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Induction of apoptosis in primary culture of rat hepatocytes by protease inhibitors
Author(s) -
Maeda Sumio,
Lin Kong Hua,
Inagaki Hidetoshi,
Saito Takao
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201491
Subject(s) - apoptosis , leupeptin , calpain , proteases , programmed cell death , proteolysis , dna fragmentation , protease , microbiology and biotechnology , cysteine protease , protease inhibitor (pharmacology) , biology , fragmentation (computing) , autophagy , biochemistry , enzyme , immunology , ecology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
There is growing evidence that suggests the involvement of intracellular proteases in the process of apoptosis or programmed cell death. In this study, we have demonstrated that leupeptin, a cysteine protease inhibitor, can significantly increase the incidence of both apoptotic nuclear morphology change and internucleosomal DNA fragmentation in primary cultured hepatocytes in the absence of known apoptotic stimuli for hepatocytes. On the other hand, aspartic and serine protease inhibitors showed little or no effects on the apoptotic changes. In addition, we found that the apoptotic changes could be induced by chloroquine, an inhibitor of lysosomal proteolysis, but could not be induced by calpain inhibitors. These data suggest that inhibition of lysosomal cysteine proteases may induce apoptosis in primary cultured hepatocytes.