| pubmed-article:18602101 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C1704256 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C0015350 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C1618608 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C1417203 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:18602101 | lifeskim:mentions | umls-concept:C0205275 | lld:lifeskim |
| pubmed-article:18602101 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:18602101 | pubmed:dateCreated | 2008-7-25 | lld:pubmed |
| pubmed-article:18602101 | pubmed:abstractText | Targeting of transforming growth factor beta (TGF-beta) to the extracellular matrix (ECM) by latent TGF-beta binding proteins (LTBPs) regulates the availability of TGF-beta for interactions with endothelial cells during their quiescence and activation. However, the mechanisms which release TGF-beta complexes from the ECM need elucidation. We find here that morphological activation of endothelial cells by phorbol 12-myristate 13-acetate (PMA) resulted in membrane-type 1 matrix metalloproteinase (MT1-MMP) -mediated solubilization of latent TGF-beta complexes from the ECM by proteolytic processing of LTBP-1. These processes required the activities of PKC and ERK1/2 signaling pathways and were coupled with markedly increased MT1-MMP expression. The functional role of MT1-MMP in LTBP-1 release was demonstrated by gene silencing using lentiviral short-hairpin RNA as well as by the inhibition with tissue inhibitors of metalloproteinases, TIMP-2 and TIMP-3. Negligible effects of TIMP-1 and uPA/plasmin system inhibitors indicated that secreted MMPs or uPA/plasmin system did not contribute to the release of LTBP-1. Current results identify MT1-MMP-mediated proteolytic processing of ECM-bound LTBP-1 as a mechanism to release latent TGF-beta from the subendothelial matrix. | lld:pubmed |
| pubmed-article:18602101 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18602101 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18602101 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18602101 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18602101 | pubmed:issn | 1090-2422 | lld:pubmed |
| pubmed-article:18602101 | pubmed:author | pubmed-author:LehtiKaisaK | lld:pubmed |
| pubmed-article:18602101 | pubmed:author | pubmed-author:Keski-OjaJorm... | lld:pubmed |
| pubmed-article:18602101 | pubmed:author | pubmed-author:VehviläinenPi... | lld:pubmed |
| pubmed-article:18602101 | pubmed:author | pubmed-author:TattiOlgaO | lld:pubmed |
| pubmed-article:18602101 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18602101 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18602101 | pubmed:volume | 314 | lld:pubmed |
| pubmed-article:18602101 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18602101 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18602101 | pubmed:pagination | 2501-14 | lld:pubmed |
| pubmed-article:18602101 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:meshHeading | pubmed-meshheading:18602101... | lld:pubmed |
| pubmed-article:18602101 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18602101 | pubmed:articleTitle | MT1-MMP releases latent TGF-beta1 from endothelial cell extracellular matrix via proteolytic processing of LTBP-1. | lld:pubmed |
| pubmed-article:18602101 | pubmed:affiliation | Departments of Pathology and Virology, University of Helsinki and Helsinki University Hospital, 00014 Helsinki, Finland. | lld:pubmed |
| pubmed-article:18602101 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18602101 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:7040 | entrezgene:pubmed | pubmed-article:18602101 | lld:entrezgene |
| entrez-gene:4052 | entrezgene:pubmed | pubmed-article:18602101 | lld:entrezgene |
| entrez-gene:4323 | entrezgene:pubmed | pubmed-article:18602101 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18602101 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18602101 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18602101 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18602101 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18602101 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18602101 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18602101 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18602101 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18602101 | lld:pubmed |
