Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells.

Csar, Xavier F., Wilson, Nicholas J., Strike, Philip, Sparrow, Lindsay, McMahon, Kerrie Ann, Ward, Alister and Hamilton, John A 2001, Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells., Proteomics, vol. 1, pp. 435-443.

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Title Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells.
Author(s) Csar, Xavier F.
Wilson, Nicholas J.
Strike, Philip
Sparrow, Lindsay
McMahon, Kerrie Ann
Ward, Alister
Hamilton, John A
Journal name Proteomics
Volume number 1
Start page 435
End page 443
Publisher Wiley - V C H Verlag
Place of publication Weinheim, Germany
Publication date 2001
ISSN 1615-9853
1615-9861
Keyword(s) Superoxide dismutase
Microsequencing
Hydroxyapatite
Protein purification;
Protein phosphorylation;
Two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis;
Macrophage-colony stimulating factor
Granulocyte-colony stimulating factor 1
Summary Using two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis (2-D SDS-PAGE) of 32P-labeled cytosolic and membrane extracts, we identified a 21.5 kDa phosphoprotein with an isoelectric point of 6.0 in NFS-60 cells that was phosphorylated maximally at 15 min by treatment with granulocyte-colony stimulating factor (G-CSF) but not with interlevkin-3 (IL-3) or colony-stimulating factor-1 (macrophage-colony stimulating factor (CSF-1 (M-CSF)). The phosphorylation of this protein, designated 21.5/6.0, was unaffected by a series of antiproliferative agents [32]. These findings suggested that the 21.5/6.0 phosphoprotein may be involved in specific G-CSF-mediated biological responses such as activation and/or differentiation. We sought to characterize this 21.5/6.0 by a novel combination of 2-D SDS-PAGE and hydroxyapatite (HTP)-chromatography. Amino acid sequence determination of 21.5/6.0 revealed it to share a high level of homology with copper/zinc superoxide dismutase (Cu/Zn-SOD), indicating that a Cu/Zn-SOD is phosphorylated following treatment with G-CSF. This is the first report of the phosphorylation and possible involvement of Cu/Zn-SOD protein in granulocyte activation/differentiation events. In addition, Cu/Zn-SOD levels and activity were diminished by G-CSF but not IL-3 treatment. This new protocol combining 2-D SDS-PAGE and HTP-chromatography allows the characterization of low abundance phosphoproteins involved in the cellular responses to G-CSF and presumably to other cytokines/growth factors.
Language eng
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2001, WILEY-VCH Verlag GmbH
Persistent URL http://hdl.handle.net/10536/DRO/DU:30009181

Document type: Journal Article
Collection: School of Medicine
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