XIAP discriminates between type I and type II FAS-induced apoptosis
Details
Publication Year 2009-08-20,Volume 460,Issue #7258,Page 1035-U128
Journal Title
NATURE
Publication Type
Journal Article
Abstract
FAS (also called APO-1 and CD95) and its physiological ligand, FASL, regulate apoptosis of unwanted or dangerous cells, functioning as a guardian against autoimmunity and cancer development(1-4). Distinct cell types differ in the mechanisms by which the 'death receptor' FAS triggers their apoptosis(1-4). In type I cells, such as lymphocytes, activation of 'effector caspases' by FAS-induced activation of caspase-8 suffices for cell killing, whereas in type II cells, including hepatocytes and pancreatic beta-cells, caspase cascade amplification through caspase-8-mediated activation of the proapoptotic BCL-2 family member BID (BH3 interacting domain death agonist) 5 is essential(6-8). Here we show that loss of XIAP (X-chromosome linked inhibitor of apoptosis protein) 9,10 function by gene targeting or treatment with a second mitochondria-derived activator of caspases (SMAC(11,) also called DIABLO(12); direct IAP-binding protein with low pI) mimetic drug in mice rendered hepatocytes and beta-cells independent of BID for FAS-induced apoptosis. These results show that XIAP is the critical discriminator between type I and type II apoptosis signalling and suggest that IAP inhibitors should be used with caution in cancer patients with underlying liver conditions.
Publisher
NATURE PUBLISHING GROUP
Keywords
ALPHA-DEPENDENT APOPTOSIS; DEFICIENT MICE; IMMUNE-SYSTEM; T-LYMPHOCYTES; CYTOCHROME-C; CELL-DEATH; PROTEIN; SMAC; ACTIVATION; RECEPTOR
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Creation Date: 2009-08-20 12:00:00
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