Department of Innovative Technologies in Medicine and Dentistry, University "G. d' Annunzio", 66100 Chieti, Italy.
CAST (Center for Advanced Studies and Technology), University "G. d' Annunzio", 66100 Chieti, Italy.
Nutrients. 2024 Aug 18;16(16):2753. doi: 10.3390/nu16162753.
Protein glutathionylation is a reversible post-translational modification that involves the attachment of glutathione to cysteine residues. It plays a role in the regulation of several cellular processes and protection against oxidative damage. Glutathionylation (GS-ylation) modulates protein function, inhibits or enhances enzymatic activity, maintains redox homeostasis, and shields several proteins from irreversible oxidative stress. Aberrant GS-ylation patterns are thus implicated in various diseases, particularly those associated with oxidative stress and inflammation, such as cardiovascular diseases, neurodegenerative disorders, cancer, and many others. Research in the recent years has highlighted the potential to manipulate protein GS-ylation for therapeutic purposes with strategies that imply both its enhancement and inhibition according to different cases. Moreover, it has become increasingly evident that monitoring the GS-ylation status of selected proteins offers diagnostic potential in different diseases. In this review, we try to summarize recent research in the field with a focus on our current understanding of the molecular mechanisms related to aberrant protein GS-ylation.
蛋白质谷胱甘肽化是一种涉及将谷胱甘肽连接到半胱氨酸残基上的可逆翻译后修饰。它在调节几种细胞过程和防止氧化损伤方面发挥作用。谷胱甘肽化（GS-ylation）调节蛋白质功能，抑制或增强酶活性，维持氧化还原平衡，并保护几种蛋白质免受不可逆的氧化应激。因此，异常的 GS-ylation 模式与各种疾病有关，特别是与氧化应激和炎症有关的疾病，如心血管疾病、神经退行性疾病、癌症等。近年来的研究强调了通过增强和抑制 GS-ylation 的策略来操纵蛋白质 GS-ylation 以达到治疗目的的潜力，具体取决于不同情况。此外，越来越明显的是，监测选定蛋白质的 GS-ylation 状态在不同疾病中具有诊断潜力。在这篇综述中，我们试图总结该领域的最新研究，重点是我们对与异常蛋白质 GS-ylation 相关的分子机制的现有理解。
