Caspase inhibition and N6-benzyladenosine-induced apoptosis in HL-60 cells

✍ Scribed by P. Mlejnek

• Publisher: John Wiley and Sons
• Year: 2001
• Tongue: English
• Weight: 300 KB
• Volume: 83
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.1262

✦ Synopsis

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.