Journal
JOURNAL OF IMMUNOLOGY
Volume 185, Issue 6, Pages 3127-3130Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1001512
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Funding
- National Institutes of Health [AR056296, AI088177]
- Cancer Center Support Grant [CCSG 2 P30 CA 21765]
- American Lebanese Syrian Associated Charities
- Fund for Scientific Research-Flanders
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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. The Journal of Immunology, 2010, 185: 3127-3130.
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