Activation of CPP32 and Mch3 alpha in wild-type p53-induced apoptosis.
DNA-damaging agents induce apoptosis primarily by a p53-dependent pathway. LTR6 cells containing a temperature-sensitive p53 were used to dissect further the mechanisms of p53-induced apoptosis. Apoptosis was accompanied by the processing and activation of CPP32 and Mch3 alpha, together with the cleavage of poly(ADP-ribose) polymerase and lamin B1. These results demonstrate a critical role for the activation of interleukin-1 beta-converting enzyme-like proteases in p53-induced apoptosis.
Chandler
J M
JM
Medical Research Council Toxicology Unit, University of Leicester, U.K.
Alnemri
E S
ES
Cohen
G M
GM
MacFarlane
M
M
D000818:Animals; D017209:Apoptosis / Q000187:drug effects; D053148:Caspase 3; D020169:Caspases; D003374:Coumarins / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D005456:Fluorescent Dyes; D007951:Leukemia, Myeloid; D051379:Mice; D009842:Oligopeptides / Q000378:metabolism; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured; D016159:Tumor Suppressor Protein p53 / Q000494:pharmacology*
D003374:Coumarins; D005456:Fluorescent Dyes; D009842:Oligopeptides; D016159:Tumor Suppressor Protein p53; C102580:acetyl-aspartyl-glutamyl-valyl-aspartyl-amino-4-methylcoumarin; C505409:Casp3 protein, mouse; D053148:Caspase 3; D020169:Caspases; D003546:Cysteine Endopeptidases