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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1999-5-20
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pubmed:abstractText |
Cross-linking of CD45 induced capping and physical sequestration from CD22 leading to an increase in tyrosine phosphorylation of CD22 and SHP-1 recruitment. Additionally, CD22 isolated from a CD45-deficient B cell line exhibited increased basal/inducible tyrosine phosphorylation and enhanced recruitment of SHP-1 compared with CD22 isolated from CD45-positive parental cells. Subsequent experiments were performed to determine whether enhanced SHP-1 recruitment to CD22 is responsible for attenuation of receptor-mediated Ca2+ responses in CD45-deficient cells. Catalytically inactive SHP-1 expressed in CD45-deficient cells interacted with CD22 and decreased phosphatase activity in CD22 immunoprecipitates to levels that were comparable to those in CD45-positive cells. Expression of catalytically inactive SHP-1 restored intracellular mobilization of Ca2+ in response to MHC class II cross-linking, but did not affect B cell Ag receptor- or class II-mediated Ca2+ influx from the extracellular space. These results indicate that CD45 regulates tyrosine phosphorylation of CD22 and binding of SHP-1. The data further indicate that enhanced recruitment and activation of SHP-1 in CD45-deficient cells affect intracellular mobilization of Ca2+, but are not responsible for abrogation of receptor-mediated Ca2+ influx from the extracellular space.
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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/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD22,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD45,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Cd22 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
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/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/SH2 Domain-Containing Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/lyn protein-tyrosine kinase,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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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 |
5278-86
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:10228003-Animals,
pubmed-meshheading:10228003-Antigens, CD,
pubmed-meshheading:10228003-Antigens, CD22,
pubmed-meshheading:10228003-Antigens, CD45,
pubmed-meshheading:10228003-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:10228003-Calcium Signaling,
pubmed-meshheading:10228003-Catalysis,
pubmed-meshheading:10228003-Cell Adhesion Molecules,
pubmed-meshheading:10228003-Intracellular Fluid,
pubmed-meshheading:10228003-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10228003-Lectins,
pubmed-meshheading:10228003-Lymphoma, B-Cell,
pubmed-meshheading:10228003-Mice,
pubmed-meshheading:10228003-Phosphorylation,
pubmed-meshheading:10228003-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:10228003-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:10228003-Protein Tyrosine Phosphatases,
pubmed-meshheading:10228003-Receptors, Antigen, B-Cell,
pubmed-meshheading:10228003-SH2 Domain-Containing Protein Tyrosine Phosphatases,
pubmed-meshheading:10228003-Tumor Cells, Cultured,
pubmed-meshheading:10228003-Tyrosine,
pubmed-meshheading:10228003-src Homology Domains,
pubmed-meshheading:10228003-src-Family Kinases
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pubmed:year |
1999
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pubmed:articleTitle |
CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1.
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pubmed:affiliation |
Department of Microbiology, Division of Developmental and Clinical Immunology, University of Alabama, Birminghamp55294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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