Journal article
Caspase-3 and inhibitor of apoptosis protein(s) interactions in Saccharomyces cerevisiae and mammalian cells
FEBS letters, Vol.481(1), pp.13-18
2000
DOI: 10.1016/S0014-5793(00)01962-1
PMID: 10984607
Abstract
Using a heterologous yeast expression assay, we show that inhibitor of apoptosis proteins (IAPs) suppress caspase-3-mediated cytotoxicity in the order of XIAP>c-IAP2>c-IAP1>survivin. The same ordering of IAP activities was demonstrated in mammalian cells expressing an auto-activating caspase-3. The relative anti-apoptotic activities of each IAP depended on the particular death stimulus. For IAP-expressing cells treated with camptothecin, survival correlated with their intrinsic anti-caspase-3 activity. However, c-IAP1-transfected cells were disproportionately resistant to tumor necrosis factor-α, suggesting that its anti-apoptotic activities extend beyond caspase-3 or -7 inhibition. Yeast-based caspase assays provide rapid, reliable information on specificity and activity of the IAPs and aid in identifying critical targets in mammalian apoptotic pathways.
Details
- Title: Subtitle
- Caspase-3 and inhibitor of apoptosis protein(s) interactions in Saccharomyces cerevisiae and mammalian cells
- Creators
- Michael E Wright - Fred Hutch Cancer CenterDavid K Han - University of WashingtonDavid M Hockenbery - Fred Hutchinson Cancer Research Center
- Resource Type
- Journal article
- Publication Details
- FEBS letters, Vol.481(1), pp.13-18
- DOI
- 10.1016/S0014-5793(00)01962-1
- PMID
- 10984607
- NLM abbreviation
- FEBS Lett
- ISSN
- 0014-5793
- eISSN
- 1873-3468
- Publisher
- Elsevier B.V
- Language
- English
- Date published
- 2000
- Academic Unit
- Molecular Physiology and Biophysics
- Record Identifier
- 9984297506802771
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