Selective inhibition of the mitochondrial permeability transition pore at the oxidation‐reduction sensitive dithiol by monobromobimane

FEBS Letters

Costantini, Paola¹  Chernyak, Boris V.¹  Petronilli, Valeria¹  Bernardi, Paolo¹ 

[1] CNR Unit for the Study of Physiology of Mitochondria and Laboratory of Biophysics and Membrane Biology, Department of Biomedical Sciences, University of Padova Medical School, Via Trieste 75, I-35121 Padova, Italy

关键词: Mitochondrial channel;    Cyclosporin A;    Membrane permeability (rat liver);    MTP;    mitochondrial permeability transition pore;    Δγ;    transmembrane potential difference;    EGTA;    ethylene-bis(oxoethylenenitrilo) tetraacetic acid;    FCCP;    carbonylcyanide-p-trifluoromethoxyphenyl hydrazone;    NEM;    N-ethylmaleimide;    MBM;    monobromobimane;    MBM+;    trimethylammonium monobromobimane;    DIA;    diamide;    AsO;    arsenite anion;   

DOI  :  10.1016/0014-5793(95)00256-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In this paper we introduce monobromobimane, a thiol reagent, as a selective blocker of the recently identified dithiol whose oxidation-reduction status modifies voltage sensing by the mitochondrial permeability transition pore, a cyclosporin A-sensitive channel. Monobromobimane does not inhibit the phosphate carrier, nor does it interfere with Ca²⁺ transport, energy coupling or ATP production and transport. We show that monobromobimane selectively prevents the shift in pore gating potential caused by some dithiol oxidants or crosslinkers but not by increasing [Ca²⁺], allowing a clear distinction of the pore agonists which act at this site.

【 授权许可】

Unknown