EFFECT OF EGF ON CELL-MATRIX INTERACTION AND TYROSINE PHOSPHORYLATION OF THE p125 FOCAL ADHESION KINASE IN HUMAN GASTRIC CARCINOMA CELLS
| Project/Area Number |
06672216
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biological pharmacy
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| Research Institution | SETSUNAN UNIVERSITY |
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Principal Investigator |
ITO Fumiaki SETSUNAN UNIVERSITY,DEPARTMENT OF PHARMACEUTICAL SCIENCES PROFESSOR, 薬学部, 教授 (80111764)
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| Co-Investigator(Kenkyū-buntansha) |
SHIBAMOTO Sayumi SETSUNAN UNIVERSITY,DEPARTMENT OF PHARMACEUTICAL SCIENCES RESEARCH ASSOCIATE, 薬学部, 助手 (80178920)
ITO Michiyasu SETSUNAN UNIVERSITY,DEPARTMENT OF PHARMACEUTICAL SCIENCES RESEARCH ASSOCIATE, 薬学部, 助手 (30201932)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1995: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1994: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | EPIDERMAL GROWTH FACTOR / FOCAL ADHESION KINASE / COLLAGEN / INTEGRIN / CADHERIN / CATENIN / CELL-CELL INTERACTION / CELL-EXTRACELLULARMATRIX INTERACTION |
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| Research Abstract |
Cell migration is a critical event in morphogenesis, tissue repair, and inflammatory reactions. Moreover, it is essential for malignant cells to infiltrate surrounding tissues. Increasing evidence suggests that the interaction of cells with the extracellular matrix affects their migratory properties. Cell migration is regulated by a variety of factors including growth factors such as epidermal growth factors (EGF). Cell adhesion to extracellular matrix molecules is mediated by a family of integrins, each of which is a cell surface protein consisting of an alpha subunit noncovalently associated with a beta subunit. Interaction of integrin with the extracellular matrix activates multiple intracellular signaling pathways, which include stimulation of tyrosine phosphorylation of a 125-kD protein. This protein was termed p125 Focal Adhesion Kinase (FAK), because it is tyrosin kinase located at focal adhesions. However, it remains to be elucidated for a role of FAK and its tyrosine phosphorylation in the formation of focal adhesions. In this present study we examined mechanism by which EGF increases the motility of human gastric carcinoma TMK-1 cells. EGF increased not only the motility of these cells, but also their adhesiveness to the extracellular matrix (type- IV collagen and fibronectin). Further, it increased tyrosine phosphorylation of FAK,which is known to occur during the process of adhesion. Since we have also found that EGF modulate the function of the cadherincatenin system via tyrosine phosphorylation of cadherin associted proteins, EGF may play an important role in the regulation of both interactions of cells with surrounding cells and extracellular matrices.
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Report
(3 results)
Research Products
(10 results)
