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Redistribution of cell death-inducing DNA fragmentation factor-like effector-a (CIDEa) from mitochondria to nucleus is associated with apoptosis in HeLa cells
E Valouskova, K Smolkova, J Santorova, P Jezek, M Modriansky
Jazyk angličtina Země Slovensko
- MeSH
- apoptóza MeSH
- buněčné jádro metabolismus MeSH
- financování organizované MeSH
- HeLa buňky MeSH
- lidé MeSH
- mitochondrie metabolismus MeSH
- proteiny regulující apoptózu biosyntéza metabolismus MeSH
- transport proteinů MeSH
- Check Tag
- lidé MeSH
Cell death-inducing DFF[DNA fragmentation factor]-like effector-a (CIDEa), may initiate apoptosis by disrupting a complex consisting of 40-kDa caspase-3-activated nuclease (DFF40/CAD) and its 45-kDa inhibitor (DFF45/ICAD). CIDEa, however, was found to be localized in mitochondria. We have performed immunodetection of CIDEa in whole cells and subcellular fractions of HeLa cells adapted for a tetracycline-inducible CIDEa expression. Using immunocytochemistry we observed redistribution, enhanced upon treatment with camptothecin or valinomycin, of CIDEa to nucleus. Similarly, CIDEa content increased in the nuclear fraction but decreased in cytosolic fraction in cells treated to initiate apoptosis. We hypothesize that CIDEa is sequestered in mitochondria while transfer of this potentially dangerous protein from mitochondria into nucleus intensifies or even initiates apoptosis.
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- $a Redistribution of cell death-inducing DNA fragmentation factor-like effector-a (CIDEa) from mitochondria to nucleus is associated with apoptosis in HeLa cells / $c E Valouskova, K Smolkova, J Santorova, P Jezek, M Modriansky
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- $a Institute of Medical Chemistry and Biochemistry, Faculty of Medicine and Dentistry, Palacky University, Hnevotinska 3, 775 15 Olomouc, Czech Republic. walouch@email.cz
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- $a Cell death-inducing DFF[DNA fragmentation factor]-like effector-a (CIDEa), may initiate apoptosis by disrupting a complex consisting of 40-kDa caspase-3-activated nuclease (DFF40/CAD) and its 45-kDa inhibitor (DFF45/ICAD). CIDEa, however, was found to be localized in mitochondria. We have performed immunodetection of CIDEa in whole cells and subcellular fractions of HeLa cells adapted for a tetracycline-inducible CIDEa expression. Using immunocytochemistry we observed redistribution, enhanced upon treatment with camptothecin or valinomycin, of CIDEa to nucleus. Similarly, CIDEa content increased in the nuclear fraction but decreased in cytosolic fraction in cells treated to initiate apoptosis. We hypothesize that CIDEa is sequestered in mitochondria while transfer of this potentially dangerous protein from mitochondria into nucleus intensifies or even initiates apoptosis.
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