G-CSF INDUCES TYROSINE PHOSPHORYLATION OF THE JAK2 PROTEIN IN THE HUMAN MYELOID G-CSF RESPONSIVE AND PROLIFERATIVE CELLS, BUT NOT IN MATURENEUTROPHILS

Citation
K. Shimoda et al., G-CSF INDUCES TYROSINE PHOSPHORYLATION OF THE JAK2 PROTEIN IN THE HUMAN MYELOID G-CSF RESPONSIVE AND PROLIFERATIVE CELLS, BUT NOT IN MATURENEUTROPHILS, Biochemical and biophysical research communications, 203(2), 1994, pp. 922-928
Citations number
21
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
203
Issue
2
Year of publication
1994
Pages
922 - 928
Database
ISI
SICI code
0006-291X(1994)203:2<922:GITPOT>2.0.ZU;2-O
Abstract
Granulocyte colony-stimulating factor (G-CSF) stimulates a rapid phosp horylation on tyrosines of several proteins of Mr. 130, 100, 90, 70, 4 4 kd in human myeloid leukemia cell line cells, Kasumi-1, which respon d to G-CSF to proliferate in vitro. In HL60 cells, only a 100 kd prote in was phosphorylated, and no detectable phosphorylated proteins were observed in neutrophils by the stimulation of G-CSF. Among these prote ins, the 130 kd protein was immunoprecipitated by anti- JAK2 serum. Wh ile JAK2 is a non receptor tyrosine kinase and is reported to be invol ved in the signal transduction by various cytokines including growth h ormone, erythropoietin, and granulocyte-macrophage colony-stimulating factor/interleukin-3, it is strongly suggested that a signaling pathwa y that relates to the cell proliferation triggered by G-CSF in immatur e hematopoietic cells also involves JAK2. (C) 1994 Academic Press, Inc .