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EFFECT OF EGF ON CELL-MATRIX INTERACTION AND TYROSINE PHOSPHORYLATION OF THE p125 FOCAL ADHESION KINASE IN HUMAN GASTRIC CARCINOMA CELLS

Research Project

Project/Area Number 06672216
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field Biological pharmacy
Research InstitutionSETSUNAN UNIVERSITY

Principal Investigator

ITO Fumiaki  SETSUNAN UNIVERSITY,DEPARTMENT OF PHARMACEUTICAL SCIENCES PROFESSOR, 薬学部, 教授 (80111764)

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)
Project Period (FY) 1994 – 1995
Project Status Completed (Fiscal Year 1995)
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)
KeywordsEPIDERMAL GROWTH FACTOR / FOCAL ADHESION KINASE / COLLAGEN / INTEGRIN / CADHERIN / CATENIN / CELL-CELL INTERACTION / CELL-EXTRACELLULARMATRIX INTERACTION
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.

Report

(3 results)
  • 1995 Annual Research Report   Final Research Report Summary
  • 1994 Annual Research Report
  • Research Products

    (10 results)

All Other

All Publications (10 results)

  • [Publications] S.Shibamoto: "Association of p120,a tyrosine kinase substrate,with E-cadherin/catenin complexes"" J. Cell Biol.128. 949-957 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Takeuchi: "Hepatocyte growth factro(HGF)-induced cell migration is modulated by epidermalgrowth factor through the tyrosine phosphorylation of HGF receptor" Exp. Cell Res.(1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Nagamine: "Dissociation of c-fos induction and MAP kinase activation from HGF-induced motility response in human gastric carcinoma cells" Eur. J. Biochem.(1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] S.Shibamoto: "Association of p120, a tyrosine kinase substrate, with E-cadherin/catenin complexes" J.Cell Biol.128. 949-957 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Takeuchi: "Hepatocyte growth factor (HGF) -induced cell migration is modulated by epidermalgrowth factor through the tyrosine phosphorylation of HGF receptor" Exp.Cell Res.(in press). (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Nagamine: "Dissociation of c-fos induction and MAP kinase activation from HGF-induced motility response in human gastric carcinoma cells" Eur.J.Biochem.(in press). (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K. Takeuchi: "Hepatocyte growth factor(HGF)-induced cell migration is modulated by epidermalgrowth factor through the tyrosine phosphorylation of HGF receptor" Exp. Cell Res.(1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] K. Nagamine: "Dissociation of c-fos induction and MAP kinase activation from HGF-induced motility response in human gastric carcinoma cells" Eur. J. Biochem.(1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] Oyama,T.: "A Truncated β-Catenin Diorupts the Interaction between E-cadherin and α-Catenin:A Cauee of Loss of Intercelluln Adhesivenessin Human Cancer All rLne" Caneer Res.54. 6282-6287 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] Shibamoto,S.: "Association of p120,a Tyrosine Kinase Substrate,with E-cadherinl Catenin Complexes" J.Cell Biol.(1995)

    • Related Report
      1994 Annual Research Report

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Published: 1994-04-01   Modified: 2016-04-21  

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