Caspase inhibition and N6-benzyladenosine-induced apoptosis in HL-60 cells
Language English Country United States Media print
Document type Journal Article
PubMed
11746510
DOI
10.1002/jcb.1262
PII: 10.1002/jcb.1262
Knihovny.cz E-resources
- MeSH
- Adenosine analogs & derivatives pharmacology MeSH
- Apoptosis drug effects MeSH
- Cell Membrane drug effects enzymology MeSH
- Cell Nucleus drug effects enzymology metabolism MeSH
- Amino Acid Chloromethyl Ketones pharmacology MeSH
- Chromatin metabolism MeSH
- HL-60 Cells cytology drug effects enzymology MeSH
- Cysteine Proteinase Inhibitors pharmacology MeSH
- Caspase Inhibitors * MeSH
- Caspase 3 MeSH
- Caspase 9 MeSH
- Caspases physiology MeSH
- Humans MeSH
- Oligopeptides pharmacology MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Adenosine MeSH
- benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone MeSH Browser
- benzyloxycarbonyl-leucyl-glutamyl-histidyl-aspartic acid fluoromethyl ketone MeSH Browser
- benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone MeSH Browser
- CASP3 protein, human MeSH Browser
- CASP9 protein, human MeSH Browser
- Amino Acid Chloromethyl Ketones MeSH
- Chromatin MeSH
- Cysteine Proteinase Inhibitors MeSH
- Caspase Inhibitors * MeSH
- Caspase 3 MeSH
- Caspase 9 MeSH
- Caspases MeSH
- N(6)-benzyladenosine MeSH Browser
- Oligopeptides MeSH
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.
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