Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:12480917rdf:typepubmed:Citationlld:pubmed
pubmed-article:12480917lifeskim:mentionsumls-concept:C0007634lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0332307lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0596901lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0699040lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0025543lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0599896lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0851285lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C1879547lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0439831lld:lifeskim
pubmed-article:12480917lifeskim:mentionsumls-concept:C0246551lld:lifeskim
pubmed-article:12480917pubmed:issue12lld:pubmed
pubmed-article:12480917pubmed:dateCreated2002-12-13lld:pubmed
pubmed-article:12480917pubmed:abstractTextPericellular matrix degradation during cancer invasion and inflammation is dependent on activation of progelatinase A by membrane type 1-matrix metalloproteinase (MT1-MMP); a stoichiometric concentration of tissue inhibitor of metalloproteinase-2 (TIMP-2) is required. Activation of progelatinase A has generally been considered to be a slow process occurring as a result of enhanced expression of MT1-MMP. We herein report that ConA treatment of HT1080 fibrosarcoma cells is followed by MT1-MMP-induced activation of progelatinase A on the cell surface within 1 hour. Cell surface biotinylation, immunohistochemistry, and (125)I-labeled TIMP-2 binding to cell surface MT1-MMP were used to characterize the appearance and function of MT1-MMP on the plasma membrane. Treatment of HT1080 cells with ConA resulted in increased specific binding of (125)I-labeled TIMP-2 to cell surface receptors within 5 minutes. TIMP-2 binds almost exclusively to activated MT1-MMP on the surface of HT1080 cells. MT1-MMP function at the cell surface was also accelerated by treatment of cells with cytochalasin D, an inhibitor of actin filaments, PMA, a stimulator of protein kinase C, and bafilomycin A(1), an inhibitor of lysosome/endosome function. A functional pool of intracellular MT1-MMP available for trafficking to the cell surface was demonstrated by repetitive ConA stimulation. ConA-induced expression of MT1-MMP mRNA (Northern blot analysis) in HT1080 cells was a delayed event (>6 hours). These data suggest that presynthesized MT1-MMP is sorted to a transient storage compartment (trans-Golgi network/endosomes), where it is available for rapid trafficking to the plasma membrane and cell surface proteolytic activity.lld:pubmed
pubmed-article:12480917pubmed:languageenglld:pubmed
pubmed-article:12480917pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:citationSubsetIMlld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12480917pubmed:statusMEDLINElld:pubmed
pubmed-article:12480917pubmed:monthDeclld:pubmed
pubmed-article:12480917pubmed:issn0023-6837lld:pubmed
pubmed-article:12480917pubmed:authorpubmed-author:CaoJianJlld:pubmed
pubmed-article:12480917pubmed:authorpubmed-author:HymowitzMiche...lld:pubmed
pubmed-article:12480917pubmed:authorpubmed-author:ZuckerStanley...lld:pubmed
pubmed-article:12480917pubmed:authorpubmed-author:ConnerCathlee...lld:pubmed
pubmed-article:12480917pubmed:authorpubmed-author:DiYanniElizab...lld:pubmed
pubmed-article:12480917pubmed:issnTypePrintlld:pubmed
pubmed-article:12480917pubmed:volume82lld:pubmed
pubmed-article:12480917pubmed:ownerNLMlld:pubmed
pubmed-article:12480917pubmed:authorsCompleteYlld:pubmed
pubmed-article:12480917pubmed:pagination1673-84lld:pubmed
pubmed-article:12480917pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:meshHeadingpubmed-meshheading:12480917...lld:pubmed
pubmed-article:12480917pubmed:year2002lld:pubmed
pubmed-article:12480917pubmed:articleTitleRapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase a activation.lld:pubmed
pubmed-article:12480917pubmed:affiliationDepartment of Research, Veterans Affairs Medical Center, Northport, New York, 11768, USA. s_zucker@yahoo.comlld:pubmed
pubmed-article:12480917pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12480917pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:12480917pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12480917lld:pubmed