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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2002-7-23
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pubmed:abstractText |
Erythropoietin (Epo)-induced glycosylphosphatidylinositol (GPI) hydrolysis was previously described to be correlated with phospholipase C-gamma 2 (PLC-gamma2) activation. Here, we analyzed the involvement of phosphatidylinositol (PtdIns) 3-kinase in GPI hydrolysis through PLC-gamma2 tyrosine phosphorylation in response to Epo in FDC-P1 cells transfected with a wild type (WT) erythropoietin-receptor (Epo-R). We showed that phosphatidylinositol 3-kinase (PtdIns 3-kinase) inhibitor LY294002 inhibits Epo-induced hydrolysis of endogenous GPI and Epo-induced PLC-gamma2 tyrosine phosphorylation in a dose-dependent manner. Wortmannin, another PtdIns 3-kinase inhibitor, also suppressed Epo-induced PLC-gamma2 tyrosine phosphorylation. We also present evidence that PLC-gamma2 translocation to the membrane fraction on Epo stimulation is completely inhibited by LY294002. Upon Epo stimulation, the tyrosine-phosphorylated PLC-gamma2 was found to be associated with the tyrosine-phosphorylated Grb2-associated binder (GAB)2, SHC and SHP2 proteins. LY294002 cell preincubation did not affect GAB2, SHC and SHP2 tyrosine phosphorylation but inhibited the binding of PLC-gamma2 to GAB2 and SHP2. Taken together, these results show that PtdIns 3-kinase controls Epo-induced GPI hydrolysis through PLC-gamma2.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/GAB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/microfilarial sheath protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0898-6568
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2002 Elsevier Science Inc.
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
869-78
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12135708-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12135708-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:12135708-Animals,
pubmed-meshheading:12135708-Cell Differentiation,
pubmed-meshheading:12135708-Cell Division,
pubmed-meshheading:12135708-Cell Membrane,
pubmed-meshheading:12135708-Cells, Cultured,
pubmed-meshheading:12135708-Dose-Response Relationship, Drug,
pubmed-meshheading:12135708-Enzyme Inhibitors,
pubmed-meshheading:12135708-Erythrocytes,
pubmed-meshheading:12135708-Erythroid Precursor Cells,
pubmed-meshheading:12135708-Erythropoietin,
pubmed-meshheading:12135708-Glycosylphosphatidylinositols,
pubmed-meshheading:12135708-Helminth Proteins,
pubmed-meshheading:12135708-Humans,
pubmed-meshheading:12135708-Hydrolysis,
pubmed-meshheading:12135708-Isoenzymes,
pubmed-meshheading:12135708-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:12135708-Phospholipase C gamma,
pubmed-meshheading:12135708-Phosphoproteins,
pubmed-meshheading:12135708-Phosphorylation,
pubmed-meshheading:12135708-Protein Binding,
pubmed-meshheading:12135708-Protein Transport,
pubmed-meshheading:12135708-Proteins,
pubmed-meshheading:12135708-Shc Signaling Adaptor Proteins,
pubmed-meshheading:12135708-Subcellular Fractions,
pubmed-meshheading:12135708-Transfection,
pubmed-meshheading:12135708-Type C Phospholipases,
pubmed-meshheading:12135708-Tyrosine
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pubmed:year |
2002
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pubmed:articleTitle |
Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells.
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pubmed:affiliation |
Laboratoire de Biochimie, CNRS, FRE 2534, IFR 53 Biomolécules, UFR Sciences Exactes et Naturelles, BP 1039, Université de Reims Champagne-Ardenne, 51687 Reims Cedex 2, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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