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Am J Physiol Cell Physiol 273: C1666-C1672, 1997;
0363-6143/97 $5.00
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Vol. 273, Issue 5, C1666-C1672, November 1997

Modulation of cardiac Ca2+ channels by isoproterenol studied in transgenic mice with altered SR Ca2+ content

Hidenori Sako1, Stuart A. Green2, Evangelia G. Kranias1, and Atsuko Yatani1

Departments of 1 Pharmacology and Cell Biophysics and 2 Medicine, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267

Phospholamban (PLB) ablation is associated with enhanced sarcoplasmic reticulum (SR) Ca2+ uptake and attenuation of the cardiac contractile responses to beta -adrenergic agonists. In the present study, we compared the effects of isoproterenol (Iso) on the Ca2+ currents (ICa) of ventricular myocytes isolated from wild-type (WT) and PLB knockout (PLB-KO) mice. Current density and voltage dependence of ICa were similar between WT and PLB-KO cells. However, ICa recorded from PLB-KO myocytes had significantly faster decay kinetics. Iso increased ICa amplitude in both groups in a dose-dependent manner (50% effective concentration, 57.1 nM). Iso did not alter the rate of ICa inactivation in WT cells but significantly prolonged the rate of inactivation in PLB-KO cells. When Ba2+ was used as the charge carrier, Iso slowed the decay of the current in both WT and PLB-KO cells. Depletion of SR Ca2+ by ryanodine also slowed the rate of inactivation of ICa, and subsequent application of Iso further reduced the inactivation rate of both groups. These results suggest that enhanced Ca2+ release from the SR offsets the slowing effects of beta -adrenergic receptor stimulation on the rate of inactivation of ICa.

beta -adrenergic agonist; phospholamban; patch clamp; cardiac myocytes; mouse heart; sarcoplasmic reticulum


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