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Granulocyte colony-stimulating factor-induced dephosphorylation of a 45 kD cytosolic protein in HL-60 cells differentiating into neutrophils.

Abstract：

:Granulocyte colony-stimulating factor (G-CSF)-induced alteration of phosphoprotein during differentiation of HL-60 cells was studied. From the two-dimensional gel electrophoresis analysis of phosphoproteins, a 45 kD phosphoprotein in the cytosolic fraction of DMSO-pretreated HL-60 cells was rapidly dephosphorylated by the addition of G-CSF. This 45 kD phosphoprotein migrated into four or five spots between 4.5 and 5.5 pI. The dephosphorylation of 45 kD protein was observed within at least 10 min and reached a maximum at 60 min. Phosphoamino acid analysis showed that only serine residue of 45 kD phosphoprotein was phosphorylated, suggesting that G-CSF induced an activation of serine phosphatase. Furthermore, Staurosporine and calphostin C inhibited the phosphorylation of 45 kD protein, suggesting that protein kinase C or its downstream kinase(s) is involved in the phosphorylation of 45 kD protein. These results indicate that G-CSF causes dephosphorylation of a 45 kD cytosolic phosphoprotein which may play a role in signal transduction of G-CSF.

journal_name

Br J Haematol

journal_title

British journal of haematology

authors

Yamaguchi T,Oshizawa T,Yamaguchi T,Suzuki K,Yamamoto Y,Hayakawa T

doi

10.1046/j.1365-2141.1998.00829.x

subject

Has Abstract

pub_date

1998-08-01 00:00:00

pages

798-803

issue

3

eissn

0007-1048

issn

1365-2141

journal_volume

102

pub_type

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