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Updated: Aug 1, 2026

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
Published on: June 1, 2022
Quinine inhibits mitochondrial ATP-regulated potassium channel from bovine heart
P Bednarczyk1, A Kicińska, V Kominkova
1Department of Biophysics, Agricultural University SGGW, 26/30 Rakowiecka St., 02-528 Warszawa, Poland.
Abstract:
The mitochondrial ATP-regulated potassium (mitoK(ATP) channel has been suggested as trigger and effector in myocardial ischemic preconditioning. However, molecular and pharmacological properties of the mitoK(ATP) channel remain unclear. In the present study, single-channel activity was measured after reconstitution of the inner mitochondrial membrane from bovine ventricular myocardium into bilayer lipid membrane. After incorporation, a potassium-selective current was recorded with mean conductance of 103 +/- 9 pS in symmetrical 150 mM KCl. Single-channel activity of this reconstituted protein showed properties of the mitoK(ATP) channel: it was blocked by 500 microM ATP/Mg, activated by the potassium-channel opener diazoxide at 30 microM, inhibited by 50 microM glibenclamide or 150 microM 5-hydroxydecanoic acid, and was not affected by the plasma membrane ATP-regulated potassium-channel blocker HMR1098 at 100 microM. We observed that the mitoK(ATP) channel was blocked by quinine in the micromolar concentration range. The inhibition by quinine was additionally verified with the use of 86Rb+ flux experiments and submitochondrial particles. Quinine inhibited binding of the sulfonylurea derivative [3H]glibenclamide to the inner mitochondrial membrane. We conclude that quinine inhibits the cardiac mitoK(ATP) channel by acting on the mitochondrial sulfonylurea receptor.
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