Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of pure ethanol and some alcoholic beverages on acid secretion and metabolism were examined in the isolated toad gastric mucosa. Pure ethanol applied to the luminal side or to the submucosal side at low concentrations (2%-10%) was a potent stimulant of acid secretion, whereas high concentrations (greater than or equal to 20%) were inhibitory. Cimetidine and calcium-free solutions did not abolish the secretory effect of ethanol. Beer and wine, but not rum and whisky, caused a significant stimulation of acid secretion. Respiration was progressively increased by ethanol at concentrations between 2% and 20%. This effect was not affected by cimetidine or by SCH 28080, an inhibitor of the gastric hydrogen-potassium-stimulated adenosine triphosphatase. Ethanol (10%) significantly increased by 46% the tissue lactate-pyruvate ratio. The oxidations of glucose, butyrate, and acetate were progressively reduced by low concentrations of ethanol (5% and 10%). The results indicate that (a) low concentrations of ethanol and alcoholic beverages with low ethanol content are direct stimulants of acid secretion and (b) the secretory and metabolic effects of low concentrations of ethanol seem to be mediated via its oxidation.
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PMID:Secretory and metabolic effects of ethanol in the isolated amphibian gastric mucosa. 190 55

Indirect evidence indicates the presence of an active H+/K+ antiporter for the secretion of acid in the distal colon. It was examined whether the H+/K+ antiporter in the rabbit distal colon was hydrogen-potassium-stimulated adenosine triphosphatase (H+,K(+)-ATPase), which acts as a proton pump in the gastric mucosa. For this purpose, four monoclonal antibodies against hog gastric H+,K(+)-ATPase were raised. Three monoclonal antibodies dose-dependently inhibited the ouabain-insensitive gastric ATP-ase activity. Antibody HK4001 completely inhibited the ATPase activity. In indirect immunofluorescence studies, all four monoclonal antibodies stained H+,K(+)-ATPase in gastric mucosae of various animal species. Two monoclonal antibodies including antibody HK4001 cross-reacted with H+,K(+)-ATPase located in crypts of the transverse and descending colon and rectum of rabbits. Because the other two antibodies did not cross-react with the H+,K(+)-ATPase in the colon, this colonic enzyme is similar but not identical to gastric H+,K(+)-ATPase. On the other hand, HK4001 and SCH 28080 did not inhibit ouabain-sensitive K(+)-dependent ATPase activity in the guinea pig distal colon, and the antibodies did not stain the enzyme in the tissue. Therefore, ouabain-sensitive H+/K+ antiporter in the guinea pig is not similar to ouabain-insensitive rabbit colonic H+,K(+)-ATPase.
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PMID:The presence of H+,K(+)-ATPase in the crypt of rabbit distal colon demonstrated with monoclonal antibodies against gastric H+,K(+)-ATPase. 217 Feb 21

The renal effects of dopamine are mainly mediated via the dopamine-1 receptor (D1 receptor). This receptor is recruited from intracellular compartments to the plasma membrane by dopamine and atrial natriuretic peptide (ANP), via adenylyl cyclase activation. We have studied whether isoproterenol, a beta-adrenoceptor (beta-AR) agonist that may interact with dopamine in the regulation of rat renal Na+, K+-adenosine triphosphatase (ATPase) activity, can recruit D1 receptors to the plasma membrane. The spatial regulation of D1 receptors was examined using confocal microscopy techniques in LLCPK cells and the functional interaction between dopamine and isoproterenol was examined by studying their effects on Na+, K+-ATPase activity in microdissected single proximal tubular segments from rat. Isoproterenol was found to translocate the D1 receptors from the interior of the cell towards the plasma membrane. The recruitment of dopamine 1 receptors was found to be cyclic adenosine phosphate (cAMP) dependent, while protein kinase C (PKC) activation was not involved. The functional studies on Na+, K+-ATPase activity showed that the effect of isoproterenol was abolished by a D1-like receptor antagonist (SCH 23390), and mediated via protein kinase A (PKA) and PKC dependent pathways. The results provide an explanation for the interaction between G protein-coupled receptors. The effects of isoproterenol on Na+, K+-ATPase activity can be explained by a heterologous recruitment of D1 receptors to the plasma membrane.
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PMID:beta-Adrenoceptor agonist sensitizes the dopamine-1 receptor in renal tubular cells. 1216 72