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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-9-9
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pubmed:abstractText |
The mevalonate metabolic pathway is necessary for the isoprenylation of a number of small GTPases. We have previously presented that Rho plays a pivotal role in 1-oleoyl-lysophosphatidic acid (LPA)-induced invasion of rat ascites hepatoma MM1 cells. Herein we report the effect of HMG-CoA reductase inhibitors, fluvastatin and lovastatin, on the in vitro invasion of MM1 cells. Fluvastatin and lovastatin inhibited LPA-induced MM1 cell invasion in a dose-dependent manner. Fluvastatin inhibited LPA-induced translocation of RhoA protein from the cytosol to the membrane and RhoA activation which was measured by pull-down assay for GTP-bound RhoA. Fluvastatin also inhibited the translocation of both endogenous and dominant-active RhoA from the cytosol to the membrane, actin stress fiber assembly and in vitro invasion of the cells expressing dominant-active RhoA (Val14-RhoA). These results indicate that HMG-CoA reductase inhibitors have the potential to reduce RhoA activation and cancer cell invasion by targeting the Rho protein isoprenylation.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Monounsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethylglutaryl-CoA...,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/Lovastatin,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/fluvastatin,
http://linkedlifedata.com/resource/pubmed/chemical/lysophosphatidic acid,
http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1019-6439
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1173-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12964001-Actins,
pubmed-meshheading:12964001-Animals,
pubmed-meshheading:12964001-Cell Division,
pubmed-meshheading:12964001-Cell Line, Tumor,
pubmed-meshheading:12964001-Cell Membrane,
pubmed-meshheading:12964001-Cytosol,
pubmed-meshheading:12964001-DNA, Complementary,
pubmed-meshheading:12964001-Dose-Response Relationship, Drug,
pubmed-meshheading:12964001-Enzyme Inhibitors,
pubmed-meshheading:12964001-Fatty Acids, Monounsaturated,
pubmed-meshheading:12964001-Guanosine Triphosphate,
pubmed-meshheading:12964001-Humans,
pubmed-meshheading:12964001-Hydroxymethylglutaryl-CoA Reductase Inhibitors,
pubmed-meshheading:12964001-Indoles,
pubmed-meshheading:12964001-Lovastatin,
pubmed-meshheading:12964001-Lysophospholipids,
pubmed-meshheading:12964001-Microscopy, Fluorescence,
pubmed-meshheading:12964001-Mutation,
pubmed-meshheading:12964001-Protein Transport,
pubmed-meshheading:12964001-Rats,
pubmed-meshheading:12964001-Time Factors,
pubmed-meshheading:12964001-rhoA GTP-Binding Protein
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pubmed:year |
2003
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pubmed:articleTitle |
Inhibition of lysophosphatidic acid-induced RhoA activation and tumor cell invasion by 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors.
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pubmed:affiliation |
Department of Tumor Biochemistry, Osaka Medical Center for Cancer and Cardiovascular Diseases, Osaka 537-8511, Japan. kusama-to@mail.mc.pref.osaka.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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