| pubmed-article:10228003 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10228003 | lifeskim:mentions | umls-concept:C1384543 | lld:lifeskim |
| pubmed-article:10228003 | lifeskim:mentions | umls-concept:C0054961 | lld:lifeskim |
| pubmed-article:10228003 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:10228003 | lifeskim:mentions | umls-concept:C1332708 | lld:lifeskim |
| pubmed-article:10228003 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:10228003 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10228003 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:10228003 | pubmed:dateCreated | 1999-5-20 | lld:pubmed |
| pubmed-article:10228003 | 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. | lld:pubmed |
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| pubmed-article:10228003 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10228003 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:10228003 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10228003 | pubmed:month | May | lld:pubmed |
| pubmed-article:10228003 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:10228003 | pubmed:author | pubmed-author:GreenS JSJ | lld:pubmed |
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| pubmed-article:10228003 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10228003 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10228003 | pubmed:volume | 162 | lld:pubmed |
| pubmed-article:10228003 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10228003 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10228003 | pubmed:pagination | 5278-86 | lld:pubmed |
| pubmed-article:10228003 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:10228003 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10228003 | pubmed:articleTitle | CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1. | lld:pubmed |
| pubmed-article:10228003 | pubmed:affiliation | Department of Microbiology, Division of Developmental and Clinical Immunology, University of Alabama, Birminghamp55294, USA. | lld:pubmed |
| pubmed-article:10228003 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10228003 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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