Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria

There we made available information about the effects of the adenine nucleotide translocase (ANT) ‘c’ conformation fixers (phenylarsine oxide (PAO), tert-butylhydroperoxide (tBHP), and carboxyatractyloside) as well as thiol reagent (4,4′-diisothiocyanostilbene-2,2′-disulfonate (DIDS)) on isolated ra...

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Main Author: Sergey M. Korotkov
Format: Article
Language:English
Published: Elsevier 2016-06-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S235234091630138X
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spelling doaj-5f5452c06a4f4fe29bb8aac4351adb492020-11-24T22:00:22ZengElsevierData in Brief2352-34092016-06-017620629Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondriaSergey M. Korotkov0Sechenov Institute of Evolutionary Physiology and Biochemistry, the Russian Academy of Sciences, Thorez pr. 44, 194223 St. Petersburg, Russian FederationThere we made available information about the effects of the adenine nucleotide translocase (ANT) ‘c’ conformation fixers (phenylarsine oxide (PAO), tert-butylhydroperoxide (tBHP), and carboxyatractyloside) as well as thiol reagent (4,4′-diisothiocyanostilbene-2,2′-disulfonate (DIDS)) on isolated rat liver mitochondria. We observed a decrease in A540 (mitochondrial swelling) and respiratory control rates (RCRADP [state 3/state 4] and RCRDNP [2,4-dinitrophenol-uncoupled state/basal state or state 4]), as well as an increase in Ca2+-induced safranin fluorescence (F485/590, arbitrary units), showed a dissipation in the inner membrane potential (ΔΨmito), in experiments with energized rat liver mitochondria, injected into the buffer containing 25–75 mM TlNO3, 125 mM KNO3, and 100 µM Ca2+. The fixers and DIDS, in comparison to Ca2+ alone, greatly increased A540 decline and the rate of Ca2+-induced ΔΨmito dissipation. These reagents also markedly decreased RCRADP and RCRDNP. The MPTP inhibitors (ADP, cyclosporin A, bongkrekic acid, and N-ethylmaleimide) fixing the ANT in ‘m’ conformation significantly hindered the above-mentioned effects of the fixers and DIDS. A more complete scientific analysis of these findings may be obtained from the manuscript “To involvement the conformation of the adenine nucleotide translocase in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria” (Korotkov et al., 2016 [1]). Keywords: Tl+, Ca2+, Oxygen consumption assay, Mitochondrial swelling, Mitochondrial membrane potential, Rat liver mitochondriahttp://www.sciencedirect.com/science/article/pii/S235234091630138X
collection DOAJ
language English
format Article
sources DOAJ
author Sergey M. Korotkov
spellingShingle Sergey M. Korotkov
Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
Data in Brief
author_facet Sergey M. Korotkov
author_sort Sergey M. Korotkov
title Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
title_short Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
title_full Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
title_fullStr Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
title_full_unstemmed Data supporting the involvement of the adenine nucleotide translocase conformation in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
title_sort data supporting the involvement of the adenine nucleotide translocase conformation in opening the tl+-induced permeability transition pore in ca2+-loaded rat liver mitochondria
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2016-06-01
description There we made available information about the effects of the adenine nucleotide translocase (ANT) ‘c’ conformation fixers (phenylarsine oxide (PAO), tert-butylhydroperoxide (tBHP), and carboxyatractyloside) as well as thiol reagent (4,4′-diisothiocyanostilbene-2,2′-disulfonate (DIDS)) on isolated rat liver mitochondria. We observed a decrease in A540 (mitochondrial swelling) and respiratory control rates (RCRADP [state 3/state 4] and RCRDNP [2,4-dinitrophenol-uncoupled state/basal state or state 4]), as well as an increase in Ca2+-induced safranin fluorescence (F485/590, arbitrary units), showed a dissipation in the inner membrane potential (ΔΨmito), in experiments with energized rat liver mitochondria, injected into the buffer containing 25–75 mM TlNO3, 125 mM KNO3, and 100 µM Ca2+. The fixers and DIDS, in comparison to Ca2+ alone, greatly increased A540 decline and the rate of Ca2+-induced ΔΨmito dissipation. These reagents also markedly decreased RCRADP and RCRDNP. The MPTP inhibitors (ADP, cyclosporin A, bongkrekic acid, and N-ethylmaleimide) fixing the ANT in ‘m’ conformation significantly hindered the above-mentioned effects of the fixers and DIDS. A more complete scientific analysis of these findings may be obtained from the manuscript “To involvement the conformation of the adenine nucleotide translocase in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria” (Korotkov et al., 2016 [1]). Keywords: Tl+, Ca2+, Oxygen consumption assay, Mitochondrial swelling, Mitochondrial membrane potential, Rat liver mitochondria
url http://www.sciencedirect.com/science/article/pii/S235234091630138X
work_keys_str_mv AT sergeymkorotkov datasupportingtheinvolvementoftheadeninenucleotidetranslocaseconformationinopeningthetlinducedpermeabilitytransitionporeinca2loadedratlivermitochondria
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