Accession Number:

ADB263453

Title:

Functional Interactions Between c-Src and HER1 Potentiate Neoplastic Transformation: Implications for the Etiology of Human Breast Cancer

Descriptive Note:

Final rept. 1 Jul 1997-30 Jun 2000

Corporate Author:

VIRGINIA UNIV CHARLOTTESVILLE

Personal Author(s):

Report Date:

2000-07-01

Pagination or Media Count:

124.0

Abstract:

In cells where the EGF receptor and pp60c-Src are overexpressed, such as a fibroblast model system or in certain human breast cancer cell lines, these two tyrosine kinases interact physically and functionally to promote tumorigenesis. When in association with c-Src, the EGFR becomes phosphorylated within the kinase domain on Tyr 845. Kinase activity of c-Src is required for this phosphorylation to occur, indicating that Tyr 845 is likely a direct target for the c-Src kinase. Tyr 845 phosphorylation occurs in response to a variety of 0-protein coupled and cytokine receptor coupled signaling pathways and c-Src kinase activity is required for this phosphorylation to occur.

Subject Categories:

  • Biochemistry
  • Anatomy and Physiology
  • Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE