| pubmed-article:8397196 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8397196 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:8397196 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:8397196 | lifeskim:mentions | umls-concept:C0065344 | lld:lifeskim |
| pubmed-article:8397196 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8397196 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:8397196 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:8397196 | pubmed:issue | 27 | lld:pubmed |
| pubmed-article:8397196 | pubmed:dateCreated | 1993-10-20 | lld:pubmed |
| pubmed-article:8397196 | pubmed:abstractText | The relative levels of phosphatidylinositol-3'-kinase (PI3K) activity were measured in interleukin-2 (IL-2)-dependent helper (HT-2) and cytolytic (CTLL-2) T-cell clones that had been stably transfected with expression plasmids encoding either the normal p56-Lck kinase or a mutant version of this kinase, p56-Lck(Y505F), that has constitutively high levels of kinase activity. Stimulation of untransfected T-cells or of transfected T-cells containing increased levels of normal p56-Lck resulted in an approximate doubling of the relative amounts of total cellular PI3K activity. In contrast, T-cells producing the activated version of p56-Lck contained levels of PI3K activity comparable to or slightly higher than those found IL-2-stimulated control cells, even in the absence of IL-2. Assessments of the relative levels of PI3K activity in immunoprecipitates prepared with the use of anti-phosphotyrosine-specific antibodies revealed constitutively high levels of anti-phosphotyrosine-immunoprecipitable PI3K activity in T-cells containing p56-Lck(Y505F), as opposed to T-cells containing normal p56-Lck where increases in anti-PY-immunoprecipitable PI3K activity were IL-2-inducible. IL-2 stimulation of T-cells containing the normal p56-Lck kinase resulted in marked increases in the relative amounts of PI3K activity and p85 that were coimmunoprecipitated when using anti-p56-Lck antibodies. In contrast, PI3K activity and the p85 subunit of PI3K could be coimmunoprecipitated from T-cells producing the activated p56-Lck(Y505F) kinase even in the absence of IL-2 stimulation, implying constitutive association of PI3K with the activated Lck kinase. Taken together with previous studies showing that IL-2 induces rapid increases in the activities of both p56-Lck and PI3K in T-cells, these findings suggest that p56-Lck lies immediately upstream of PI3K in a signal transduction cascade initiated by the binding of IL-2 to its specific receptor on T-lymphocytes. | lld:pubmed |
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| pubmed-article:8397196 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8397196 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8397196 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8397196 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8397196 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8397196 | pubmed:author | pubmed-author:ReedJ CJC | lld:pubmed |
| pubmed-article:8397196 | pubmed:author | pubmed-author:TorigoeTT | lld:pubmed |
| pubmed-article:8397196 | pubmed:author | pubmed-author:GaultonG NGN | lld:pubmed |
| pubmed-article:8397196 | pubmed:author | pubmed-author:MeridaII | lld:pubmed |
| pubmed-article:8397196 | pubmed:author | pubmed-author:TaichmanRR | lld:pubmed |
| pubmed-article:8397196 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8397196 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:8397196 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8397196 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8397196 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8397196 | pubmed:pagination | 20031-6 | lld:pubmed |
| pubmed-article:8397196 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8397196 | pubmed:meshHeading | pubmed-meshheading:8397196-... | lld:pubmed |
| pubmed-article:8397196 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8397196 | pubmed:articleTitle | Evidence that protein tyrosine kinase p56-Lck regulates the activity of phosphatidylinositol-3'-kinase in interleukin-2-dependent T-cells. | lld:pubmed |
| pubmed-article:8397196 | pubmed:affiliation | Department of Pathology & Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104. | lld:pubmed |
| pubmed-article:8397196 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8397196 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8397196 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8397196 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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