pubmed-article:12480917 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
pubmed-article:12480917 | lifeskim:mentions | umls-concept:C0246551 | lld:lifeskim |
pubmed-article:12480917 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:12480917 | pubmed:dateCreated | 2002-12-13 | lld:pubmed |
pubmed-article:12480917 | pubmed:abstractText | Pericellular 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:12480917 | pubmed:language | eng | lld:pubmed |
pubmed-article:12480917 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12480917 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12480917 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12480917 | pubmed:month | Dec | lld:pubmed |
pubmed-article:12480917 | pubmed:issn | 0023-6837 | lld:pubmed |
pubmed-article:12480917 | pubmed:author | pubmed-author:CaoJianJ | lld:pubmed |
pubmed-article:12480917 | pubmed:author | pubmed-author:HymowitzMiche... | lld:pubmed |
pubmed-article:12480917 | pubmed:author | pubmed-author:ZuckerStanley... | lld:pubmed |
pubmed-article:12480917 | pubmed:author | pubmed-author:ConnerCathlee... | lld:pubmed |
pubmed-article:12480917 | pubmed:author | pubmed-author:DiYanniElizab... | lld:pubmed |
pubmed-article:12480917 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12480917 | pubmed:volume | 82 | lld:pubmed |
pubmed-article:12480917 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12480917 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12480917 | pubmed:pagination | 1673-84 | lld:pubmed |
pubmed-article:12480917 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:12480917 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12480917 | pubmed:articleTitle | Rapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase a activation. | lld:pubmed |
pubmed-article:12480917 | pubmed:affiliation | Department of Research, Veterans Affairs Medical Center, Northport, New York, 11768, USA. s_zucker@yahoo.com | lld:pubmed |
pubmed-article:12480917 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12480917 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:12480917 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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