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Differential inhibition by acetazolamide on carbonic anhydrase distribution in the quail kidney: a proposal for a membrane-bound isoenzyme

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Summary

The effects of different concentrations of acetazolamide, a specific carbonic anhydrase inhibitor, have been investigated in the quail kidney. The histochemical patterns, interpreted by means of quantitative analyses proved that 0.1 μm acetazolamide inhibited the enzyme activity in all the reactive tubular segments except for distal tubules. At this site, the reaction product disappeared from the cytoplasm but strong positivity persisted at the apical surface. The luminal staining was still present at higher inhibitor concentrations up to 0.8 μm acetazolamide. Under histophotometric analyses, the residual reactivity proved to be nearly the same at the increasing inhibitor concentrations assayed. The validity of the results was checked by similar investigations in other control tissues.

On the basis of the properties known for carbonic anhydrase in mammalian kidney, we conclude that the luminal membrane staining in the quail distal tubules might be due to a carbonic anhydrase isoenzyme that is similar, both in affinity for acetazolamide and in intracellular localization, to the membrane-bound enzyme purified from mammalian proximal convoluted tubules.

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References

  • Anderson, R. E., Gay, C. V. &Schraer, H. (1982) Carbonic anhydrase localization by light and electron microscopy: a comparison of methods.J. Histochem. Cytochem. 30, 1135–45.

    Google Scholar 

  • Berliner, R. W. (1957) Some aspects of ion exchange in electrolyte transport by the renal tubules. InMetabolic Aspects of Transport across Cell Membranes. (edited byMadison, W. I.) pp. 203–20. University of Wisconsin Press.

  • Bernstein, R. S. &Shraer, R. (1972) Purification and properties of an avian carbonic anhydrase from the erythrocytes ofGallus domesticus.J. Biol. Chem. 247, 1306–22.

    Google Scholar 

  • Brown, D., Zhu, X. L. &Sly, W. S. (1990) Localization of membrane-associated carbonic anhydrase type IV in kidney epithelial cells.Proc. Natl. Acad. Sci. USA 87, 7457–61.

    Google Scholar 

  • Burg, M. &Green, N. (1977) Bicarbonate transport by isolated perfused rabbit proximal convoluted tubules.Am. J. Physiol. 223, F307–14.

    Google Scholar 

  • Carter, N. D., Dodgson, S. J. &Quant, P. A. (1990) Expression of hepatic mitochondrial carbonic anhydrase V.Biochim. Biophys. Acta 1036, 237–41.

    Google Scholar 

  • Churg, A. (1973). Carbonic anhydrase histochemistry: evidence for non-enzymatic reaction and artifact production.Histochemie 36, 293–302.

    Google Scholar 

  • Dodgson, S. J. &Cherian, K. (1989) Mitochondrial carbonic anhydrase is involved in rat renal glucose synthesis.Am. J. Physiol. 257, E791–6.

    Google Scholar 

  • Eveloff, J., Swenson, E. R. &Maren, T. H. (1979) Carbonic anhydrase activity of brush border and plasma membranes prepared from rat kidney cortex.Biochem. Pharmacol. 28, 1434–7.

    Google Scholar 

  • Gabrielli, M. G., Palatroni, P. &Vincenzetti, S. (1990) Renal carbonic anhydrase in the quailCoturnix coturnix japonica. I. Activity and distribution in male and female metanephros.Histochem. J. 22, 579–87.

    Google Scholar 

  • Hansson, H. P. J. (1967). Histochemical demonstration of carbonic anhydrase activity.Histochemie 11, 112–8.

    Google Scholar 

  • Hewett-Emmett, D., Cook, R. G. &Dodgson, S. J. (1986) Carbonic anhydrase from hepatocyte mitochondria of guinea pigs is the product of a novel gene and is not a CA II ‘splisozyme’.Isozyme Bull. 19, 13.

    Google Scholar 

  • Karlmark, B., Agerup, G. &Wistrand, P. J. (1979) Renal proximal tubular acidification: role of brush-border and cytoplasmic carbonic anhydrase.Acta Physiol. Scand. 106, 145–50.

    Google Scholar 

  • Lönnerholm, G. (1974) Carbonic anhydrase histochemistry, a critical study of Hansson's cobalt-phosphate method.Acta Physiol. Scand. (suppl.)418, 1–43.

    Google Scholar 

  • Lönnerholm, G. (1980) Carbonic anhydrase in rat liver and rabbit skeletal muscle: further evidence for the specificity of the histochemical cobalt-phosphate method of Hansson.J. Histochem. Cytochem. 28, 427–33.

    Google Scholar 

  • Lönnerholm, G. (1984) Histochemical localization of carbonic anhydrase in mammalian tissues.Ann. N. Y. Acad. Sci. 429, 369–81.

    Google Scholar 

  • Lucci, M. S., Pucacco, L. R., Dubose, T. D., Jr,Kokko, J. P. &Carter, N. W. (1980) Direct evaluation of acidification by rat proximal tubule: role of carbonic anhydrase.Am. J. Physiol. 238, F372–9.

    Google Scholar 

  • Lucci, M. S., Tinker, J. P., Weiner, I. M. &Dubose, T. D. Jr (1983) Function of proximal tubule carbonic anhydrase defined by selective inhibition.Am. J. Physiol. 245, F443–9.

    Google Scholar 

  • Maren, T. H. (1980a) Kinetics, equilibrium and inhibition in the Hansson histochemical procedure for carbonic anhydrase: a validation of the method.Histochem. J. 12, 183–90.

    Google Scholar 

  • Maren, T. H. (1980b) Current status of membrane-bound carbonic anhydrase.Ann. N. Y. Acad. Sci. 341, 246–58.

    Google Scholar 

  • Maren, T. H. &Ellison, A. C. (1967) A study of renal carbonic anhydrase.Mol. Pharmacol. 3, 503–8.

    Google Scholar 

  • Maren, T. H. &Sanyal, G. (1983) The activity of sulfonamides and anions against the carbonic anhydrases of animals, plants and bacteria.Ann. Rev. Pharmacol. Toxicol. 23, 439–59.

    Google Scholar 

  • Maren, T. H., Friedland, B. R. &Rittmaster, R. S. (1980) Kinetic properties of primitive vertebrate carbonic anhydrases.Comp. Biochem. Biophys. 67B, 69–74.

    Google Scholar 

  • McKinley, D. N. &Whitney, P. L. (1976) Particulate carbonic anhydrase in homogenates of human kidney.Biochim. Biophys. Acta 445, 780–90.

    Google Scholar 

  • McKinney, T. D. &Burg, M. B. (1977). Bicarbonate and fluid absorption by renal proximal straight tubules.Kidney Int. 12, 1–8.

    Google Scholar 

  • Muther, T. F. (1972) A critical evaluation of the histochemical method for carbonic anhydrase.J. Histochem. Cytochem. 20, 319–30.

    Google Scholar 

  • Muther, T. F. (1977) On the lack of specificity of the cobalt-bicarbonate method for carbonic anhydrase.J. Histochem. Cytochem. 25, 1043–50.

    Google Scholar 

  • Palatroni, P., Gabrielli, M. G. &Scattolini, B. (1980) Histochemical localization of carbonic anhydrase in fowl proventriculus.Experientia 36, 678–9.

    Google Scholar 

  • Pitts, R. F. &Alexander, R. S. (1945) The nature of the renal tubular mechanism for acidifying the urine.Am. J. Physiol. 144 239–54.

    Google Scholar 

  • Rector, F. C. Jr. Carter, N. W. &Seldin, D. W. (1965) The mechanism of bicarbonate reabsorption in the proximal and distal tubules of the kidney.J. Clin. Invest. 44 278–90.

    Google Scholar 

  • Ridderstråle, Y. (1976) Intracellular localization of carbonic anhydrase in the frog nephron.Acta Physiol. Scand. 98, 465–9.

    Google Scholar 

  • Rosen, S. &Musser, G. L. (1972) Observations of the specificity of newer histochemical methods for the demonstration of carbonic anhydrase activity.J. Histochem. Cytochem. 20, 951–4.

    Google Scholar 

  • Sanyal, G., Pessah, N. I. &Maren, T. H. (1981) Kinetics and inhibition of membrane bound carbonic anhydrase from canine renal cortex.Biochim. Biophys. Acta 657, 128–37.

    Google Scholar 

  • Sperber, I. (1960) Excretion. InExcretion in Biology and Comparative Physiology of Birds. (edited byA. J. Marshall) pp. 469–92. New York: Academic Press.

    Google Scholar 

  • Storey, B. T., Dodgson, S. J. &Foster, R. E. (1984) Mitochondrial carbonic anhydrase: the purified enzyme.Ann. N. Y. Acad. Sci. 429, 210–1.

    Google Scholar 

  • Sugal, N. &Ito, S. (1980) Carbonic anhydrase, ultrastructural localization in the mouse gastric mucosa and improvements in the technique.J. Hitochem. Cytochem. 28, 511–25.

    Google Scholar 

  • Väänänen, H. K., Carter, N. D. &Dodgson, S. J. (1991) Immunocytochemical localization of mitochondrial carbonic anhydrase in rat tissues.J. Histochem. Cytochem. 39 451–9.

    Google Scholar 

  • Vincent, S. H. &Silverman, D. N. (1980) The carbon dioxide hydration activity of brush-border carbonic anhydrase from the dog kidney.Arch. Biochem. Biophys. 205, 51–6.

    Google Scholar 

  • Whitney, P. L. &Briggle, T. V. (1982) Membrane-associated carbonic anhydrase purified from bovine lung.J. Biol. Chem. 257, 12 056–9.

    Google Scholar 

  • Wistrand, P. J. (1980a) Human renal cytoplasmic carbonic anhydrase. Tissue levels and kinetic properties under near physiological conditions.Acta Physiol. Scand. 109, 239–48.

    Google Scholar 

  • Wistrand, P. J. (1980b) Solubilization and preliminary characterization of membrane-bound carbonic anhydrase.Uppsala J. Med. Sci. 85, 75.

    Google Scholar 

  • Wistrand, P. J. (1984) Properties of membrane-bound carbonic anhydrase.Ann. N. Y. Acad. Sci. 429, 195–206.

    Google Scholar 

  • Wistrand, P. J. &Kinne, R. (1977) Carbonic anhydrase activity of isolated brush border and basal-lateral membranes of renal tubular cells.Pflugers Arch. 370, 121–6.

    Google Scholar 

  • Wistrand, P. J. &Knuuttila, K. G. (1989) Renal membranebound carbonic anhydrase. Purification and properties.Kidney Int. 35, 851–9.

    Google Scholar 

  • Wistrand, P. J., Lindahl, S. &Wahlstrand, T. (1975) Human renal carbonic anhydrase. Purification and properties.Eur. J. Biochem. 57, 189–95.

    Google Scholar 

  • Zhu, X. L. &Sly, W. S. (1990) Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney.J. Biol. Chem. 265, 8795–801.

    Google Scholar 

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  1. Department of Molecular, Cellular and Animal Biology, University of Camerino, via le A. Moro, 62032, Camerino (Mc), Italy

    Maria Gabriella Gabrielli & Pietro Palatroni

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  1. Maria Gabriella Gabrielli
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  2. Pietro Palatroni
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Gabrielli, M.G., Palatroni, P. Differential inhibition by acetazolamide on carbonic anhydrase distribution in the quail kidney: a proposal for a membrane-bound isoenzyme. Histochem J 24, 51–58 (1992). https://doi.org/10.1007/BF01043287

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  • DOI: https://doi.org/10.1007/BF01043287

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