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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0033681,
umls-concept:C0033684,
umls-concept:C0041485,
umls-concept:C0185117,
umls-concept:C0205217,
umls-concept:C1150423,
umls-concept:C1155003,
umls-concept:C1274040,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2911684
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pubmed:issue |
5
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pubmed:dateCreated |
1999-4-14
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pubmed:abstractText |
The Src-homology domain 2 (SH2)-containing cytoplasmic tyrosine phosphatase, SHP-1 (SH2-containing protein tyrosine phosphatase-1), interacts with several B cell surface and intracellular signal transduction molecules through its SH2 domains. Mice with the motheaten and viable motheaten mutations are deficient in SHP-1 and lack most mature B cells. To define the role of SHP-1 in mature B cells, we expressed phosphatase-inactive SHP-1 (C453S) in a mature B cell lymphoma line. SHP-1 (C453S) retains the ability to bind to both substrates and appropriate tyrosine-phosphorylated proteins and therefore can compete with the endogenous wild-type enzyme. We found that B cells expressing SHP-1 (C453S) demonstrated enhanced and prolonged tyrosine phosphorylation of proteins with molecular masses of 110, 70, and 55-60 kDa after stimulation with anti-mouse IgG. The tyrosine kinase Syk was hyperphosphorylated and hyperactive in B cells expressing SHP-1 (C453S). SHP-1 and Syk were coimmunoprecipitated from wild-type K46 cells, K46 SHP-1 (C453S) cells, and splenic B cells, and SHP-1 dephosphorylated Syk. Cells expressing SHP-1 (C453S) showed increased Ca2+ mobilization, extracellular signal-regulated kinase activation, and homotypic adhesion after B cell Ag receptor engagement. Thus, SHP-1 regulates multiple early and late events in B lymphocyte activation.
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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 |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
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/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase,
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 |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
162
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2717-24
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:10072516-Animals,
pubmed-meshheading:10072516-B-Lymphocytes,
pubmed-meshheading:10072516-Enzyme Precursors,
pubmed-meshheading:10072516-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10072516-Lymphocyte Activation,
pubmed-meshheading:10072516-Mice,
pubmed-meshheading:10072516-Mice, Inbred C57BL,
pubmed-meshheading:10072516-Phosphorylation,
pubmed-meshheading:10072516-Protein Phosphatase 1,
pubmed-meshheading:10072516-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:10072516-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:10072516-Protein Tyrosine Phosphatases,
pubmed-meshheading:10072516-Protein-Tyrosine Kinases,
pubmed-meshheading:10072516-Rabbits,
pubmed-meshheading:10072516-Receptors, Antigen, B-Cell,
pubmed-meshheading:10072516-Signal Transduction,
pubmed-meshheading:10072516-Tumor Cells, Cultured,
pubmed-meshheading:10072516-Tyrosine
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pubmed:year |
1999
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pubmed:articleTitle |
Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation.
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pubmed:affiliation |
Departments ofPathology and Molecular Microbiology and Medicine, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110, 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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