Source:http://linkedlifedata.com/resource/pubmed/id/12039799
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2002-5-31
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pubmed:abstractText |
Matrix metalloproteinases (MMPs) are proteolytic enzymes that degrade extracellular matrix proteins. These enzymes are implicated in a variety of physiological and pathological events characterized by extracellular matrix remodeling. Recent studies suggest that MMPs may have a signaling capacity, but direct evidence supporting this concept is lacking. In the present study, we demonstrate that outside-in signals delivered by exogenous MMP-1 (interstitial collagenase) markedly increase the number of tyrosine-phosphorylated proteins in platelets. Active MMP-1 also targets beta(3) integrins to areas of cell contact and primes platelets for aggregation. Examination of the endogenous enzyme demonstrated that activated platelets process latent MMP-1 into its active form. Neutralization of MMP-1 activity with MMP inhibitors or specific blocking antibodies markedly attenuates agonist-induced phosphorylation of intracellular proteins, movement of beta(3) integrins to cell contact points, and intercellular aggregation. The finding that MMP-1 is rapidly activated in platelets and controls functional responses identifies a new role for this metalloproteinase as a signaling molecule that regulates thrombotic events.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin beta3,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1524-4571
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pubmed:author |
pubmed-author:AllenLorenL,
pubmed-author:FalkJeanne MJM,
pubmed-author:GaltSpencer WSW,
pubmed-author:KraissLarry WLW,
pubmed-author:LindemannStephanS,
pubmed-author:McIntyreThomas MTM,
pubmed-author:MeddDonald JDJ,
pubmed-author:PrescottStephen MSM,
pubmed-author:WeyrichAndrew SAS,
pubmed-author:ZimmermanGuy AGA
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pubmed:issnType |
Electronic
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pubmed:day |
31
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1093-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12039799-Antigens, CD,
pubmed-meshheading:12039799-Blood Platelets,
pubmed-meshheading:12039799-Humans,
pubmed-meshheading:12039799-Integrin beta3,
pubmed-meshheading:12039799-Matrix Metalloproteinase 1,
pubmed-meshheading:12039799-Phosphorylation,
pubmed-meshheading:12039799-Platelet Activation,
pubmed-meshheading:12039799-Platelet Aggregation,
pubmed-meshheading:12039799-Platelet Membrane Glycoproteins,
pubmed-meshheading:12039799-Protease Inhibitors,
pubmed-meshheading:12039799-Proteins,
pubmed-meshheading:12039799-Signal Transduction
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pubmed:year |
2002
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pubmed:articleTitle |
Outside-in signals delivered by matrix metalloproteinase-1 regulate platelet function.
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pubmed:affiliation |
Departments of Vascular Surgery, Internal Medicine, Program in Human Molecular Genetics, University of Utah, Salt Lake City, USA. sgalt@hsc.utah.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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