http://linkedlifedata.com/resource/pubmed/chemical/MMP7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 7,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Pepsin A,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
277 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1649600-Cell Line,
pubmed-meshheading:1649600-Collagen,
pubmed-meshheading:1649600-Elastin,
pubmed-meshheading:1649600-Extracellular Matrix,
pubmed-meshheading:1649600-Fibroblasts,
pubmed-meshheading:1649600-Gelatinases,
pubmed-meshheading:1649600-Gingiva,
pubmed-meshheading:1649600-Humans,
pubmed-meshheading:1649600-Kinetics,
pubmed-meshheading:1649600-Matrix Metalloproteinase 3,
pubmed-meshheading:1649600-Matrix Metalloproteinase 7,
pubmed-meshheading:1649600-Metalloendopeptidases,
pubmed-meshheading:1649600-Molecular Weight,
pubmed-meshheading:1649600-Pepsin A,
pubmed-meshheading:1649600-Proteoglycans,
pubmed-meshheading:1649600-Recombinant Proteins,
pubmed-meshheading:1649600-Substrate Specificity
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pubmed:year |
1991
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pubmed:articleTitle |
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).
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pubmed:affiliation |
Strangeways Research Laboratory, Worts' Causeway, Cambridge, U.K.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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