A tight quality control system over protein folding, turnover and synthesis, involving molecular chaperones and co-chaperones, maintains the balance of cardiac proteins. Various cardiac pathologies, including myocardial infarction, increase stresses and post-translational modifications favoring misfolding due to an overwhelmed quality control system. The toxic nature of accumulated misfolded proteins further worsens the condition. The important molecular chaperones which act as quality control proteins are involved in protecting the heart, these include heat shock protein70 (HSP70) and HSP90. Here, we review the emerging roles of heat shock proteins in the maintenance of cardiac cell populations in experimental models of ischemia/reperfusion (I/R) injury. Furthermore, we discuss the expression of HSP70 and HSP90 with therapeutic and diagnostic considerations. Although there is only a partial understanding of these important HSPs in I/R injury, there is an immense therapeutic potential of modulating these HSPs to counteract the imbalance between misfolding and endogenous protein quality control systems.

中文翻译：

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在缺血和再灌注过程中，热休克蛋白及其在原代鼠心脏细胞群体中的表达。

涉及分子伴侣和副伴侣的蛋白质折叠，转换和合成的严格质量控制体系，可维持心脏蛋白质的平衡。由于质量控制体系不堪重负，包括心肌梗塞在内的各种心脏疾病都会增加压力和翻译后修饰，从而有利于错误折叠。积累的错误折叠的蛋白质的毒性进一步恶化了病情。用作质量控制蛋白的重要分子伴侣涉及保护心脏，其中包括热休克蛋白70（HSP70）和HSP90。在这里，我们在缺血/再灌注（I / R）损伤的实验模型中回顾了热休克蛋白在维持心肌细胞群体中的新兴作用。此外，我们讨论HSP70和HSP90的表达与治疗和诊断方面的考虑。尽管对I / R损伤中的这些重要HSP仅有部分了解，但调节这些HSP来抵消错折叠和内源蛋白质质量控​​制系统之间的不平衡具有巨大的治疗潜力。