| pubmed-article:20713892 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C2936529 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C1306235 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C1424250 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C1538577 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C1826433 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C0152060 | lld:lifeskim |
| pubmed-article:20713892 | lifeskim:mentions | umls-concept:C0205154 | lld:lifeskim |
| pubmed-article:20713892 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:20713892 | pubmed:dateCreated | 2010-9-3 | lld:pubmed |
| pubmed-article:20713892 | pubmed:abstractText | Caspase-mediated cleavage of the DNA damage sensor poly(ADP-ribose) polymerase 1 (PARP1) is a hallmark of apoptosis. However, it remains unclear whether PARP1 is processed during pyroptosis, a specialized cell-death program that occurs upon activation of caspase-1 in inflammasome complexes. In this article, we show that activation of the Nlrp3 and Nlrc4 inflammasomes induces processing of full-length PARP1 into a fragment of 89 kDa in a stimulus-dependent manner. Macrophages deficient for caspase-1 and those lacking the inflammasome adaptors Nlrp3, Nlrc4, and ASC were highly resistant to cleavage, whereas macrophages lacking the downstream inflammasome effector caspase-7 were partially protected. A modest, but statistically significant, reduction in Nlrp3 inflammasome-induced pyroptosis was observed in PARP1 knockout macrophages. Thus, protease-mediated inactivation of PARP1 is a shared feature of apoptotic, necrotic, and pyroptotic cells. | lld:pubmed |
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| pubmed-article:20713892 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20713892 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20713892 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:20713892 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20713892 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:20713892 | pubmed:issn | 1550-6606 | lld:pubmed |
| pubmed-article:20713892 | pubmed:author | pubmed-author:LamkanfiMoham... | lld:pubmed |
| pubmed-article:20713892 | pubmed:author | pubmed-author:KannegantiThi... | lld:pubmed |
| pubmed-article:20713892 | pubmed:author | pubmed-author:MalireddiR... | lld:pubmed |
| pubmed-article:20713892 | pubmed:author | pubmed-author:IppaguntaSiri... | lld:pubmed |
| pubmed-article:20713892 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20713892 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:20713892 | pubmed:volume | 185 | lld:pubmed |
| pubmed-article:20713892 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20713892 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20713892 | pubmed:pagination | 3127-30 | lld:pubmed |
| pubmed-article:20713892 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
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| pubmed-article:20713892 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20713892 | pubmed:articleTitle | Cutting edge: proteolytic inactivation of poly(ADP-ribose) polymerase 1 by the Nlrp3 and Nlrc4 inflammasomes. | lld:pubmed |
| pubmed-article:20713892 | pubmed:affiliation | Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105-2794, USA. | lld:pubmed |
| pubmed-article:20713892 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20713892 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20713892 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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