pubmed-article:1551921 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1551921 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
pubmed-article:1551921 | lifeskim:mentions | umls-concept:C0021547 | lld:lifeskim |
pubmed-article:1551921 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
pubmed-article:1551921 | lifeskim:mentions | umls-concept:C0300926 | lld:lifeskim |
pubmed-article:1551921 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:1551921 | lifeskim:mentions | umls-concept:C0702240 | lld:lifeskim |
pubmed-article:1551921 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:1551921 | pubmed:dateCreated | 1992-4-28 | lld:pubmed |
pubmed-article:1551921 | pubmed:abstractText | Perturbation of the T cell antigen-specific receptor leads to a series of signaling events that includes a rapid increase in phosphoinositide hydrolysis, intracellular Ca2+, and tyrosine phosphorylation. We have examined the function of tyrosine phosphorylation in isolation by introducing the v-src tyrosine kinase into a T cell hybridoma. T cell receptor-mediated increases in phosphoinositide hydrolysis and, in particular the generation of inositol 1,4,5-trisphosphate, were comparable between v-src+ and v-src- cells. Unexpectedly, the v-src+ cells exhibited spontaneously elevated intracellular Ca2+ and exaggerated Ca2+ increases when stimulated via the T cell receptor. The enhanced Ca2+ response was not due to tyrosine phosphorylation of the T cell receptor itself, since the phenotype was evident in T cell receptor zeta chain-/v-src+ cells as well. These results demonstrate that an active protein tyrosine kinase can markedly affect intracellular Ca2+ handling by a process independent of inositol 1,4,5-trisphosphate production and T cell receptor tyrosine phosphorylation and raise the possibility that tyrosine kinases may directly regulate T cell receptor-mediated changes in intracellular Ca2+. | lld:pubmed |
pubmed-article:1551921 | pubmed:language | eng | lld:pubmed |
pubmed-article:1551921 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1551921 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1551921 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1551921 | pubmed:month | Apr | lld:pubmed |
pubmed-article:1551921 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1551921 | pubmed:author | pubmed-author:YamadaHH | lld:pubmed |
pubmed-article:1551921 | pubmed:author | pubmed-author:LECHWW | lld:pubmed |
pubmed-article:1551921 | pubmed:author | pubmed-author:O'SheaJ JJJ | lld:pubmed |
pubmed-article:1551921 | pubmed:author | pubmed-author:AshwellJ DJD | lld:pubmed |
pubmed-article:1551921 | pubmed:author | pubmed-author:NiklinskaB... | lld:pubmed |
pubmed-article:1551921 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1551921 | pubmed:day | 5 | lld:pubmed |
pubmed-article:1551921 | pubmed:volume | 267 | lld:pubmed |
pubmed-article:1551921 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1551921 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1551921 | pubmed:pagination | 7154-9 | lld:pubmed |
pubmed-article:1551921 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:1551921 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1551921 | pubmed:articleTitle | Tyrosine kinase-regulated and inositol phosphate-independent Ca2+ elevation and mobilization in T cells. | lld:pubmed |
pubmed-article:1551921 | pubmed:affiliation | Immune Cell Biology Section, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
pubmed-article:1551921 | pubmed:publicationType | Journal Article | lld:pubmed |
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