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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1997-4-18
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pubmed:abstractText |
Interleukin 4 (IL-4) is a potent cytokine produced by T cells and to a lesser extent by tumor-associated natural killer cells, basophils, and mast cells. IL-4 treatment of T cells and macrophages leads to augmentation of their cytotoxic activity. In human B cells, IL-4 is a potent stimulator of Ig class switching from IgM to IgE. The diverse biological responses induced by IL-4 are mediated through a high affinity receptor complex (IL-4R). Although a wealth of information has accumulated regarding IL-4R, the exact mechanisms of IL-4R-mediated signaling pathways in human B cells are not well defined. In an attempt to characterize the IL-4-induced signals in human B cells, we have found that IL-4 treatment induced rapid dephosphorylation of the 85-kDa regulatory subunit of phosphatidylinositol 3-kinase. To identify the protein-tyrosine phosphatase involved in the IL-4-mediated dephosphorylation, we performed Western blot analysis using monoclonal antibodies specific to protein-tyrosine phosphatases. Upon IL-4 treatment, SHP-1 was specifically translocated to the cellular membrane fraction. Furthermore, immunoprecipitation studies revealed that SHP-1 could be specifically coimmunoprecipitated with the IL-4R as well as with phosphatidylinositol 3-kinase (p85). Collectively, our observations suggest that in addition to protein phosphorylation, protein tyrosine dephosphorylation may play a role in the IL-4-induced signaling pathways.
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pubmed:grant |
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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/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7927-31
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9065461-Antigens, CD,
pubmed-meshheading:9065461-B-Lymphocytes,
pubmed-meshheading:9065461-Biological Transport,
pubmed-meshheading:9065461-Cell Membrane,
pubmed-meshheading:9065461-Humans,
pubmed-meshheading:9065461-Interleukin-4,
pubmed-meshheading:9065461-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9065461-Kinetics,
pubmed-meshheading:9065461-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:9065461-Phosphorylation,
pubmed-meshheading:9065461-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:9065461-Protein Binding,
pubmed-meshheading:9065461-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:9065461-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:9065461-Protein Tyrosine Phosphatases,
pubmed-meshheading:9065461-Receptors, Interleukin,
pubmed-meshheading:9065461-Receptors, Interleukin-4,
pubmed-meshheading:9065461-Recombinant Proteins,
pubmed-meshheading:9065461-Signal Transduction,
pubmed-meshheading:9065461-Tumor Cells, Cultured,
pubmed-meshheading:9065461-Tyrosine
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pubmed:year |
1997
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pubmed:articleTitle |
Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells.
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pubmed:affiliation |
Department of Medicine, The Johns Hopkins University School of Medicine, Asthma and Allergy Center, Baltimore, Maryland 21224, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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