Involvement of Tyrosine Phosphatases in Insulin Signaling and Apoptosis in Breast Cancer

Abstract

Our preliminary studies demonstrated that increased intracellular calcium activates calpain to induce partial proteolysis and cytoplasmic translocation of PTP1B, a tyrosine phosphatase proposed to regulate signaling by insulin, IGF-1 and other cytokines. Cytoplasmic translocation of PTP1B results in a distinct pattern of protein tyrosine phosphorylation and these events may regulate cell growth or apoptosis by reducing activated growth factor signaling. In this scheme, calcium-mediated apoptosis and growth inhibition may be directed through mobilization of PTP1B.

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Document Details

Document Type
Technical Report
Publication Date
Jun 01, 2002
Accession Number
ADA411798

Entities

People

  • Nicholas J. Donato

Organizations

  • The University of Texas MD Anderson Cancer Center

Tags

DTIC Thesaurus Topics

  • Abstracts
  • Apoptosis
  • Biomedical Research
  • Breast Cancer
  • Cancer
  • Cell Physiological Processes
  • Cells
  • Cytokines
  • Diseases And Disorders
  • Growth Factors
  • Insulin
  • Neoplasms
  • Phosphorylation
  • Proteins
  • Tumor Cell Line
  • Tyrosine

Fields of Study

  • Biology

Readers

  • Cellular and Molecular Pathways of Apoptosis.