| pubmed-article:12039799 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12039799 | lifeskim:mentions | umls-concept:C0127082 | lld:lifeskim |
| pubmed-article:12039799 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:12039799 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:12039799 | lifeskim:mentions | umls-concept:C1254881 | lld:lifeskim |
| pubmed-article:12039799 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12039799 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:12039799 | pubmed:dateCreated | 2002-5-31 | lld:pubmed |
| pubmed-article:12039799 | 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. | lld:pubmed |
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| pubmed-article:12039799 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12039799 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12039799 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12039799 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12039799 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12039799 | pubmed:month | May | lld:pubmed |
| pubmed-article:12039799 | pubmed:issn | 1524-4571 | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:McIntyreThoma... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:ZimmermanGuy... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:WeyrichAndrew... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:PrescottSteph... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:GaltSpencer... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:KraissLarry... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:LindemannStep... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:AllenLorenL | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:MeddDonald... | lld:pubmed |
| pubmed-article:12039799 | pubmed:author | pubmed-author:FalkJeanne... | lld:pubmed |
| pubmed-article:12039799 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:12039799 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:12039799 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:12039799 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12039799 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12039799 | pubmed:pagination | 1093-9 | lld:pubmed |
| pubmed-article:12039799 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12039799 | pubmed:meshHeading | pubmed-meshheading:12039799... | lld:pubmed |
| pubmed-article:12039799 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12039799 | pubmed:articleTitle | Outside-in signals delivered by matrix metalloproteinase-1 regulate platelet function. | lld:pubmed |
| pubmed-article:12039799 | pubmed:affiliation | Departments of Vascular Surgery, Internal Medicine, Program in Human Molecular Genetics, University of Utah, Salt Lake City, USA. sgalt@hsc.utah.edu | lld:pubmed |
| pubmed-article:12039799 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12039799 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12039799 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:12039799 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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