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In vitro effects of palmityl carnitine on cardiac plasma membrane sodium potassium atpase and sarcoplasmic reticulum calcium atpase and calcium transport



In vitro effects of palmityl carnitine on cardiac plasma membrane sodium potassium atpase and sarcoplasmic reticulum calcium atpase and calcium transport



Journal of Biological Chemistry 254(24): 12404-12410



Palmitylcarnitine, an endogenous long-chain fatty acyl ester, produced marked changes in the structure and function of cardiac sarcoplasmic reticulum and sarcolemmal Na,K-ATPase isolated from canine ventricular muscle. Low concentrations (5-50 .mu.M) of palmitylcarnitine enhance Ca2+-ATPase activity and Ca2+ binding to sarcoplasmic reticulum and enhance [3H]ouabain binding to Na,K-ATPase above equilibrium binding levels but inhibit Na,K-ATPase hydrolytic activity. Increasing concentrations of palmitylcarnitine (50-200 .mu.M) further inhibit Na,K-ATPase activity and markedly decrease the binding of [3H]ouabain to this enzyme. Sarcoplasmic reticulum Ca2+-ATPase activity and Ca2+ binding are similarly inhibited by these higher concentrations of palmitylcarnitine. Palmitylcarnitine also produced concentration-dependent changes in the fluorescence intensity of a lipid-bound fluorescent probe, dansyl (5-dimethylaminonaphthalene-1-sulfonyl) phosphatidylethanolamine, which was incorporated into sarcoplasmic reticulum and Na,K-ATPase membranes. Palmitylcarnitine induced an enhancement of fluorescence in both membrane systems and this enhancement of fluorescence was linearly related to the inhibition of Na,K-ATPase activity. The biphasic action of palmitylcarnitine on the functional properties of sarcoplasmic reticulum and Na,K-ATPase resembles the actions of detergents on these membrane systems. Palmitylcarnitine acts as a naturally occurring detergent and a mechanism is proposed to explain its actions in vitro.

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Accession: 005648220

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