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Caspase inhibition and N 6 ‐benzyladenosine‐induced apoptosis in HL‐60 cells
Author(s) -
Mlejnek P.
Publication year - 2001
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.1262
Subject(s) - apoptosis , caspase , microbiology and biotechnology , intrinsic apoptosis , programmed cell death , proteases , caspase 2 , biology , caspase 3 , chemistry , biochemistry , enzyme
Abstract As an extension of our recently published work (Mlejnek and Kuglík [2000] J. Cell. Biochem. 77:6–17), the role of caspases in N 6 ‐benzylaminopurine riboside (BAPR)‐induced apotosis in HL‐60 cells was evaluated in this study. Here, BAPR‐induced apoptosis was accompanied by activation of caspase‐3 and caspase‐9. However, when these caspases were selectively inhibited, the progression of BAPR‐induced apoptosis was not markedly affected. Besides that, activation of caspase‐3 and caspase‐9 was found to be rather late event in apoptotic process. These results suggested that other caspases might be critically implicated. Indeed, pan‐specific caspase inhibitor, Z‐VAD‐FMK, completely prevented DNA cleavage and apoptotic bodies formation. However, Z‐VAD‐FMK failed to prevent cell death and it was incapable to fully counteract the main apoptotic hallmark‐chromatin condensation. Finally, our data indicate that cellular decision between apoptosis and necrosis is made upon the availability of both caspase proteases and intracellular ATP. J. Cell. Biochem. 83: 678–689, 2001. © 2001 Wiley‐Liss, Inc.