| pubmed-article:7646452 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C0059249 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C0103404 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:7646452 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:7646452 | pubmed:dateCreated | 1995-9-20 | lld:pubmed |
| pubmed-article:7646452 | pubmed:abstractText | In order to understand how signal transduction occurs during T cell activation, it is necessary to identify the key regulatory molecules whose function is influenced by phosphorylation. Annexins II (A-II) and V (A-V) belong to a large family of Ca(2+)-dependent phospholipid-binding proteins. Among many putative functions, annexins may be involved in signal transduction during cellular proliferation and differentiation. In the present study we show that A-II is phosphorylated in vivo in the Jurkat human T cell line. Indeed, A-II is phosphorylated after stimulation by phorbol myristate acetate and on serine residues after T cell antigen receptor (TcR) stimulation. In cytosol from Jurkat cells, A-II is phosphorylated only by Ca2+/phospholipid-stimulated kinases such as Ca(2+)-dependent protein kinases C (cPKCs). A-V inhibits the phosphorylation of A-II and other substrates of cPKCs and has no effect on kinases activated only by phospholipids. In conclusion, A-II is phosphorylated both in vitro and in vivo in Jurkat cells, and may play a role as a substrate during signal transduction in lymphocytes via the TcR through the PKC pathway. On the other hand, A-V could act as a potent modulator of cPKCs in Jurkat cells. | lld:pubmed |
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| pubmed-article:7646452 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7646452 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7646452 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7646452 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7646452 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7646452 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7646452 | pubmed:author | pubmed-author:Russo-MarieFF | lld:pubmed |
| pubmed-article:7646452 | pubmed:author | pubmed-author:DuboisTT | lld:pubmed |
| pubmed-article:7646452 | pubmed:author | pubmed-author:RothhutBB | lld:pubmed |
| pubmed-article:7646452 | pubmed:author | pubmed-author:OudinetJ PJP | lld:pubmed |
| pubmed-article:7646452 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7646452 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7646452 | pubmed:volume | 310 ( Pt 1) | lld:pubmed |
| pubmed-article:7646452 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7646452 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7646452 | pubmed:pagination | 243-8 | lld:pubmed |
| pubmed-article:7646452 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7646452 | pubmed:meshHeading | pubmed-meshheading:7646452-... | lld:pubmed |
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