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rdf:type |
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lifeskim:mentions |
umls-concept:C0013879,
umls-concept:C0018284,
umls-concept:C0042071,
umls-concept:C0086418,
umls-concept:C0205263,
umls-concept:C0334227,
umls-concept:C0542341,
umls-concept:C0678594,
umls-concept:C1140680,
umls-concept:C1514485,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1880022
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pubmed:issue |
1-2
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pubmed:dateCreated |
1998-12-2
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pubmed:abstractText |
Ovarian cancer metastasis is associated with an increase in the urokinase-type plasminogen activator (uPA) and its receptor uPAR. We present evidence that binding of uPA to uPAR provokes a mitogenic response in the human ovarian cancer cell line OV-MZ-6 in which endogenous uPA production had been significantly reduced by stable uPA 'antisense' transfection. High molecular weight (HMW) uPA, independent of its enzymatic activity, produced an up to 95% increase in cell number concomitant with 2-fold elevated [3H]thymidine incorporation as did the catalytically inactive but uPAR binding amino-terminal fragment of uPA, ATF. uPA-induced cell proliferation was significantly decreased by blocking uPA/uPAR interaction by the monoclonal antibody IIIF10 and by soluble uPAR. The efficiency of the uPAR binding synthetic peptide cyclo19,31 uPA19-31 to enhance OV-MZ-6 cell growth proved this molecular domain to be the minimal structural determinant for uPA mitogenic activity. Dependence of uPA-provoked cell proliferation on uPAR was further demonstrated in Raji cells which do not express uPAR and were thus not induced by uPA. However, upon transfection with full-length uPAR, Raji cells acquired a significant growth response to HMW uPA and ATF.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/PLAUR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Plasminogen Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Urokinase Plasminogen...,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Urokinase-Type Plasminogen Activator
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-5793
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pubmed:author |
pubmed-author:FischerKK,
pubmed-author:GraeffHH,
pubmed-author:HarbeckNN,
pubmed-author:HeissPP,
pubmed-author:KesslerHH,
pubmed-author:LutherTT,
pubmed-author:LutzVV,
pubmed-author:MagdolenVV,
pubmed-author:NishiguchiTT,
pubmed-author:ReuningUU,
pubmed-author:SchmittMM,
pubmed-author:WilhelmOO
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
438
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
101-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9821967-Antibodies, Monoclonal,
pubmed-meshheading:9821967-Cell Cycle,
pubmed-meshheading:9821967-Cell Division,
pubmed-meshheading:9821967-DNA, Antisense,
pubmed-meshheading:9821967-DNA, Neoplasm,
pubmed-meshheading:9821967-Female,
pubmed-meshheading:9821967-Humans,
pubmed-meshheading:9821967-Lymphocytes,
pubmed-meshheading:9821967-Molecular Weight,
pubmed-meshheading:9821967-Ovarian Neoplasms,
pubmed-meshheading:9821967-Peptide Fragments,
pubmed-meshheading:9821967-Plasminogen Activators,
pubmed-meshheading:9821967-Protein Binding,
pubmed-meshheading:9821967-Receptors, Cell Surface,
pubmed-meshheading:9821967-Receptors, Urokinase Plasminogen Activator,
pubmed-meshheading:9821967-Transfection,
pubmed-meshheading:9821967-Tumor Cells, Cultured,
pubmed-meshheading:9821967-Type C Phospholipases,
pubmed-meshheading:9821967-Urokinase-Type Plasminogen Activator
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pubmed:year |
1998
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pubmed:articleTitle |
Urokinase induces proliferation of human ovarian cancer cells: characterization of structural elements required for growth factor function.
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pubmed:affiliation |
Frauenklinik der Technischen Universität München, Klinikum rechts der Isar, Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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