α-thrombin activates Akt via a nonreceptor tyrosine kinase in IIC9 cells

Polly J. Phillips-Mason, Reema Goel, Joseph J. Baldassare

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Previous data from our laboratory show that PI 3-kinase is required for α-thrombin-stimulated G1 progression in IIC9 cells. In IIC9 cells, PI 3-kinase acts downstream of Ras to activate Akt, in a pathway parallel to ERK1. Here we show that α-thrombin does not transactivate either the EGF receptor or the PDGF receptor as measured by tyrosine phosphorylation, suggesting that activation of PI 3-kinase by α-thrombin is not the result of an RTK. Interestingly, both genistein and PP1 block α-thrombin-stimulated Akt phosphorylation, suggesting the involvement of a member of the Src family of non-receptor tyrosine kinases.

Original languageEnglish (US)
Pages (from-to)142-144
Number of pages3
JournalAnnals of the New York Academy of Sciences
Volume973
DOIs
StatePublished - Jan 1 2002

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science

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