Apoptosis triggered redistribution of caspase‐9 from cytoplasm to mitochondria

FEBS Letters

Stenovec, M¹  Zorec, R¹  Milisav, I¹  Kreft, M¹  Potokar, M¹ 

[1] Laboratory of Neuroendocrinology–Molecular Cell Physiology, Institute of Pathophysiology, Medical Faculty Ljubljana, Zaloska 4, SI-1000 Ljubljana, Slovenia

关键词: Caspase-9;    Apoptosis;    Activation;    Intracellular distribution;    Mitochondrion;    Rotenone;    EGFP;    enhanced green fluorescent protein;    TMRM;    tetramethylrhodamine methyl ester;    Casp9E;    a fusion protein between caspase-9 and EGFP;    Sec61E;    a fusion protein between Sec61 and EGFP;   

DOI  :  10.1016/S0014-5793(03)00494-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown