To involvement the conformation of the adenine nucleotide translocase in opening the Tl+-induced permeability transition pore in Ca2+-loaded rat liver mitochondria
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- 作者：Sergey M. Korotkova ; korotkov@SK1645.spb.edu" class="auth_mail" title="E-mail the corresponding author ; Svetlana A. Konovalovaa ; Irina V. Brailovskayaa ; Nils-Erik L. Sarisb
- 关键词：MPTP ; mitochondrial permeability transition pore ; PiC ; mitochondrial phosphate carrier ; CyP-D ; cyclophilin D ; ANT ; adenine nucleotide translocase ; IMM ; inner mitochondrial membrane ; CsA ; cyclosporine A ; ΔΨmito ; mitochondrial membrane potential ; CATR ; carboxyatractyloside ; BKA ; bongkrekic acid ; tBHP ; tert-butylhydroperoxide ; PAO ; phenylarsine oxide ; DIDS ; 4 ; 4&prime ; -Diisothiocyanostilbene-2 ; 2&prime ; -disulfonate ; NEM ; N-ethylmaleimide ; EMA ; eosin-5-maleimide ; CaRLM ; Ca2 ; +-loaded rat liver mit
- 刊名：Toxicology in Vitro
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：32
- 期：Complete
- 页码：320-332
- 全文大小：1716 K
文摘
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The involvement of ANT conformation in Tl+-induced mitochondrial pore is proposed.
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Thiol reagents (PAO, tBHP, DIDS) fixing the ANT in ‘c’ conformation researched
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Ability of ADP to inhibit the pore decreased in the presence of the reagents.
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N-ethylmaleimide (NEM) reacting with Cys56 of ANT inhibited the pore opening.
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CsA and NEM recovered ability of ADP to inhibit the pore stimulated by the reagents.