Sulfation of glycolipids by human gastric mucosa in disease

The activity levels of sulfotransferase enzymes involved in the transfer of sulfate from 3′-phosphoadenosine 5′-phosphosulfale to mucosal membrane and mucus gel glycolipids were studied in fundic and antral mucosal biopsies of patients with severe and chronic gastritis, gastric atrophy, gastric ulcer, and gastric cancer. With sulfotransferase which catalyzes the sulfation of mucus triglucosyl glyceroglucoliptd increase in enzyme activity over the control was observed in patients with chronic and severe gastritis, and gastric atrophy, while a decrease in activity was noted in patients wiih gastric ulcer and gastric cancer. The differences were significant al ρ < 0.001 for severe gastritis, gastric ulcer and gastric cancer. The increase in activity of sulfotransferase enzyme involved in the sulfation of membrane galac-losylceramide over the control was observed in antral and fundic mucosa of all patients. Significant (p < 0.001) differences were found in patients with severe gastritis, gastric atrophy and gastric ulcer. The results indicate thai considerable changes in the activities of the mucosal sulfotransferase enzymes involved in the synthesis of membrane and secretory sulfolipids occur in gastric disease.