Source:http://linkedlifedata.com/resource/pubmed/id/12417038
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
2002-11-5
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| pubmed:abstractText |
We investigated the mechanism of the enhancement of metastatic potential induced by transfection of the fyn gene, a member of the src family. We employed two murine fyn cDNA-transfected clones, ML-SN1 and ML-SN2, which were previously established from an ML-01 low-metastatic clone of Meth A sarcoma of BALB / c mice and were proven to have higher metastatic ability than ML-01 and the mock-transfected clone ML-MT-neo (Takayama et al., 1993). Our present investigation revealed that the two transfectants showed higher metastatic ability and higher rates of adherence to type IV collagen than ML-MT-neo. However, no difference was found in in vitro or in vivo growth rates, attachment to laminin or endothelial cells or cell motility through a reconstituted basement membrane. Analysis of surface membrane proteins labeled with (125)I on SDS-PAGE showed that a 29 kD band specifically bound to type IV collagen-coupled beads was more intense in ML-SN2 than in ML-MT-neo. Genistein, a protein tyrosine kinase inhibitor, dramatically reduced protein tyrosine kinase (PTK) activity of ML-SN2 in a dose-dependent fashion, corresponding to the reduction of adhesiveness to type IV collagen. The expression of the type IV collagen-binding protein (p29) of ML-SN2 was also reduced significantly by genistein treatment. These results suggested that the fyn product in Meth A cells augments the expression of a type IV collagen-binding protein through elevation of the PTK activity of the membrane fraction and thus facilitates the metastasis of Meth A.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type IV,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Fyn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Genistein,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0910-5050
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
93
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1090-9
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:12417038-Animals,
pubmed-meshheading:12417038-Antigens, CD29,
pubmed-meshheading:12417038-Carrier Proteins,
pubmed-meshheading:12417038-Cell Adhesion Molecules,
pubmed-meshheading:12417038-Cell Movement,
pubmed-meshheading:12417038-Collagen Type IV,
pubmed-meshheading:12417038-Female,
pubmed-meshheading:12417038-Fibronectins,
pubmed-meshheading:12417038-Fibrosarcoma,
pubmed-meshheading:12417038-Genistein,
pubmed-meshheading:12417038-Laminin,
pubmed-meshheading:12417038-Lung Neoplasms,
pubmed-meshheading:12417038-Mice,
pubmed-meshheading:12417038-Mice, Inbred BALB C,
pubmed-meshheading:12417038-Proto-Oncogene Proteins,
pubmed-meshheading:12417038-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:12417038-Sarcoma, Experimental,
pubmed-meshheading:12417038-Transfection,
pubmed-meshheading:12417038-Tumor Cells, Cultured
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| pubmed:year |
2002
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| pubmed:articleTitle |
Enhanced expression of type IV collagen-binding protein (p29) in Fyn-transfected murine fibrosarcoma cells.
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| pubmed:affiliation |
The Fourth Department of Internal Medicine, Sapporo Medical University School of Medicine, South-1 West-16, Chuo-ku, Sapporo 060-8543, Japan.
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| pubmed:publicationType |
Journal Article
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