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Glutathione disulfide (GSSG) is the oxidized dimer form of glutathione, formed by a disulfide bond between two molecules of reduced glutathione. It is an endogenous molecule involved in cellular redox homeostasis and acts as a key indicator of oxidative stress within cells. In biological systems, GSSG is reduced back to its active form (glutathione) by the enzyme glutathione reductase using NADPH as a cofactor. This process helps maintain the balance between oxidized and reduced forms of glutathione, which is critical for protecting cells from oxidative damage. Glutathione disulfide can also act as an ingredient in ophthalmic irrigation solutions used during eye surgeries[1][3]. As part of its mechanism, it participates in antioxidant defense by being generated during the reduction of peroxides via enzymes such as glutathione peroxidases and peroxiredoxins[3]. Additionally, it may function as an endogenous neuromodulator at high concentrations through interactions with NMDA and AMPA receptors[3].
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