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Effect of metabolic inhibition on the activity of L-type Ca2+ channels in the presence of non-hydrolysable ATP analogs

Abstract : The effect of the protonophore FCCP. an uncoupler of oxidative phosphorylation, was examined on beta-adrenergic receptors agonist isoprenaline (ISO) stimulated L-type Ca2+ current (ICa) in frog ventricular myocytes dialyzed with an intracellular solution containing 3 mM ATP. FCCP dose-dependently and reversibly inhibited the ISO ( 1 µM) stimulated ICa. FCCP (0.1 µM) reduced the ISO-stimulated ICa by 87 +/- 1% (p<0.05, n=4). FCCP (0.1 µM) also strongly inhibited ICa when 3 mM ATP-gamma-S was added to intracellular solution (by 78.9% =/- 3.6%, n=4, p<0.05), whereas the substitution of ATP by 3 µM AMP-PCP and 0.5 mM ATP-gamma-S completely abolished the FCCP-induced inhibition of ICa. Our results demonstrate that the suppression of the activity of L-type Ca2+ channels during metabolic inhibition is caused by ATP hydrolysis and this effect is not related with decreased protein phosphorylation.
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https://hal-universite-paris-saclay.archives-ouvertes.fr/hal-03623456
Contributor : RODOLPHE FISCHMEISTER Connect in order to contact the contributor
Submitted on : Tuesday, March 29, 2022 - 5:00:28 PM
Last modification on : Friday, April 15, 2022 - 11:34:48 AM

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  • HAL Id : hal-03623456, version 1

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Giedrius Kanaporis, Rimantas Treinys, Jonas Jurevičius, Rodolphe Fischmeister. Effect of metabolic inhibition on the activity of L-type Ca2+ channels in the presence of non-hydrolysable ATP analogs. Biologija, 2004. ⟨hal-03623456⟩

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