Department of Pathology, University of Vermont College of Medicine, Burlington, Vermont 05405, USA.
J Cell Biochem. 2013 Sep;114(9):1962-8. doi: 10.1002/jcb.24551.
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.
谷胱甘肽传统上被认为是一种抗氧化剂，可保护细胞免受氧化应激。因此，还原型谷胱甘肽的损失和谷胱甘肽二硫化物的形成被认为是氧化应激的经典参数，在疾病中会增加。最近的研究表明，谷胱甘肽通过对蛋白质内的反应性半胱氨酸进行共价修饰（称为 S-谷胱甘肽化），在生物和病理生理过程中发挥更直接的作用。在蛋白质内形成 S-谷胱甘肽化部分会导致结构和功能的改变。激活、失活、功能丧失和功能获得都归因于 S-谷胱甘肽化。在病理生理环境中，S-谷胱甘肽化受到严格调控。本文简要概述了蛋白质巯基氧化还原修饰这一新兴领域。我们还将介绍新开发的用于检测蛋白质内 S-谷胱甘肽化的原位方法，这将有助于进一步发现 S-谷胱甘肽化在生物学和疾病中的作用。
