pubmed-article:18081036 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C0007620 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C2749595 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C1413357 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
pubmed-article:18081036 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:18081036 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:18081036 | pubmed:dateCreated | 2007-12-26 | lld:pubmed |
pubmed-article:18081036 | pubmed:abstractText | Effective stimulation of NF-kappaB in T cells following TCR ligation requires the activity of caspase-8. The active caspase-8 complex includes the paracaspase, MALT1, and Bcl-10, which connect to the NF-kappaB pathway. It has been less clear what regulates the level of caspase-8 activity during T cell activation. A likely candidate is cellular FLIP (c-FLIP), an enzymatically inert caspase-8 homologue. Two alternatively spliced forms of c-FLIP exist, a long form (c-FLIP(L)) and a short-form (c-FLIP(S)). The latter lacks the C-terminal caspase-like domain. c-FLIP(L) can heterodimerize with and activate caspase-8 through an activation loop in the C terminus of c-FLIP(L). Here we show that, in contrast to c-FLIP(L), c-FLIP(S) inhibits activation of caspase-8 in T cells, and consequently reduces recruitment of MALT1 and Bcl-10 to the active caspase complex. This results in reduced activity of NF-kappaB. Consequently, T cells from c-FLIP(S)-transgenic mice undergo more rapid cell death both spontaneously and after activation. The findings suggest that c-FLIP(S) functions to reduce the expansion of T cells during an immune response. | lld:pubmed |
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pubmed-article:18081036 | pubmed:language | eng | lld:pubmed |
pubmed-article:18081036 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18081036 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18081036 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18081036 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18081036 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18081036 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18081036 | pubmed:month | Jan | lld:pubmed |
pubmed-article:18081036 | pubmed:issn | 0014-2980 | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:RuxA HAH | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:BuddRalph CRC | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:FortnerKaren... | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:HustonGailG | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:RussellJennif... | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:HolochDanielD | lld:pubmed |
pubmed-article:18081036 | pubmed:author | pubmed-author:Hinshaw-Makep... | lld:pubmed |
pubmed-article:18081036 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18081036 | pubmed:volume | 38 | lld:pubmed |
pubmed-article:18081036 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18081036 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18081036 | pubmed:pagination | 54-63 | lld:pubmed |
pubmed-article:18081036 | pubmed:dateRevised | 2011-5-12 | lld:pubmed |
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pubmed-article:18081036 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18081036 | pubmed:articleTitle | c-FLIP(S) reduces activation of caspase and NF-kappaB pathways and decreases T cell survival. | lld:pubmed |