Department of Biochemistry and Molecular Biology, School of Medicine, Jordan University of Science and Technology, Irbid, Jordan.
Physiol Res. 2021 Dec 30;70(Suppl4):S443-S470. doi: 10.33549/physiolres.934805.
Sarcoplasmic reticulum (SR) is a specialized tubular network, which not only maintains the intracellular concentration of Ca2+ at a low level but is also known to release and accumulate Ca2+ for the occurrence of cardiac contraction and relaxation, respectively. This subcellular organelle is composed of several phospholipids and different Ca2+-cycling, Ca2+-binding and regulatory proteins, which work in a coordinated manner to determine its function in cardiomyocytes. Some of the major proteins in the cardiac SR membrane include Ca2+-pump ATPase (SERCA2), Ca2+-release protein (ryanodine receptor), calsequestrin (Ca2+-binding protein) and phospholamban (regulatory protein). The phosphorylation of SR Ca2+-cycling proteins by protein kinase A or Ca2+-calmodulin kinase (directly or indirectly) has been demonstrated to augment SR Ca2+-release and Ca2+-uptake activities and promote cardiac contraction and relaxation functions. The activation of phospholipases and proteases as well as changes in different gene expressions under different pathological conditions have been shown to alter the SR composition and produce Ca2+-handling abnormalities in cardiomyocytes for the development of cardiac dysfunction. The post-translational modifications of SR Ca2+ cycling proteins by processes such as oxidation, nitrosylation, glycosylation, lipidation, acetylation, sumoylation, and O GlcNacylation have also been reported to affect the SR Ca2+ release and uptake activities as well as cardiac contractile activity. The SR function in the heart is also influenced in association with changes in cardiac performance by several hormones including thyroid hormones and adiponectin as well as by exercise-training. On the basis of such observations, it is suggested that both Ca2+-cycling and regulatory proteins in the SR membranes are intimately involved in determining the status of cardiac function and are thus excellent targets for drug development for the treatment of heart disease.
肌浆网(SR)是一种特殊的管状网络,它不仅维持细胞内 Ca2+浓度处于低水平,还负责分别释放和积累 Ca2+,以实现心脏的收缩和舒张。这个亚细胞细胞器由几种磷脂和不同的 Ca2+循环、Ca2+结合和调节蛋白组成,它们协同工作以确定其在心肌细胞中的功能。心脏 SR 膜中的一些主要蛋白质包括 Ca2+-泵 ATP 酶(SERCA2)、Ca2+释放蛋白(ryanodine 受体)、钙结合蛋白(calsequestrin)和调节蛋白(phospholamban)。已经证明,蛋白激酶 A 或 Ca2+-钙调蛋白激酶(直接或间接)对 SR Ca2+循环蛋白的磷酸化可增强 SR Ca2+释放和 Ca2+摄取活性,促进心脏收缩和舒张功能。在不同病理条件下,磷脂酶和蛋白酶的激活以及不同基因表达的变化已被证明会改变 SR 组成,并导致心肌细胞 Ca2+处理异常,从而导致心脏功能障碍。SR Ca2+循环蛋白的翻译后修饰,如氧化、硝化、糖基化、脂化、乙酰化、SUMO 化和 O-GlcNAc 化等,也被报道会影响 SR Ca2+释放和摄取活性以及心脏收缩活性。心脏的 SR 功能也会受到几种激素(包括甲状腺激素和脂联素)以及运动训练等因素的影响,这些因素会改变心脏的性能。基于这些观察结果,有人认为,SR 膜中的 Ca2+循环和调节蛋白都密切参与决定心脏功能的状态,因此是开发治疗心脏病药物的理想靶点。