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Die Bedeutung der HCO −3 -ATPase in der H+/HCO −3 -Sekretion

The role of HCO −3 -ATPase in H+/HCO −3 -secretion

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Summary

Active buffer transport, e.g. H+-secretion by stomach and kidney and HCO −3 -secretion by pancreas and salivary glands, is linked with the presence of a HCO −3 stimulated ATP-Phosphohydrolase. In contrast to (Na+-K−)-ATPase which is considered to be equivalent to the Na+ pump, the HCO −3 -ATPase requires onlyone ion for activation and is insensitive to ouabain. The HCO −3 -ATPase is found in the plasma membrane of the epithelia, but in contrast to the (Na+-K+)-ATPase it is located in the luminal cell border. The activity of the HCO −3 -ATPase changes in parallel along with the rate of active buffer transport, a finding which underlines its importance as a transport enzyme. Several disorders of buffer transport are described which are possibly associated with a defect of the HCO −3 -ATPase system.

Zusammenfassung

Dem aktiven Puffertransport, der an Magen und Niere zur H+-Sekretion, am Pankreas und Speicheldrüse zur HCO −3 -Sekretion führt, ist eine ATP-Phosphohydrolase zugeordnet, die typischerweise durch HCO −3 -Ionen stimuliert wird. Im Gegensatz zur (Na+-K+)-ATPase, dem Transportenzym des Na+-Transportes, benötigt dieses Enzym nurein Ion und ist Ouabain unempfindlich. Die HCO −3 -ATPase ist an die Plasmamembran der einzelnen Epithelien gebunden, jedoch im Gegensatz zur (Na+-K+)-ATPase luminal lokalisiert. Das Enzym ändert seine Aktivität proportional zur Rate des aktiven Puffertransportes, was seine Bedeutung als Transportenzym unterstreicht. Es werden Krankheitsbilder des gestörten Puffertransportes aufgeziegt, bei denen möglicherweise der Defekt im HCO −3 -ATPase-System zu suchen ist.

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Literatur

  1. Bersimbaev, R.I., Argutinskaya, S.V., Salganik, R.I.: The stimulating action of gastrin pentapeptide and histamine on adenyl cyclase activity in rat stomach. Experientia27, 1389–1390 1971

    PubMed  Google Scholar 

  2. Bieck, P.R., Oates, J.A., Robison, G.A., Adkins, R.B.: Cyclic AMP in the regulation of gastric secretion in dogs and humans. Amer. J. Physiol.224, 158–164 (1973)

    PubMed  Google Scholar 

  3. Blum, A.L., Shah, G., Pierre, T.St., Helander, F., Sung, C.P., Sachs, G.: Properties of soluble ATPase of gastric mucosa II. Effect of HCO −3 . Biochim. Biophys. Acta249, 101–113 (1971)

    PubMed  Google Scholar 

  4. Bonting, S.L., Caravaggio, L.L.: Studies on sodium-potassium activated adenosine triphosphatase. V. Correlation of enzyme activity with cation flux in six tissues. Arch. Biochem. Biophys.101, 37–46 (1963)

    Google Scholar 

  5. Brønstedt, J.N.: Zur Theorie der chemischen Reaktionsgeschwindigkeit. Zeitschrift f. Physikal. Chemie102, 169 (1923)

    Google Scholar 

  6. Domschke, W., Domschke, S., Classen, M., Demling, J.: Histamine and cyclic 3′5′-AMP in gastric acid secretion. Nature (London)241, 454–455 (1973)

    PubMed  Google Scholar 

  7. Hogben, C.A.M.: Electrolytes in Biological Systems. A.M. Shanes, ed. Amer. Physiol. Soc., Washington, D.C., p. 176, 1955

    Google Scholar 

  8. Imamura, A.: The effects of carbondioxide and bicarbonate on chloride fluxes across frog gastric mucosa. Biochim. Biophys. Acta196, 245–253 (1970)

    PubMed  Google Scholar 

  9. Kasbekar, D.K., Durbin, R.P.: An adenosine triphosphatase from frog gastric mucosa. Biochim. Biophys. Acta105, 472–482 (1965)

    PubMed  Google Scholar 

  10. Katz, A.I., Lindheimer, M.D.: Renal sodium-and potassium activated adenosine triphosphosphatase and sodium reabsorption in the hypothyroid rats. J. Clin. Invest.52, 796–804 (1973)

    PubMed  Google Scholar 

  11. Kinne-Saffran, E.M., Kinne, R.: Presence of bicarbonate stimulated ATPase in the brush border microvillus membranes of the proximal tubule. Proc. Soc. Exper. Biol. Med.146, 751–753 (1974)

    Google Scholar 

  12. Kitahara, S., Imamura, A.: Chloride transport, acid secretion and carbonic anhydrase activity in frog stomach. Life Sciences5, 215–218 (1966)

    Google Scholar 

  13. Knauf, H.: Grundsätzliches zur Funktion von Biomembranen. Verh. dtsch. Ges. inn. Med. Bd 81 (1975) im Druck

  14. Knauf, H., Simon, B., Wais, U.: Non-specific inhibition of membrane ATPase by amiloride A comparative in vivo and in vitro study with ouabain Naunyn Schmiedeberg's Arch. Pharmakol. subm. f. publ. (1975)

  15. Knauf, H., Lübcke, R.: unveröffentlichte Befunde

  16. Koenig, C., Vial, J.D.: A histochemical study of adenosine triphosphatase in the toad (bufo spinulosus) gastric mucosa. J. Histochem. Cytochem.18, 340–353 (1970)

    PubMed  Google Scholar 

  17. Kreuz, W.: Structural principles of biomembranes. Angewandte Chemie11, 551–567 (1972)

    PubMed  Google Scholar 

  18. Loeschke, K., Uhlich, E., Kinne, R.: Stimulation of sodium transport and (Na+-K+)-ATPase activity in the hypertrophing rat cecum. Pflügers Arch.346, 233–242 (1974)

    Google Scholar 

  19. Martonosi, A., Donley, I.R., Pucell, A.G., Halpin, R.A.: Sarcoplasmic Reticulum: XI. The mode of involvement of phospholipids in the hydrolysis of ATP by sarcoplasmic reticulum membranes. Arch. Biochem. Biophys.144, 529–540 (1971)

    PubMed  Google Scholar 

  20. Meissner, G., Fleischer, S.: The role of phospholipids in Ca2+-ATPase activity of sarcoplasmic reticulum. Biochim. biophys. Acta (Amst.)255, 19–33 (1972)

    PubMed  Google Scholar 

  21. Miyagi, Sh., Shoemaker, Ch.P., Powers, S.R.: Carbon dioxide metabolism in the intact mammalian stomach. Surgery59, 1083–1091 (1966)

    PubMed  Google Scholar 

  22. Narumi, S., Kanno, M.: Effects of gastric acid stimulants and inhibitors in the activities of HCO −3 stimulated, Mg2+ dependent ATPase and carbonic anhydrase in rat gastric mucosa. Biochim. biophys. Acta (Amst.)311, 80–89 (1973)

    PubMed  Google Scholar 

  23. Nakajima, S., Hirschowitz, B.I., Sachs, G.: Studies on adenyl cyclase in necturus gastric mucosa. Arch. biochem. Biophys.143, 123–126 (1971)

    PubMed  Google Scholar 

  24. dePont, J.J.H.H.M., Hansen, T., Bonting, S.L.: An anion-sensitive ATPase in lizard gastric mucosa. Biochim. biophys. Acta (Amst.)311, 80–89 (1972)

    Google Scholar 

  25. Racker, E.: Adenosine triphosphatase and oxidative phosphorylation. Fed. Proc.21, 54A (1962)

  26. Ray, T.K., Forte, J.G.: Soluble and bound protein kinases of rabbit gastric secretory cells. Biochim. Biophys. Res. Commun.61, 1199–1206, 1974

    Google Scholar 

  27. Ray, T.K., Forte, J.G.: Studies on phosphodiesterases from oxyntic cells of bullfrog gastric mucosa. I. Intracellular localization, partial purification, and properties. Arch. Biochem. Biophys.155, 24–31 (1973)

    PubMed  Google Scholar 

  28. Sachs, G., Mitch, W., Hirschowitz, B.I.: Frog gastric mucosal ATPase. Proc. Soc. Exper. Biol. Med.119, 1023–1027 (1965)

    Google Scholar 

  29. Sachs, G., Shah, G., Strych, A., Cline, G., Hirschowitz, B.I.: Properties of ATPase of gastric mucosa. III. Distribution of HCO −3 -stimulated ATPase in gastric mucosa. Biochim. biophys. Acta (Amst.)266, 625–638 (1972)

    PubMed  Google Scholar 

  30. Sachs, G., Wiebelhaus, V.D., Blum, A.L., Hirschowitz, B.I.: Role of ATP and ATPase in gastric acid secretion. In: Gastric Secretion. Ed. Sachs, G., Heinz, E., Ullrich, K.J., Academic Press, New York and London, p. 321–343, 1972

    Google Scholar 

  31. Schmidt, U., Schmid, J., Schmid, H., Dubach, V.C.: Sodium-and potassium activated ATPase. A possible target of aldosterone. J. Clin. Invest.55, (3) 629–631 (1975)

    Google Scholar 

  32. Schwartz, E.: A magnesium dependent bicarbonate stimulated ATPase in the avian oviduct: Subcellular localization and relationship to bicarbonate transport. Fed. Proc.520, R1314 (1974)

  33. Schwartz, I.L., Shlatz, L.J., Kinne-Saffran, E.M., Kinne, R.: Target cell polarity and membrane phosphorylation in relation to the mechanism of action of antidiuretic hormone. Proc. Nat. Acad. Sci. (USA)71, 2595–2599 (1974)

    PubMed  Google Scholar 

  34. Schulz, I.: Pancreatic bicarbonate transport. In: Gastric Secretion. Ed. Sachs, G., Heinz, E., Ullrich, K.J. Academic Press, New York and London, p. 363–379 (1972)

    Google Scholar 

  35. Simon, B.: The HCO −3 -stimulated-ATPase in cat and rabbit pancreatic tissue. In: Gastric Secretion. Ed. Sachs, G., Heinz, E., Ullrich, K.J. Academic Press, New York and London, p. 345–348, 1972

    Google Scholar 

  36. Simon, B., Kinne, R., Sachs, G.: The presence of a HCO −3 -ATPase in pancreatic tissue. Biochim. Biophys. Acta282, 293–300, 1972

    PubMed  Google Scholar 

  37. Simon, B., Thomas, L.: HCO −3 -ATPase from mammalian pancreas. Properties and its arrangement with other enzyme activities. Biochim. Biophys. Acta288, 434–442 (1972)

    PubMed  Google Scholar 

  38. Simon, B., Kinne, R., Knauf, H.: The presence of a HCO −3 -ATPase in glandula submandibularis of rabbit. Pflügers Arch.337, 177–183 (1972)

    Google Scholar 

  39. Simon, B.: Charakterisierung einer HCO −3 -stimulierbaren-ATPase; ihre Rolle im H+/HCO −3 -Transport des exokrinen Pankreas. Habilitationsschrift, Frankfurt 1974

  40. Simon, B.: New biochemical aspects of bicarbonate transport in mammalian pancreas. Proceed. 12th. Intern. Congress Intern. Med., Tel Aviv, 1974. S. Karger, Basel, Switzerland, im Druck (1975)

  41. Simon, B., Kather, H.: Neue Aspekte des HCO −3 -Transportes des exokrinen Pankreas. Verh. dtsch. Ges. inn. Med. Bd. 81, im Druck (1975)

  42. Simon, B., Zimmerschied, G., Kinne, R.: Role of phospholipids in the HCO −3 -ATPase activity of plasma membranes from dog gastric mucosa. Hoppe-Seyler's Zeitschr. physiol. Chem., im Druck (1975)

  43. Simon, B.: Unveröffentlichte Befunde

  44. Skou, J.C.: In: Current Topics in Bioenergetics, Ed.: R. Sanadi. Academic Press, New York and London 1971

    Google Scholar 

  45. Spenney, J.G., Strych, A., Price, A.H., Helander, H.F., Sachs, G.: V. Preparation of membranes and mitochondria by zonal centrifugation. Biochim. Biophys. Acta311, 545–564 (1973)

    PubMed  Google Scholar 

  46. Stahl, W.L.: Role of phospholipid in the Na+, K+-stimulated adenosine triphosphatase system of brain microsomes. Arch. Biochem. Biophys.154, 56–67 (1973)

    Google Scholar 

  47. Sung, C.P., Jenkins, B.C., Burns, L.R., Hackney, V., Spenney, J.G., Sachs, G., Wiebelhaus, V.D.: Adenyl and guanyl cyclase in rabbit gastric mucosa. Amer. J. Physiol.225, 1359–1363 (1973)

    PubMed  Google Scholar 

  48. Turbeck, O.B., Nedergaard, S., Kruse, H.: An anion-stimulated adenosine triphosphatase from the potassium transporting mid-gut of the larva of hyalophora. Biochim. Biophys. Acta163, 354–361 (1968)

    PubMed  Google Scholar 

  49. Tanaka, R., Abood, L.G.: Phospholipid requirement of Na+-K+ activated adenosine triphosphatase from rat brain. Arch. Biochem. Biophys.108, 47–52 (1964)

    PubMed  Google Scholar 

  50. Wais, U., Knauf, H.: H+-transport and microsomal HCO −3 -ATPase in salivary duct epithelium. Pflügers Arch.355, R 76 (1975)

    Google Scholar 

  51. Wais. U., Knauf, H.: H+ Transport and membrane-bound HCO −3 -ATPase in salivary duct epithelium. Pflügers Arch. submitted f. publication (1975)

  52. Wais, U., Knauf, H., Kreutz, W.: HCO −3 -ATPase in renal cortex related to acid base disturbances. In Vorbereitung (1975)

  53. Wiebelhaus, V.D., Sung, C.P., Helander, H.F., Shah, G., Blum, A.L., Sachs, G.: Solubilization of anion ATPase from necturus oxyntic cells. Biochim. Biophys. Acta241, 49–56 (1971)

    PubMed  Google Scholar 

  54. Wizemann, V., Schulz, I.: Influence of amphotericin, amiloride, ionophores and 2,4-dinitrophenol on the secretion of the isolated cat's pancreas. Pflügers Arch.339, 317–338 (1973)

    Google Scholar 

  55. Wizemann, V., Christian, A.L., Wiechmann, J., Schulz, I.: The distribution of membrane bound enzymes in the acini and ducts of the cat pancreas. Pflügers Arch.347, 39–47 (1974)

    Google Scholar 

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  1. Medizinische Universitätslinik Heidelberg, Germany

    B. Simon & H. Knauf

  2. Medizinische Universitätsklinik Freiburg, Germany

    B. Simon & H. Knauf

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Simon, B., Knauf, H. Die Bedeutung der HCO −3 -ATPase in der H+/HCO −3 -Sekretion. Klin Wochenschr 54, 97–104 (1976). https://doi.org/10.1007/BF01468786

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