Kadambi V J, Ponniah S, Harrer J M, Hoit B D, Dorn G W, Walsh R A, Kranias E G
Department of Pharmacology, University of Cincinnati, College of Medicine, Ohio 45267, USA.
J Clin Invest. 1996 Jan 15;97(2):533-9. doi: 10.1172/JCI118446.
Phospholamban is the regulator of the cardiac sarcoplasmic reticulum (SR) Ca(2+)-ATPase activity and an important modulator of basal contractility in the heart. To determine whether all the SR Ca(2+)-ATPase enzymes are subject to regulation by phospholamban in vivo, transgenic mice were generated which overexpressed phospholamban in the heart, driven by the cardiac-specific alpha-myosin heavy chain promoter. Quantitative immunoblotting revealed a twofold increase in the phospholamban protein levels in transgenic hearts compared to wild type littermate hearts. The transgenic mice showed no phenotypic alterations and no changes in heart/body weight, heart/lung weight, and cardiomyocyte size. Isolated unloaded cardiac myocytes from transgenic mice exhibited diminished shortening fraction (63%) and decreased rates of shortening (64%) and relengthening (55%) compared to wild type (100%) cardiomyocytes. The decreases in contractile parameters of transgenic cardiomyocytes reflected decreases in the amplitude (83%) of the Ca2+ signal and prolongation (131%) in the time for decay of the Ca2+ signal, which was associated with a decrease in the apparent affinity of the SR Ca(2+)-ATPase for Ca2+ (56%), compared to wild type (100%) cardiomyocytes. In vivo analysis of left ventricular systolic function using M mode and pulsed-wave Doppler echocardiography revealed decreases in fractional shortening (79%) and the normalized mean velocity of circumferential shortening (67%) in transgenic mice compared to wild type (100%) mice. The differences in contractile parameters and Ca2+ kinetics in transgenic cardiomyocytes and the depressed left ventricular systolic function in transgenic mice were abolished upon isoproterenol stimulation. These findings indicate that a fraction of the Ca(2+)-ATPases in native SR is not under regulation by phospholamban. Expression of additional phospholamban molecules results in: (a) inhibition of SR Ca2+ transport; (b) decreases in systolic Ca2+ levels and contractile parameters in ventricular myocytes; and (c) depression of basal left ventricular systolic function in vivo.
受磷蛋白是心肌肌浆网(SR)Ca(2+)-ATP酶活性的调节因子,也是心脏基础收缩性的重要调节分子。为了确定体内所有的SR Ca(2+)-ATP酶是否都受受磷蛋白的调节,通过心脏特异性α-肌球蛋白重链启动子驱动,构建了在心脏中过表达受磷蛋白的转基因小鼠。定量免疫印迹显示,与野生型同窝仔鼠心脏相比,转基因心脏中受磷蛋白的水平增加了两倍。转基因小鼠未表现出表型改变,心脏/体重、心脏/肺重量和心肌细胞大小也没有变化。与野生型(100%)心肌细胞相比,来自转基因小鼠的离体无负荷心肌细胞表现出缩短分数降低(63%)、缩短速率降低(64%)和再伸长速率降低(55%)。转基因心肌细胞收缩参数的降低反映了Ca2+信号幅度降低(83%)和Ca2+信号衰减时间延长(131%),这与SR Ca(2+)-ATP酶对Ca2+的表观亲和力降低(56%)有关,而野生型(100%)心肌细胞则无此现象。使用M型和脉冲波多普勒超声心动图对左心室收缩功能进行体内分析显示,与野生型(100%)小鼠相比,转基因小鼠的缩短分数降低(79%),圆周缩短标准化平均速度降低(67%)。异丙肾上腺素刺激后,转基因心肌细胞收缩参数和Ca2+动力学的差异以及转基因小鼠左心室收缩功能的降低均被消除。这些发现表明,天然SR中的一部分Ca(2+)-ATP酶不受受磷蛋白的调节。额外的受磷蛋白分子表达会导致:(a)抑制SR Ca2+转运;(b)心室肌细胞收缩期Ca2+水平和收缩参数降低;(c)体内基础左心室收缩功能降低。