| pubmed-article:10716728 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C1332709 | lld:lifeskim |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10716728 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:10716728 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10716728 | pubmed:dateCreated | 2000-4-24 | lld:pubmed |
| pubmed-article:10716728 | pubmed:abstractText | Protein kinase C-theta (PKCtheta) is a Ca(2+)-independent member of the PKC family that is selectively expressed in skeletal muscle and T lymphocytes and plays an important role in T cell activation. However, the molecular basis for the important functions of PKCtheta in T cells and the manner in which it becomes coupled to the T cell receptor-signaling machinery are unknown. We addressed the functional relationship between PKCtheta and CD28 costimulation, which plays an essential role in T cell receptor-mediated IL-2 production. Here, we provide evidence that PKCtheta is functionally coupled to CD28 costimulation by virtue of its selective ability to activate the CD28RE/activator protein-1 (AP-1) element in the IL-2 gene promoter. First, CD28 costimulation enhanced the membrane translocation and catalytic activation of PKCtheta. Second, among several PKC isoforms, PKCtheta was the only one capable of activating NF-kappaB or CD28RE/AP-1 reporters in T cells (but not in 293T cells). Third, wild-type PKCtheta synergized with CD28/CD3 signals to activate CD28RE/AP-1. In addition, PKCtheta selectively synergized with Tat to activate a CD28RE/AP-1 reporter. Fourth, CD3/CD28-induced CD28RE/AP-1 activation and NF-kappaB nuclear translocation were blocked by a selective PKCtheta inhibitor. Last, PKCtheta-mediated activation of the same reporter was inhibited by the proteasome inhibitor MG132 (which blocks IkappaB degradation) and was found to involve IkappaB-kinase beta. These findings identify a unique PKCtheta-mediated pathway for the costimulatory action of CD28, which involves activation of the IkappaB-kinase beta/IkappaB/NF-kappaB-signaling cascade. | lld:pubmed |
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| pubmed-article:10716728 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10716728 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10716728 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10716728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10716728 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10716728 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10716728 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10716728 | pubmed:author | pubmed-author:AltmanAA | lld:pubmed |
| pubmed-article:10716728 | pubmed:author | pubmed-author:VillalbaMM | lld:pubmed |
| pubmed-article:10716728 | pubmed:author | pubmed-author:EnglundNN | lld:pubmed |
| pubmed-article:10716728 | pubmed:author | pubmed-author:CoudronniereN... | lld:pubmed |
| pubmed-article:10716728 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10716728 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10716728 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10716728 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10716728 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10716728 | pubmed:pagination | 3394-9 | lld:pubmed |
| pubmed-article:10716728 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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