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Glutathione S-transferase (GST) inhibitors block enzymes that conjugate glutathione to electrophiles. Conjugation makes reactive drugs, carcinogens and oxidative stress products more water soluble and easier to export from cells. Cytosolic GSTs fall into several classes, including alpha, mu, pi and omega, with distinct substrate preferences. GST pi 1 (GSTP1) is abundant in many tumor cells and binds c-Jun N-terminal kinase (JNK), which restrains stress signaling. Ezatiostat is a glutathione analog that is converted in cells to TLK117, an inhibitor of GSTP1-1, and is also listed as ezatiostat hydrochloride. NBDHEX also targets GSTP1-1, whereas GSTO1-IN-1 acts on the omega-class enzyme GSTO1. Natural products such as coniferyl ferulate and benastatin B are listed as broader GST inhibitors.
Cafestol palmitate is identified as a glutathione S-transferase activator. It enhances the activity of this enzyme in murine models, potentially contributing to improved detoxification processes. In addition, Cafestol palmitate demonstrates modest inhibitory effects on COX-2, suggesting a potential role in inflammation-related research applications.
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