Project/Area Number |
08672325
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Surgical dentistry
|
Research Institution | Health Sciences University of Hokkaido |
Principal Investigator |
OKUMURA Kazuhiko Health Sciences University of Hokkaido, 1st Dept.OMS,Assistant prof., 歯学部, 講師 (60194510)
|
Co-Investigator(Kenkyū-buntansha) |
KONISHI Atsushi Health Sciences University of Hokkaido, 1st Dept.OMS,Staff, 歯学部, 助手 (80225466)
|
Project Period (FY) |
1996 – 1997
|
Project Status |
Completed (Fiscal Year 1997)
|
Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1997: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1996: ¥900,000 (Direct Cost: ¥900,000)
|
Keywords | human OSCC cells / invasion / metastasis / PI3-kinase / FAK / tyrosine phosphorylation / Cell adhesiveness / Cell mitility / Rho family / 浸潤・転移 / PI3-Kinase / Focal adhesion kinase |
Research Abstract |
We established different invasiveness clones from human oral squamous cell carcinoma (OSCC) cell line SAS.The factor that defines the invasiveness of the two clones was also examined and two clones showed remarkably different cell motility. Here we report that analyzed signal transduction of cell motility in the OSCC. The role of phosphatidyinositol 3-kinase (PI3-kinase) activity in serum-stimulated tyrosine phosphorylation of focal adhesion kinase (p125^<FAK>) has been examined. The tyrosine phosdphorylation of p125^<FAK> of high-invasion clone SAS-H1, but not low-invasion clone SAS-L1 in response to serum was markedly inhibited by both wortmannin and LY294002, inhibitor of PI3-kinase in dose dependent manner. Furthermore, wortmannin inhibited adhesiveness to extracellular matrixs and cell motility. Serum-stimulated PI3-kinase activity, increased invasion of SAS-H1, but not SAS-L1 by endothelial cell monolayr assay. Thus, we have identified a PI3-kinase dependent signal transduction pathway in the cell motility of high-invasion OSCC cells, as SAS-H1, which leads to the phosphorylation of p125^<FAK>.
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