Gastric peroxidase (GPO)

Gastric peroxidase (GPO) is a 70 kDa heme-containing antioxidant enzyme primarily localized within the gastric mucosal cells, where it serves as a critical defense mechanism against oxidative injury (Bandyopadhyay et al., 2002, Life Sciences). Its primary biological function is the scavenging of hydrogen peroxide (H2O2), which prevents the generation of highly reactive hydroxyl radicals that cause lipid peroxidation and cellular damage to the stomach lining (Das et al., 1997, Biochemical Pharmacology). The enzyme is of significant pharmacological interest because its activity is potently inhibited by non-steroidal anti-inflammatory drugs (NSAIDs) such as indomethacin and aspirin, a process that contributes significantly to the development of gastric ulcers and erosions (Chattopadhyay et al., 2006, Free Radical Biology and Medicine). Conversely, endogenous molecules like melatonin have been shown to stimulate or preserve GPO activity, thereby exerting a potent gastroprotective effect against various ulcerogens (Ganguly et al., 2006, Journal of Pineal Research). While GPO is not typically the primary target for systemic drug development, its modulation is a key factor in the pathogenesis of acid-peptic diseases and the therapeutic efficacy of gastroprotective agents.

Other names

Stomach peroxidaseGastric mucosal peroxidase

Catalyzes the reduction of hydrogen peroxide to water, preventing the formation of toxic hydroxyl radicals and subsequent lipid peroxidation in the gastric mucosa (Bandyopadhyay et al., 2002, Life Sciences).