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• W2136545895 abstract "The biochemical properties of the mitochondrial K channel are very similar to those of plasma membrane K channels, including inhibition by low concentrations of ATP and glyburide (Paucek, P., Mironova, G., Mahdi, F., Beavis, A. D., Woldegiorgis, G., and Garlid, K. D.(1992) J. Biol. Chem. 267, 26062-26069). Plasma membrane K channels are highly sensitive to the family of drugs known as K channel openers, raising the question whether mitochondrial K channels are similarly sensitive to these agents. We addressed this question by measuring K flux in intact rat liver mitochondria and in liposomes containing K channels purified from rat liver and beef heart mitochondria. K channel openers completely reversed ATP inhibition of K flux in both systems. In liposomes, ATP-inhibited K flux was restored by diazoxide (K = 0.4 μM), cromakalim (K = 1 μM), and two developmental cromakalim analogues, EMD60480 and EMD57970 (K = 6 nM). Similar K values were observed in intact mitochondria. These potencies are well within the range observed with plasma membrane K channels. We also compared the potencies of these K channel openers on the plasma membrane K channel purified from beef heart myocytes. The K channel from cardiac mitochondria is 2000-fold more sensitive to diazoxide than the channel from cardiac sarcolemma, indicating that two distinct receptor subtypes coexist within the myocyte. We suggest that the mitochondrial K channel is an important intracellular receptor that should be taken into account in considering the pharmacology of K channel openers. The biochemical properties of the mitochondrial K channel are very similar to those of plasma membrane K channels, including inhibition by low concentrations of ATP and glyburide (Paucek, P., Mironova, G., Mahdi, F., Beavis, A. D., Woldegiorgis, G., and Garlid, K. D.(1992) J. Biol. Chem. 267, 26062-26069). Plasma membrane K channels are highly sensitive to the family of drugs known as K channel openers, raising the question whether mitochondrial K channels are similarly sensitive to these agents. We addressed this question by measuring K flux in intact rat liver mitochondria and in liposomes containing K channels purified from rat liver and beef heart mitochondria. K channel openers completely reversed ATP inhibition of K flux in both systems. In liposomes, ATP-inhibited K flux was restored by diazoxide (K = 0.4 μM), cromakalim (K = 1 μM), and two developmental cromakalim analogues, EMD60480 and EMD57970 (K = 6 nM). Similar K values were observed in intact mitochondria. These potencies are well within the range observed with plasma membrane K channels. We also compared the potencies of these K channel openers on the plasma membrane K channel purified from beef heart myocytes. The K channel from cardiac mitochondria is 2000-fold more sensitive to diazoxide than the channel from cardiac sarcolemma, indicating that two distinct receptor subtypes coexist within the myocyte. We suggest that the mitochondrial K channel is an important intracellular receptor that should be taken into account in considering the pharmacology of K channel openers." @default.
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• W2136545895 date "1996-04-01" @default.
• W2136545895 modified "2023-10-14" @default.
• W2136545895 title "The Mitochondrial K Channel as a Receptor for Potassium Channel Openers" @default.
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• W2136545895 doi "https://doi.org/10.1074/jbc.271.15.8796" @default.
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