Mechanism of c-Src Synergy with the EGFR in Breast Cancer.

Abstract

We have discovered a mechanism of c-Src synergy with the EGFR and located specific points at which the pathway can be interdicted. Specifically, we have shown that kinase-inactive c-Src is able to inhibit tumorigenicity of the IOT 1/2 mouse fibroblast model cells by not phosphorylating the receptor on Tyr 845 in the activation loop of the kinase. The phosphorylation of Tyr 845 is required for EGF and serum-induced DNA synthesis through the EGFR. This phosphorylation site in cancer cells presents an appealing target for cancer therapy of tumors that overexpress the EGFR and c-Src, such as breast cancer. We have also shown that inhibition of c-Src in breast tumor cells efficiently blocks tumor formation further supporting that this may be an effective therapeutic target. Finally, in an effort to isolate a single domain of c-Src to target, we have demonstrated that the SH2 domain and surprisingly the kinase domain of c-Src have inhibitory effects on tumorigenicity and growth of breast tumor cells.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1998
Accession Number
ADA357255

Entities

Organizations

  • University of Virginia

Tags

DTIC Thesaurus Topics

  • Antibodies
  • Biomedical Research
  • Breast Cancer
  • Cell Line
  • Cells
  • Chemistry
  • Diseases And Disorders
  • Fibroblasts
  • Inhibition
  • Kinases
  • Materials
  • Neoplasms
  • Phosphorylation
  • Three Dimensional
  • Tumor Cell Line
  • Two Dimensional
  • Tyrosine

Fields of Study

  • Biology

Readers

  • Breast cancer cell signaling and growth regulation.

Technology Areas

  • 5G