| pubmed-article:10082557 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C1413227 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C1335283 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C1705637 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10082557 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:10082557 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10082557 | pubmed:dateCreated | 1999-4-20 | lld:pubmed |
| pubmed-article:10082557 | pubmed:abstractText | The negative regulation of T- or B-cell antigen receptor signaling by CD5 was proposed based on studies of thymocytes and peritoneal B-1a cells from CD5-deficient mice. Here, we show that CD5 is constitutively associated with phosphotyrosine phosphatase activity in Jurkat T cells. CD5 was found associated with the Src homology 2 (SH2) domain containing hematopoietic phosphotyrosine phosphatase SHP-1 in both Jurkat cells and normal phytohemagglutinin-expanded T lymphoblasts. This interaction was increased upon T-cell receptor (TCR)-CD3 cell stimulation. CD5 co-cross-linking with the TCR-CD3 complex down-regulated the TCR-CD3-increased Ca2+ mobilization in Jurkat cells. In addition, stimulation of Jurkat cells or normal phytohemagglutinin-expanded T lymphoblasts through TCR-CD3 induced rapid tyrosine phosphorylation of several protein substrates, which was substantially diminished after CD5 cross-linking. The CD5-regulated substrates included CD3zeta, ZAP-70, Syk, and phospholipase Cgammal but not the Src family tyrosine kinase p56(lck). By mutation of all four CD5 intracellular tyrosine residues to phenylalanine, we found the membrane-proximal tyrosine at position 378, which is located in an immunoreceptor tyrosine-based inhibitory (ITIM)-like motif, crucial for SHP-1 association. The F378 point mutation ablated both SHP-1 binding and the down-regulating activity of CD5 during TCR-CD3 stimulation. These results suggest a critical role of the CD5 ITIM-like motif, which by binding to SHP-1 mediates the down-regulatory activity of this receptor. | lld:pubmed |
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| pubmed-article:10082557 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10082557 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10082557 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10082557 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10082557 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10082557 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10082557 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10082557 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:10082557 | pubmed:author | pubmed-author:BrownB IBI | lld:pubmed |
| pubmed-article:10082557 | pubmed:author | pubmed-author:KannerS BSB | lld:pubmed |
| pubmed-article:10082557 | pubmed:author | pubmed-author:WhitneyG SGS | lld:pubmed |
| pubmed-article:10082557 | pubmed:author | pubmed-author:AruffoA AAA | lld:pubmed |
| pubmed-article:10082557 | pubmed:author | pubmed-author:Perez-VillarJ... | lld:pubmed |
| pubmed-article:10082557 | pubmed:author | pubmed-author:HewgillD HDH | lld:pubmed |
| pubmed-article:10082557 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10082557 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:10082557 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10082557 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10082557 | pubmed:pagination | 2903-12 | lld:pubmed |
