S-glutathionylation in cancer: from fundamental mechanisms to clinical applications

作者：Shuai Dong, Li Linghu, Desheng Xiao, Shuang Liu, Yongguang Tao · 发表于：Pharmacological Research · 年份：2025 · DOI：10.1016/j.phrs.2025.107924 · 被引用次数：6 · 研究领域：Sulfur Compounds in Biology、Glutathione Transferases and Polymorphisms、Redox biology and oxidative stress

Glutathione (GSH) is a thiol-containing antioxidant composed of glutamic acid, cysteine and glycine. GSH can form a disulfide bond with the cysteine sulfhydryl group of a protein, resulting in S-glutathionylation (-SSG). S-glutathionylation is a reversible posttranslational modification that plays important roles in redox regulation, detoxification, cell signaling pathway regulation, cell death, infection and inflammation. Recent studies have shown that GSH and glutathionylation also have a significant effect on a variety of common cancers. GSH has the potential to serve as an auxiliary diagnostic tool for cancer. S-glutathionylation can regulate the level of the modified protein to regulate tumor cell proliferation and patient survival. In addition, glutathionylation can affect resistance to anticancer clinical drugs, as well as immunotherapy. These findings provide a new therapeutic target for cancer treatment. This review comprehensively reviews the key roles of glutathionylation and its potential mechanisms in a variety of common cancers. Finally, we discuss in depth the role of glutathionylation in resistance to radiotherapy, chemotherapy, targeted drugs and immune checkpoint inhibitors. This study provides a theoretical basis for the development of new cancer treatment drugs.