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rdf:type |
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lifeskim:mentions |
umls-concept:C0007577,
umls-concept:C0007600,
umls-concept:C0013081,
umls-concept:C0017262,
umls-concept:C0017638,
umls-concept:C0185117,
umls-concept:C0298340,
umls-concept:C0376315,
umls-concept:C0600210,
umls-concept:C0812201,
umls-concept:C2911684
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pubmed:issue |
21
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pubmed:dateCreated |
2001-11-5
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pubmed:abstractText |
Ets transcription factors are associated with tumor malignancy. We reported previously that the stable transfection of the dominant-negative form of Ets-1 (Ets-DN) in the glioma cell line U251 induced down-regulation of urokinase-type plasminogen activator mRNA expression and invasiveness (M. Nakada et al., J. Neuropathol. Exp. Neurol., 58: 329-334, 1999). Here we analyzed effects of Ets-DN expression on cell adhesion, migration, and phosphorylation of focal adhesion kinase. U251 cells expressing Ets-DN (U251-DN) showed reduced cell adhesion, spreading, and extension of actin stress fibers on dishes coated with fibronectin but not on dishes coated with collagen. Migration of U251-DN cells was found to be significantly inhibited compared with that of parental cells when examined by wound-induced migration assay on fibronectin-coated dishes. Phosphorylation levels of focal adhesion kinase in U251-DN cells were also attenuated on dishes coated with fibronectin. Reduced expression level of integrin alpha5 subunit in U251-DN cells was demonstrated by semiquantitative reverse transcription-PCR analysis. Semiquantitative reverse transcription-PCR of surgical samples of brain tumors revealed that the expression level of Ets-1 mRNA correlated with that of integrin alpha5 mRNA in glioma. The experimental metastatic ability of U251-DN cells examined in chick embryo was considerably lower than that of parental cells. These results suggest that Ets-1 contributes to glioma malignancy by up- regulating expression of the integrin alpha5 subunit, which composes integrin alpha5beta1 and mediates intracellular signaling and the subsequent acceleration of the invasive process, including cell adhesion and migration.
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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/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type I,
http://linkedlifedata.com/resource/pubmed/chemical/ETS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Protein-Tyrosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Globins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha5,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin beta3,
http://linkedlifedata.com/resource/pubmed/chemical/PTK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Protein c-ets-1,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-ets,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0008-5472
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7985-91
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11691823-Animals,
pubmed-meshheading:11691823-Antigens, CD,
pubmed-meshheading:11691823-Cell Adhesion,
pubmed-meshheading:11691823-Cell Movement,
pubmed-meshheading:11691823-Chick Embryo,
pubmed-meshheading:11691823-Collagen Type I,
pubmed-meshheading:11691823-Down-Regulation,
pubmed-meshheading:11691823-Fibronectins,
pubmed-meshheading:11691823-Focal Adhesion Kinase 1,
pubmed-meshheading:11691823-Focal Adhesion Protein-Tyrosine Kinases,
pubmed-meshheading:11691823-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:11691823-Glioma,
pubmed-meshheading:11691823-Globins,
pubmed-meshheading:11691823-Humans,
pubmed-meshheading:11691823-Integrin alpha5,
pubmed-meshheading:11691823-Integrin beta3,
pubmed-meshheading:11691823-Liver Neoplasms,
pubmed-meshheading:11691823-Phosphorylation,
pubmed-meshheading:11691823-Platelet Membrane Glycoproteins,
pubmed-meshheading:11691823-Protein-Tyrosine Kinases,
pubmed-meshheading:11691823-Proto-Oncogene Protein c-ets-1,
pubmed-meshheading:11691823-Proto-Oncogene Proteins,
pubmed-meshheading:11691823-Proto-Oncogene Proteins c-ets,
pubmed-meshheading:11691823-RNA, Messenger,
pubmed-meshheading:11691823-Transcription Factors,
pubmed-meshheading:11691823-Transfection,
pubmed-meshheading:11691823-Tumor Cells, Cultured
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pubmed:year |
2001
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pubmed:articleTitle |
Expression of dominant-negative form of Ets-1 suppresses fibronectin-stimulated cell adhesion and migration through down-regulation of integrin alpha5 expression in U251 glioma cell line.
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pubmed:affiliation |
Department of Molecular Virology and Oncology, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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