{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Glutathione S‐transferase omega 1‐1 (GSTO1‐1), a member of the omega class of phase II detoxification enzymes, is emerging as a multifunctional catalyst that plays pivotal roles in redox homeostasis, detoxification, inflammation, and cell survival. Studies quantifying GSTO1 protein in human brain microvessels and other tissues demonstrate its ubiquitous expression, supporting a role in cellular defense mechanisms."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n At the enzymatic level, GSTO1‐1 catalyzes deglutathionylation reactions by removing glutathione adducts from proteins—a process that serves as a “redox switch” regulating the activity of multiple substrates (for example, β‐actin) and influencing the processing of inflammatory mediators such as interleukin‐1β (via post‐translational modifications)."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " These functions underscore a central role in modulating the intracellular glutathionylation cycle and maintaining an appropriate redox balance."}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Genetic variation in GSTO1 has been linked to alterations in enzyme activity and has been implicated in a number of human diseases. Several independent studies have reported that polymorphisms in GSTO1 (for example, the Ala140Asp and other variants) modify arsenic biotransformation efficiency and alter urinary profiles of arsenic metabolites. Such alterations are associated with increased susceptibility to arsenic‐related toxicities—including skin lesions and, potentially, arsenic‐induced cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "12"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition to its role in detoxification, GSTO1‐1 has been implicated in the regulation of inflammatory responses. Its catalytic activity is required for proper activation of innate immune signaling pathways, as evidenced by experiments showing that GSTO1‐1 is necessary for toll‐like receptor 4 (TLR4)–mediated responses, including the generation of reactive oxygen species (ROS) and the metabolic reprogramming of macrophages in response to lipopolysaccharide stimulation (which in turn affects both the NLRP3 inflammasome and cytokine production)."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "16"}]}, {"type": "t", "text": " \n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n GSTO1‐1’s functional impact extends to neurodegenerative and age‐related disorders. Expression and genetic association studies in Alzheimer’s and Parkinson’s diseases have implicated GSTO1 polymorphisms in modifying age‐at‐onset and disease risk, suggesting that altered enzyme activity may affect neuronal redox balance and inflammatory signaling in the brain."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "22"}]}, {"type": "t", "text": " Furthermore, in cancer cells, overexpression of GSTO1‐1 has been shown to interfere with apoptosis—promoting chemoresistance (for example, against cisplatin) through activation of pro‐survival pathways such as Akt and ERK and suppression of apoptotic signals like JNK."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Finally, a broader role for GSTO1‐1 in cellular stress response is supported by its involvement in diverse conditions ranging from inflammatory airway disease to cataract formation, whereby differential expression (or genetic variants) of GSTO1 contributes to the modulation of oxidative stress and cellular protection (see also"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": " Collectively, these findings establish GSTO1‐1 as a critical mediator of redox regulation, xenobiotic metabolism, inflammation, and cell survival. Its versatile functions and the impact of its genetic variability make GSTO1‐1 a promising target for therapeutic intervention in conditions ranging from arsenic toxicity and chemoresistant cancers to neurodegenerative and inflammatory diseases.\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Additional insights into GSTO1 family members are provided by studies on GSTO2, which share overlapping yet distinct functions with GSTO1‐1, further broadening our understanding of the omega class in cellular physiology."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ramzi Shawahna, Yasuo Uchida, Xavier Declèves, et al. 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