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• W1969855480 abstract "Ethanol increases the vulnerability of mitochondria to induction of the mitochondrial permeability transition (MPT). Cyclophilin-D activity enhances the potential for the permeability transition pore (PTP) to open. In the present study, we demonstrate that ethanol and its metabolism sensitize the PTP to opening, in part by increasing the acetylation and activity of cyclophilin-D. This effect of ethanol is mediated by inhibiting the activity of sirtuin-3, an NAD+ dependent deacetylase that is localized to the mitochondrial matrix. The ethanol-enhanced acetylation of cyclophilin-D also increases the interaction of cyclophilin-D with the adenine nucleotide translocator-1 (ANT-1) and is dependent on ethanol metabolism. Moreover, activation of AMPK, a known positive modulator of sirtuin activity, prevented the ethanol-induced suppression of sirtuin-3 activity and the attendant increase of cyclophilin-D acetylation, activity and association with ANT-1. Additionally, AMPK reactivation of sirtuin-3 prevented the sensitization to the MPT and the enhancement of cell killing by TNF in cells exposed to ethanol." @default.
• W1969855480 created "2016-06-24" @default.
• W1969855480 creator A5062155802 @default.
• W1969855480 creator A5087744752 @default.
• W1969855480 date "2010-12-01" @default.
• W1969855480 modified "2023-09-26" @default.
• W1969855480 title "Ethanol sensitizes mitochondria to the permeability transition by inhibiting deacetylation of cyclophilin-D mediated by sirtuin-3" @default.
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• W1969855480 doi "https://doi.org/10.1242/jcs.073502" @default.
• W1969855480 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6295654" @default.
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