Inhibition of the mitochondrial cyclosporin A‐sensitive permeability transition pore by the arginine reagent phenylglyoxal

FEBS Letters

Eriksson, Ove¹  Fontaine, Eric¹  Petronilli, Valeria¹  Bernardi, Paolo¹ 

[1] CNR Unit for Study of Biomembranes and Laboratory of Biophysics and Membrane Biology, Department of Biomedical Sciences, University of Padova Medical School, viale G. Colombo 3, I-35121 PadovaItaly

关键词: Mitochondrial channel;    Permeability transition;    Calcium;    Cyclosporin A;    Voltage-gating;    Arginine;    Phenylglyoxal (rat liver);    PT;    permeability transition;    CsA;    cyclosporin A;    Δψ;    transmembrane electric potential difference;    PGO;    phenylglyoxal;    HEPES;    4-(2-hydroxyethyl)-1-piperazine-ethanesulphonic acid;    EGTA;    ethylene-bis(oxoethylenenitrilo) tetraacetic acid;    RR;    ruthenium red;    FCCP;    carbonylcyanide-p-trifluoromethoxyphenyl hydrazone;   

DOI  :  10.1016/S0014-5793(97)00549-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mitochondrial permeability transition pore, a cyclosporin A-sensitive channel, is controlled by the transmembrane electric potential difference across the inner membrane. Here, we show that treatment of rat liver mitochondria with the arginine reagent phenylglyoxal inhibits the permeability transition pore triggered by depolarization with uncoupler after Ca²⁺ accumulation. Phenylglyoxal does not change the extent of mitochondrial Ca²⁺ uptake or the extent of membrane depolarization, indicating that covalent modification of arginine (and possibly lysine) residues directly affects the open probability of the pore. We propose that arginine residues play a role in the physiological control of the permeability transition pore by the mitochondrial transmembrane potential.

【 授权许可】

Unknown