Caspase inhibition and N6-benzyladenosine-induced apoptosis in HL-60 cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
11746510
DOI
10.1002/jcb.1262
PII: 10.1002/jcb.1262
Knihovny.cz E-zdroje
- MeSH
- adenosin analogy a deriváty farmakologie MeSH
- apoptóza účinky léků MeSH
- buněčná membrána účinky léků enzymologie MeSH
- buněčné jádro účinky léků enzymologie metabolismus MeSH
- chloromethylketony aminokyselin farmakologie MeSH
- chromatin metabolismus MeSH
- HL-60 buňky cytologie účinky léků enzymologie MeSH
- inhibitory cysteinových proteinas farmakologie MeSH
- inhibitory kaspas * MeSH
- kaspasa 3 MeSH
- kaspasa 9 MeSH
- kaspasy fyziologie MeSH
- lidé MeSH
- oligopeptidy farmakologie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- adenosin MeSH
- benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone MeSH Prohlížeč
- benzyloxycarbonyl-leucyl-glutamyl-histidyl-aspartic acid fluoromethyl ketone MeSH Prohlížeč
- benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone MeSH Prohlížeč
- CASP3 protein, human MeSH Prohlížeč
- CASP9 protein, human MeSH Prohlížeč
- chloromethylketony aminokyselin MeSH
- chromatin MeSH
- inhibitory cysteinových proteinas MeSH
- inhibitory kaspas * MeSH
- kaspasa 3 MeSH
- kaspasa 9 MeSH
- kaspasy MeSH
- N(6)-benzyladenosine MeSH Prohlížeč
- oligopeptidy 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.
Citace poskytuje Crossref.org