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Apoptosis triggered redistribution of caspase‐9 from cytoplasm to mitochondria
Author(s) -
Potokar M,
Milisav I,
Kreft M,
Stenovec M,
Zorec R
Publication year - 2003
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(03)00494-0
Subject(s) - microbiology and biotechnology , cytoplasm , apoptosis , mitochondrion , apoptosome , caspase , caspase 3 , caspase 2 , caspase 9 , rotenone , cytochrome c , chemistry , biology , programmed cell death , biochemistry
Caspase‐9 is an apoptosis initiator protease activated as a response to the mitochondrial damage in the cytoplasmic complex apoptosome. By fluorescence labelling of proteins, confocal microscopy and subcellular fractionations we demonstrate that caspase‐9 is in the cytoplasm of non‐apoptotic pituitary cells. The activation of apoptosis with rotenone triggers the redistribution of caspase‐9 to mitochondria. Experiments using the general caspase inhibitor z‐VAD.fmk and the specific caspase‐9 inhibitor z‐LEHD.fmk show that the caspase‐9 redistribution is a regulated process and requires the activity of a caspase other than the caspase‐9. We propose that this spatial regulation is required to control the activity of caspase‐9.