| Literature DB >> 23770286 |
Abstract
IAPs are a group of regulatory proteins that are structurally related. Their conserved homologues have been identified in various organisms. In human, eight IAP members have been recognized based on baculoviral IAP repeat (BIR) domains. IAPs are key regulators of apoptosis, cytokinesis and signal transduction. The antiapoptotic property of IAPs depends on their professional role for caspases. IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms. IAPs impede apoptotic process via membrane receptor-dependent (extrinsic) cascade and mitochondrial dependent (intrinsic) pathway. IAP-mediated apoptosis affects the progression of liver diseases. Therapeutic options of liver diseases may depend on the understanding toward mechanisms of the IAP-mediated apoptosis.Entities:
Keywords: APAF-1; ASO; Antisense oligonucleotides; BIR; Baculovirus IAP repeat; CD2; CDK4; Caspase; FLICE-inhibitory proteins; FLIPs; HCC; HSP90; Hepatic apoptosis; IAPs; NF-κB; RIP1; Rb; Second mitochondria-derived activator of caspase/direct inhibitor of apoptosis-binding protein with low pI; Smac/Diablo; TNF; TNF receptor-associated factor 2; TRAF2; apoptotic protease activating factor 1; cluster of differentiation 2; cyclin dependent kinase 4; heat shock protein 90; hepatocellular carcinoma; inhibitor of apoptosis proteins; nuclear factor kappa-light-chain-enhancer of activated B cells; receptor-interacting protein 1; retinoblastoma; tumor necrosis factor
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Year: 2013 PMID： 23770286 DOI： 10.1016/j.cellsig.2013.06.003
Source DB: PubMed Journal: Cell Signal ISSN： 0898-6568 Impact factor: 4.315