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Titolo:
Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells
Autore:
Csar, XF; Wilson, NJ; Strike, P; Sparrow, L; McMahon, KA; Ward, AC; Hamilton, JA;
Indirizzi:
Univ Melbourne, Royal Melbourne Hosp, Arthritis & Inflammat Res Ctr, Dept Med, Parkville, Vic 3050, Australia Univ Melbourne Parkville Vic Australia3050 arkville, Vic 3050, Australia Commonwealth Sci & Ind Res Org, Div Hlth Sci & Nutr, Clayton, Vic, Australia Commonwealth Sci & Ind Res Org Clayton Vic Australia ton, Vic, Australia Ludwig Inst Canc Res, Melbourne, Vic, Australia Ludwig Inst Canc Res Melbourne Vic Australia , Melbourne, Vic, Australia
Titolo Testata:
PROTEOMICS
fascicolo: 3, volume: 1, anno: 2001,
pagine: 435 - 443
SICI:
1615-9853(200103)1:3<435:CSDIPA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-NECROSIS-FACTOR; FACTOR-RECEPTOR; TYROSINE PHOSPHORYLATION; HEMATOPOIETIC-CELLS; SIGNAL-TRANSDUCTION; GENE-EXPRESSION; G-CSF; PROTEINS; ACTIVATION; DIFFERENTIATION;
Keywords:
superoxide dismutase; granulocyte-colony stimulating factor granulocyte-colony stimulating factor 1 macrophage-colony stimulating factor; two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis; protein phosphorylation; protein purification; hydroxyapatite; microsequencing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Csar, XF Univ Melbourne, Royal Melbourne Hosp, Arthritis & Inflammat Res Ctr, Dept Med, Parkville, Vic 3050, Australia Univ Melbourne Parkville Vic Australia 3050 Vic 3050, Australia
Citazione:
X.F. Csar et al., "Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells", PROTEOMICS, 1(3), 2001, pp. 435-443

Abstract

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-I (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 of21.5/6.0 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 CuZn-SOD protein in granulocyte activation/differentiation events. In addition, Cu/Zn-SOD levels and activity werediminished 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 03:45:49