Glutathione and other cellular thiols (GSH)

Glutathione (GSH) and other cellular thiols, including cysteine and homocysteine, are vital low-molecular-weight molecules containing a sulfhydryl group that maintains cellular redox balance [1, 3]. As the most abundant non-protein thiol, glutathione acts as a potent antioxidant by directly scavenging reactive oxygen species and serving as a cofactor for enzymes like glutathione peroxidase [2, 4]. These molecules play a central role in the detoxification of endogenous and exogenous toxins through conjugation, a process often facilitated by glutathione S-transferases [3, 5]. In clinical contexts, thiol levels are frequently dysregulated; for instance, elevated GSH in cancer cells is associated with resistance to platinum-based chemotherapy and radiation [5]. Conversely, thiol depletion is a hallmark of oxidative stress in neurodegenerative diseases like Parkinson's and chronic inflammatory conditions [2, 5]. Pharmacological intervention includes the use of N-acetylcysteine to replenish GSH during acetaminophen toxicity or the use of inhibitors like buthionine sulfoximine to deplete thiols in oncology [1, 4]. Understanding the dynamics of these thiols is crucial for developing therapies that modulate the cellular antioxidant capacity to treat metabolic, oncological, and toxicological conditions [3, 5].

Other names

Low-molecular-weight thiolsNon-protein thiolsSulfhydryl compoundsLMW thiolsCellular sulfhydryls

Precursor-mediated replenishment of thiol pools, enzymatic inhibition of thiol synthesis, and direct chemical conjugation for detoxification or depletion.