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J Biol Chem, Vol. 273, Issue 6, 3230-3235, February 6, 1998
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From the Treatment of cells with granulocyte
colony-stimulating factor (G-CSF) leads to tyrosine phosphorylation of
cellular proteins. G-CSF stimulates both the activation of protein
tyrosine kinases Lyn, Jak1, and Jak2 and the association of these
enzymes with the G-CSF receptor. Wild-type, lyn-deficient,
and syk-deficient chicken B lymphocyte cell lines were
transfected with the human G-CSF receptor, and stable transfectants
were studied. G-CSF-dependent tyrosyl phosphorylation of
Jak1 and Jak2 occurred in all three cell lines. Wild-type and
syk-deficient transfectants responded to G-CSF in a
dose-responsive fashion with increased thymidine incorporation, but
none of the clones of lyn-deficient transfectants did.
Ectopic expression of Lyn, but not that of c-Src, in the lyn-deficient cells restored their mitogenic
responsiveness to G-CSF. Ectopic expression in wild-type cells of
the kinase-inactive form of Lyn, but not of the kinase-inactive form of
Jak2, inhibited thymidine incorporation in response to G-CSF. These
studies show that the absence of Lyn results in the loss of mitogenic
signaling in the G-CSF signaling pathway and that activation of Jak1 or Jak2 is not sufficient to cause mitogenesis.
Division of Hematology-Oncology, Children's
Hospital of Pittsburgh, Pittsburgh, Pennsylvania 15213, Departments of
§ Pharmacology and Medicine, University of Pittsburgh
School of Medicine and University of Pittsburgh Cancer Institute,
Pittsburgh, Pennsylvania 15213, and ** Division of Cardiovascular
Medicine, American Cyanamid, Pearl River, New York 10965
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