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cIAP‐1, but not XIAP, is cleaved by caspases during the apoptosis induced by TGF‐β in fetal rat hepatocytes
Author(s) -
Herrera Blanca,
Fernández Margarita,
Benito Manuel,
Fabregat Isabel
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02774-6
Subject(s) - xiap , inhibitor of apoptosis , caspase , apoptosis , microbiology and biotechnology , transforming growth factor , chemistry , caspase 3 , epidermal growth factor , programmed cell death , biology , biochemistry , receptor
We have studied the expression of XIAP, cIAP‐1 and cIAP‐2 in fetal rat hepatocytes and its possible regulation by pro‐apoptotic stimuli (transforming growth factor‐β (TGF‐β)) and survival signals (epidermal growth factor (EGF)). The three forms of inhibitor of apoptosis proteins (IAPs) are expressed in fetal hepatocytes and only cIAP‐1, but not XIAP or cIAP‐2, is cleaved during TGF‐β‐induced apoptosis. The pan‐caspase inhibitor Z‐VAD.fmk blocked this effect, which indicates that cIAP‐1 is a caspase substrate. EGF plays a dual role in the regulation of IAPs expression. On one hand, it increases cIAP‐1 and cIAP‐2 basal expression and, on the other hand, it blocks the cleavage of cIAP‐1 by caspases induced by TGF‐β.