GSTO1 Activators

The category termed GSTO1 Activators encompasses chemical compounds that can indirectly influence the activity of Glutathione S-transferase omega-1 (GSTO1). GSTO1 is an enzyme that plays a key role in the detoxification process by catalyzing the conjugation of glutathione to a range of substrates. There were no known direct activators of GSTO1. However, the compounds listed in the table are implicated in the same or related pathways and can therefore indirectly modulate GSTO1 activity. These compounds, including Ethacrynic acid, Cibacron Blue 3GA, Sulfasalazine, Ellipticine, Menadione, Bromosulfophthalein, Chlorambucil, Piperlongumine, Oltipraz, Diethylmaleate, Ethacraplatin, and Curcumin, can affect GSTO1 by interacting with related cellular processes and pathways. For example, these compounds can inhibit glutathione S-transferases (GSTs), a family of enzymes including GSTO1, which are involved in the detoxification of endogenous compounds and xenobiotics by conjugation with glutathione. By inhibiting GSTs, these compounds can indirectly influence the activity of GSTO1.

Additionally, these compounds can affect the availability and function of glutathione, the primary substrate for GSTO1. Glutathione is a tripeptide that plays a crucial role in protecting cells from oxidative stress. By modulating the levels or function of glutathione, these compounds can indirectly influence GSTO1 activity. Understanding the effects of these compounds on GSTs and glutathione can provide valuable insights into the complex mechanisms of cellular detoxification processes. These chemicals, while not directly activating GSTO1, can influence the pathways and processes related to GSTO1 and thus affect its activity.