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肌浆网磷酸受纳蛋白在心脏中的特异性过表达改变了转基因小鼠的钙动力学及由此产生的心肌细胞力学特性。

Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice.

作者信息

Kadambi V J, Ponniah S, Harrer J M, Hoit B D, Dorn G W, Walsh R A, Kranias E G

机构信息

Department of Pharmacology, University of Cincinnati, College of Medicine, Ohio 45267, USA.

出版信息

J Clin Invest. 1996 Jan 15;97(2):533-9. doi: 10.1172/JCI118446.

Abstract

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.

摘要

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。

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