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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-4-22
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pubmed:abstractText |
Membrane-type-1 matrix metalloproteinase has been identified as an activator of the matrix metalloproteinase progelatinase A at cell surfaces. We report here that a soluble active form of membrane-type-2 matrix metalloproteinase can also process progelatinase A in a comparable fashion to the type-1 at rates which are dependent on the concentration of the proenzyme. Activation is inhibited by tissue inhibitors of metalloproteinases TIMP-2 and TIMP-3, but only partially by TIMP-1. These results suggest that cellular activation of progelatinase A may be initiated by different members of the membrane-type matrix metalloproteinase family depending on tissue distribution.
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pubmed:grant |
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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/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Gelatinases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/progelatinase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2956
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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 |
244
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
653-7
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:9119036-Amino Acid Sequence,
pubmed-meshheading:9119036-Base Sequence,
pubmed-meshheading:9119036-Binding Sites,
pubmed-meshheading:9119036-DNA Primers,
pubmed-meshheading:9119036-Enzyme Activation,
pubmed-meshheading:9119036-Enzyme Precursors,
pubmed-meshheading:9119036-Escherichia coli,
pubmed-meshheading:9119036-Gelatinases,
pubmed-meshheading:9119036-Glycoproteins,
pubmed-meshheading:9119036-Humans,
pubmed-meshheading:9119036-Kinetics,
pubmed-meshheading:9119036-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:9119036-Metalloendopeptidases,
pubmed-meshheading:9119036-Protease Inhibitors,
pubmed-meshheading:9119036-Protein Processing, Post-Translational,
pubmed-meshheading:9119036-Proteins,
pubmed-meshheading:9119036-Recombinant Proteins,
pubmed-meshheading:9119036-Tissue Inhibitor of Metalloproteinase-2,
pubmed-meshheading:9119036-Tissue Inhibitor of Metalloproteinase-3,
pubmed-meshheading:9119036-Tissue Inhibitor of Metalloproteinases
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pubmed:year |
1997
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pubmed:articleTitle |
Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases.
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pubmed:affiliation |
Strangeways Research Laboratory, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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