G-CSF induces tyrosine phosphorylation of the JAK2 protein in the human myeloid G-CSF responsive and proliferative cells, but not in mature neutrophils

K Shimoda, H Iwasaki, S Okamura, Y Ohno… - Biochemical and …, 1994 - Elsevier
K Shimoda, H Iwasaki, S Okamura, Y Ohno, A Kubota, F Arima, T Otsuka, Y Niho
Biochemical and biophysical research communications, 1994Elsevier
Granulocyte colony-stimulating factor (G-CSF) stimulates a rapid phosphorylation on
tyrosines of several proteins of Mr. 130, 100, 90, 70, 44 kd in human myeloid leukemia cell
line cells, Kasumi-1, which respond to G-CSF to proliferate in vitro. In HL60 cells, only a 100
kd protein was phosphorylated, and no detectable phosphorylated proteins were observed
in neutrophils by the stimulation of G-CSF. Among these proteins, the 130 kd protein was
immunoprecipitated by anti-JAK2 serum. While JAK2 is a non receptor tyrosine kinase and …
Abstract
Granulocyte colony-stimulating factor (G-CSF) stimulates a rapid phosphorylation on tyrosines of several proteins of Mr. 130, 100, 90, 70, 44 kd in human myeloid leukemia cell line cells, Kasumi-1, which respond to G-CSF to proliferate in vitro. In HL60 cells, only a 100 kd protein was phosphorylated, and no detectable phosphorylated proteins were observed in neutrophils by the stimulation of G-CSF. Among these proteins, the 130 kd protein was immunoprecipitated by anti- JAK2 serum. While JAK2 is a non receptor tyrosine kinase and is reported to be involved in the signal transduction by various cytokines including growth hormone, erythropoietin, and granulocyte-macrophage colony-stimulating factor/interleukin-3, it is strongly suggested that a signaling pathway that relates to the cell proliferation triggered by G-CSF in immature hematopoietic cells also involves JAK2.
Elsevier