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Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

机译：钙蛋白酶超家族及其转基因动物的扩大成员和作用

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Calpains are intracellular Ca2+-dependent cysteine proteases (Clan CA, family C02, EC 3.4.22.17) found in almost all eukaryotes and some bacteria. Calpains display limited proteolytic activity at neutral pH, proteolysing substrates to transform and modulate their structures and activities, and are therefore called “modulator proteases”. The human genome has 15 genes that encode a calpain-like protease domain, generating diverse calpain homologues that possess combinations of several functional domains such as Ca2+-binding domains and Zn-finger domains. The importance of the physiological roles of calpains is reflected in the fact that particular defects in calpain functionality cause a variety of deficiencies in many different organisms, including lethality, muscular dystrophies, lissencephaly, and tumorigenesis. In this review, the unique characteristics of this distinctive protease superfamily are introduced in terms of genetically modified animals, some of which are animal models of calpain deficiency diseases.
机译：钙蛋白酶是在几乎所有真核生物和某些细菌中发现的细胞内Ca 2+依赖性半胱氨酸蛋白酶（Clan CA，家族C02，EC 3.4.22.17）。钙蛋白酶在中性pH下显示出有限的蛋白水解活性，蛋白酶水解底物以转化和调节其结构和活性，因此被称为“调节蛋白酶”。人类基因组中有15个基因编码钙蛋白酶样蛋白酶结构域，产生多种钙蛋白酶同源物，这些同源物具有多个功能域的结合，例如Ca 2 + 结合域和Zn-指结构域。钙蛋白酶的生理作用的重要性反映在以下事实上：钙蛋白酶功能的特定缺陷会导致许多不同生物体的各种缺陷，包括致死性，肌肉营养不良，lisencephaly和肿瘤发生。在这篇综述中，从转基因动物的角度介绍了这种独特的蛋白酶超家族的独特特征，其中一些是钙蛋白酶缺乏症动物模型。

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