Malhotra A, Lopez M C, Nakouzi A
Department of Medicine, Montefiore Medical Center, Bronx, NY 10467, USA.
Mol Cell Biochem. 1995 Oct 18;151(2):165-72. doi: 10.1007/BF01322339.
Our group has documented that myocardial performance is impaired in the hearts of chronically diabetic rats and rabbits. Abnormalities in the contractile proteins and regulatory proteins may be responsible for the mechanical defects in the streptozotocin (STZ)-diabetic hearts. Previously, the major focus of our research on contractile proteins in abnormal states has concentrated on myosin ATPase and its isoenzymes. Our present study is based on the overall hypothesis that regulatory proteins, in addition to contractile protein, myosin contribute to altered cardiac contractile performance in the rat model of diabetic cardiomyopathy. The purpose of our research was to define the role of cardiac regulatory proteins (troponin-tropomyosin) in the regulation of actomyosin system in diabetic cardiomyopathy. For baseline data, myofibrillar ATPase studies were conducted in the myofibrils from control and diabetic rats. To focus on the regulatory proteins (troponin and tropomyosin), individual proteins of the cardiac system were reconstituted under controlled conditions. By this approach, myosin plus actin and troponin-tropomyosin from the normal and diabetic animals could be studied enzymatically. The proteins were isolated from the cardiac muscle of control and STZ-diabetic (4 weeks) rats. Sodium dodecyl sulfate gel electrophoretic patterns demonstrate differences in the cardiac TnT and TnI regions of diabetic animals suggesting the different amounts of TnT and/or TnI or possibly different cardiac isozymes in the regulatory protein complex. Myofibrils probed with a monoclonal antibody TnI-1 (specific for adult cardiac TnI) show a downregulation of cardiac TnI in diabetics when compared to its controls. Enzymatic data confirm a diminished calcium sensitivity in the regulation of the cardiac actomyosin system when regulatory protein(s) complex was recombined from diabetic hearts. Actomyosin ATPase activity in the hearts of diabetic animals was partially reversed when myosin from diabetic rats was regulated with the regulatory protein complex isolated from control hearts. To our knowledge, this is the first study which demonstrates that the regulatory proteins from normal hearts can upregulate cardiac myosin isolated from a pathologic rat model of diabetes. This diminished calcium sensitivity along with shifts in cardiac myosin heavy chain (V1-->V3) may be partially responsible for the impaired cardiac function in the hearts of chronic diabetic rats.
我们的研究小组已证明,长期患糖尿病的大鼠和兔子的心脏中心肌功能受损。收缩蛋白和调节蛋白的异常可能是链脲佐菌素(STZ)诱导的糖尿病心脏机械缺陷的原因。此前,我们对异常状态下收缩蛋白的研究主要集中在肌球蛋白ATP酶及其同工酶上。我们目前的研究基于这样一个总体假设:除收缩蛋白肌球蛋白外,调节蛋白也会导致糖尿病性心肌病大鼠模型中心脏收缩功能改变。我们研究的目的是确定心脏调节蛋白(肌钙蛋白 - 原肌球蛋白)在糖尿病性心肌病中对肌动球蛋白系统调节的作用。作为基线数据,我们在对照大鼠和糖尿病大鼠的肌原纤维中进行了肌原纤维ATP酶研究。为了聚焦于调节蛋白(肌钙蛋白和原肌球蛋白),在可控条件下对心脏系统的各个蛋白进行了重组。通过这种方法,可以对来自正常和糖尿病动物的肌球蛋白加肌动蛋白以及肌钙蛋白 - 原肌球蛋白进行酶学研究。这些蛋白是从对照大鼠和STZ诱导的糖尿病(4周)大鼠的心肌中分离出来的。十二烷基硫酸钠凝胶电泳图谱显示糖尿病动物心脏的肌钙蛋白T(TnT)和肌钙蛋白I(TnI)区域存在差异,这表明调节蛋白复合物中TnT和/或TnI的量不同,或者可能存在不同的心脏同工酶。用单克隆抗体TnI - 1(对成年心脏TnI具有特异性)探测的肌原纤维显示,与对照相比,糖尿病大鼠心脏中的心脏TnI下调。酶学数据证实,当从糖尿病心脏重组调节蛋白复合物时,心脏肌动球蛋白系统调节中的钙敏感性降低。当用从对照心脏分离的调节蛋白复合物调节糖尿病大鼠的肌球蛋白时,糖尿病动物心脏中的肌动球蛋白ATP酶活性部分恢复。据我们所知,这是第一项表明正常心脏的调节蛋白可以上调从糖尿病病理大鼠模型中分离出的心脏肌球蛋白的研究。这种钙敏感性降低以及心脏肌球蛋白重链的转变(V1→V3)可能部分导致了慢性糖尿病大鼠心脏功能受损。