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α‐Thrombin Activates Akt via a Nonreceptor Tyrosine Kinase in IIC9 Cells
Author(s) -
PHILLIPSMASON POLLY J.,
GOEL REEMA,
BALDASSARE JOSEPH J.
Publication year - 2002
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2002.tb04623.x
Subject(s) - protein kinase b , tyrosine kinase , platelet derived growth factor receptor , phosphorylation , thrombin , receptor tyrosine kinase , thrombin receptor , proto oncogene tyrosine protein kinase src , microbiology and biotechnology , chemistry , bruton's tyrosine kinase , kinase , genistein , tyrosine phosphorylation , cancer research , signal transduction , biology , receptor , endocrinology , biochemistry , platelet , immunology , growth factor
A bstract : Previous data from our laboratory show that PI 3‐kinase is required for α‐thrombin‐stimulated G 1 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 nonreceptor tyrosine kinases.