Source:http://linkedlifedata.com/resource/pubmed/id/11680888
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-10-29
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Durapatite,
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte Colony-Stimulating...,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteome,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1615-9853
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
435-43
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11680888-Animals,
pubmed-meshheading:11680888-Cell Line,
pubmed-meshheading:11680888-Chromatography,
pubmed-meshheading:11680888-Durapatite,
pubmed-meshheading:11680888-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:11680888-Granulocyte Colony-Stimulating Factor,
pubmed-meshheading:11680888-Interleukin-3,
pubmed-meshheading:11680888-Isoelectric Point,
pubmed-meshheading:11680888-Mice,
pubmed-meshheading:11680888-Molecular Weight,
pubmed-meshheading:11680888-Phosphoproteins,
pubmed-meshheading:11680888-Phosphorylation,
pubmed-meshheading:11680888-Proteome,
pubmed-meshheading:11680888-Superoxide Dismutase
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pubmed:year |
2001
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pubmed:articleTitle |
Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells.
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pubmed:affiliation |
University of Melbourne, Arthritis and Inflammation Research Centre, Department of Medicine, Royal Melbourne Hospital, Parkville 3050, Victoria, Australia. xfc@unimelb.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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