期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 373, 期 2, 页码 346-351出版社
ELSEVIER SCIENCE INC
DOI: 10.1006/abbi.1999.1567
关键词
cathepsin D; lysosomal destabilization; oxidative stress; apoptosis; caspase
Apoptosis was inhibited in rat cardiomyocytes pretreated with the aspartic protease inhibitor pepstatin A and subsequently exposed to naphthazarin (5,8-dihydroxy-1,4-naphthoquinone). Cathepsin D was released from lysosomes to the cytosol upon exposure to naphthazarin, and the enzyme activity decreased simultaneously. Later, cathepsin D reappeared in granules of increased size, and enzyme activity was restored. Activation of caspase-3-like proteases was detected, and the number of cells showing apoptotic morphology increased with time. Pepstatin A pretreatment did not prevent release of cathepsin D from lysosomes but did significantly inhibit subsequent naphthazarin-induced caspase activation and apoptotic morphology. This suggests that cathepsin D exerts its apoptosis-stimulating effect upstream of caspase-3-like activation. (C) 2000 Academic Press.
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