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• W2022189013 abstract "Recent evidence demonstrates that long-chain acyl coenzyme A esters (CoAs) activate cardiac and β-cell plasma-membrane (pmKATP) adenosine triphosphate (ATP)-sensitive potassium channels. In this study, we have investigated the differential effects of acyl CoAs of short and medium side-chain length on cardiac and β-cell pmKATP isoforms. At the single-channel level, the addition of acyl CoAs of differing side-chain length (2 to 16 carbons) to the inside face of membrane patches from ventricular myocytes caused varying increases in pmKATP channel open probability proportional to increases in acyl side-chain length (20 μmol/L acetyl CoA: 310% ± 90%, 20 μmol/L decanoyl CoA: 570% ± 150%). A similar dependence of activation on side-chain length was observed in recombinant pmKATP channels (SUR2A/Kir6.2) with full activation of current requiring both the acyl and CoA moieties in the esterified form. We found the recombinant β-cell KATP channel (SUR1/Kir6.2) to be much less sensitive to medium-chain acyl CoAs (decanoyl CoA: 124% ± 15% v 231% ± 25% in SUR2A/Kir6.2), suggesting a role for the cardiac sulfonylurea receptor, SUR2A, in the molecular mechanism of activation by these compounds. We propose that fatty acid metabolism, and the resultant generation of acyl CoAs of varying side-chain length, may be an important regulator of cellular excitability via interactions with the KATP channel." @default.
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• W2022189013 date "2003-10-01" @default.
• W2022189013 modified "2023-09-29" @default.
• W2022189013 title "Acyl coenzyme A esters differentially activate cardiac and β-cell adenosine triphosphate-sensitive potassium channels in a side-chain length-specific manner" @default.
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• W2022189013 doi "https://doi.org/10.1016/s0026-0495(03)00199-9" @default.
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