Skip to main content
Log in

Comparative immunohistolocalization of carbonic anhydrase isozymes I, II and III in the equine and bovine digestive tract

  • Published:
The Histochemical Journal Aims and scope Submit manuscript

Summary

Immunohistochemical localizations of carbonic anhydrase isozymes (CA-I, CA-II and CA-III) in equine and bovine digestive tracts were studied. In the horse, epithelial cells in both the oesophagus and non-glandular part of the stomach lacked all three isozymes. In contrast, surface epithelial and parietal cells in the glandular region of the stomach showed reactivity for CA-II. In the small intestine, absorptive columnar cells covering the villi in the duodenum were positive for CA-II. The epithelium of the jejunum and ileum lacked all three isozymes. In the large intestine, CA-II was detected in the columnar cells in the upper part of the crypt. In cattle, epithelial cells of the oesophagus showed reactions for CA-I and CA-III but not for CA-II. Although the absorptive epithelial cells of the small intestine lacked CA-I, CA-II and CA-III, those of the upper part of large intestine crypts were heavily stained for all three isozymes.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Aafjes, J. H. Carbonic anhydrase in the wall of the forestomach of cows. Br. Vet. J. 123 252–55

  • Argenzio, R. A. (1984) Introduction to Gastrointestinal. In Duke's Physiology of Domestic Animals. Digestion, Absorption and Metabolism function (edited by Swenson, M. J.). pp. 290–310.

  • Armstrong, J. M., Mayers, D. V., Verpoorte, J. A. & Edsall, J. T. (1966) Purification and properties of human erythrocyte carbonic anhydrase. J. Biol. Chem. 241, 5137–49.

    Google Scholar 

  • Asari, M., Sasaki, K., KanoY. & Nishita, T. (1989) Immunohistochemical localization of carbonic anhydrase isozymes I, II and III in the bovine salivary glands and stomach. Arch. Histol. Cytol. 52, 337–44.

    Google Scholar 

  • Asari, M., Sasaki, K., Kano, Y. & Nishita, T. (1991) Immunohis-tolocalization of the carbonic anhydrase isozymes I, II and III in equine salivary glands. Okajimas Folia Anat. Jap. 67, 467–72.

    Google Scholar 

  • Carpentier, P., Chetail, M. & Fournie, J. (1985) Carbonic anhydrase in the rat salivary glands: distribution and ultrastructural localization. Biol. Cell. 54, 241–50.

    Google Scholar 

  • Carter, M. J. & Parsons, D. S. (1970) The purification and properties of carbonic anhydrase from guinea-pig erythrocytes and mucosae of the gastrointestinal tract. Biochem. J. 120, 797–808.

    Google Scholar 

  • Carter, M. J. (1971) The carbonic anhydrase in the rumen epithelial tissue of the ox. Biochem. Biophys. Acta 235, 222–36.

    Google Scholar 

  • Carter, N. D., Hewett-Emmett, D., Jeffery, S. & Tashian, R. E. (1981) Testosterone-induced, sulfonamide-resistant carbonic anhydrase isozyme of rat liver is indistinguishable from skeletal muscle carbonic anhydrase. Fed. Eur. Biochem. Soc. Lett. 128, 114–8.

    Google Scholar 

  • DeutschH. F. (1987) Carbonic anhydrase. Int. J. Biochem. 19, 101–13.

    Google Scholar 

  • Deutsch, H. F., Funakoshi, S., Fujita, T., Taniguchi, N. & Hirai, H. (1972) Isolation in crystalline form and properties of six horse erythrocyte carbonic anhydrases. J. Biol. Chem. 247, 4499–502.

    Google Scholar 

  • Engberg, P., Millquist, E., Pohl, G. & Lindskog, S. (1985) Purification and some properties of carbonic anhydrase from bovine skeletal muscle. Arch. Biochem. Biophys. 241, 628–38.

    Google Scholar 

  • Funakoshi, S. & Deutsch, H. F. (1971) Human carbonic anhydrase. VI levels of isozymes in old and younger erythrocytes and in various tissues. J. Biol. Chem. 246, 1088–92.

    Google Scholar 

  • Galfi, P., Kutas, F. & Neogrady, S. (1982) Immunohistochemical detection of bovine ruminal carbonic anhydrase isoenzyme. Histochemistry 74, 577–84.

    Google Scholar 

  • Gros, G. & Dodgson, S. J. (1988) Velocity of CO2 exchange in muscle and liver. Ann. Rev. Physiol. 50, 669–94.

    Google Scholar 

  • Hennigar, R. A., Schulte, B. A. & Spicer, S. S. (1983) Immunolo-calization of carbonic anhydrase isozymes in rat and mouse salivary and exorbital lacrimal glands. Anat. Rec. 207, 605–14.

    Google Scholar 

  • Igarashi, S., KanoY., Nishita, T., Amasaki, H. & Asari, M. (1992) Comparison of the distribution of carbonic anhydrase isozymes (CA-I, CA-II, CA-III) in the rat gastrointestinal tract. J. Vet. Med. Sci. 54, 535–9.

    Google Scholar 

  • IkejimaT. & Ito, S. (1984) Carbonic anhydrase in mouse salivary glands and saliva: a histochemical, immunohistochemical, and enzyme activity study. J. Histochem. Cytochem. 32, 625–35.

    Google Scholar 

  • Jacobson, E. D. (1978) The Gastrointestinal System: Essentials of Human Physiology (edited by Rase, G.). pp. 370–443. Chicago Year Book Medical Publ.

  • Jeffery, S. (1991) Immunological Methods for Detection and Quantification of CA Isozymes In The Carbonic Anhydrases: Cellular Physiology and Molecular Genetic, (edited by Dodgson, S. J., Tashian, R. E., Gros, G. & Carter, N. D.). pp. 153–9.

  • JefferyS., Carter, N. D. & SmithA. (1986) Immunocytochemical localization of carbonic anhydrase isozymes I, II and III in rat skeletal muscle. J. Histochem. Cytochem. 34, 513–6.

    Google Scholar 

  • Karhukorpi, E-K. (1991) Carbonic anhydrase II in rat acid secreting cells: comparison of osteoclasts with gastric parietal cells and kidney intercalated cells. Acta Histochem. 90, 11–20.

    Google Scholar 

  • Kumpulainen, T. (1979) Immunohistochemical localization of human carbonic anhydrase isozymes C. Histochemistry 62, 271–80.

    Google Scholar 

  • Leblond, C. P. (1965) The time dimension in histology. Am J. Anat. 116, 1–28.

    Google Scholar 

  • Nishita, T. & Deutsch, H. F. (1981) Isolation of equine muscle carbonic anhydrase in crystalline form. Biochem. Biophys. Res. Commun. 103, 573–80.

    Google Scholar 

  • Nishita, T., Matsushita, H. & Kai, M. (1987) Immunocytochemical localization of carbonic anhydrase III in equine skeletal muscle. Equine Vet. J. 19, 509–13.

    Google Scholar 

  • Nishita, T., Oshige, H., Matsushita, H., Kano, Y. & Asari, M. (1989) The immunohistolocalization of carbonic anhydrase III in the submandibular gland of rats and hamsters. Histochemical J. 21, 8–14.

    Google Scholar 

  • Nishita, T., Kinoshita, C., Maegaki, M. & Asari, M. (1990) Immunohistochemical studies of the carbonic anhydrase isozymes in the bovine placenta. Placenta 11, 329–36.

    Google Scholar 

  • Register, A. M., Koester, M. K. & Noltman, E. A. (1978) Discovery of carbonic anhydrase in rabbit skeletal muscle and evidence for its identity with basic muscle protein. J. Biol. Chem. 253, 4143–52.

    Google Scholar 

  • Shima, K., Tashiro, K., Hibi, N., Tsukada, Y. & Hirai, H. (1984) Carbonic anhydrase III: immunohistochemical localization of the carbonic anhydrase isozymes for their function in normal and pathologic cells. Ann. N.Y. Acad. Sci. 429, 382–97.

    Google Scholar 

  • Spicer, S. S., Stoward, P. J. & Tashian, R. E. (1979) The immunohistolocalization of carbonic anhydrase in rodent tissue. J. Histochem. Cytochem. 27, 820–31.

    Google Scholar 

  • Spicer, S. S., Ge, Z-H., Tashian, R. E., Hazen-Martin, D. J. & Schultz, B. A. (1990) Comparative distribution of carbonic anhydrase isozymes III and II in rodent tissues. Am. J. Anat. 187, 55–64.

    Google Scholar 

  • Swenson, E. R. (1991) Distribution and functions of carbonic anhydrase in the gastrointestinal tract. In The Carbonic Anhydrases: Cellular Physiology and Molecular Genetics (edited by Dodgson, S. J., Tashian, R. E., Gros, G. & Carter, N. D.), pp. 265–87.

  • Tashian, R. E. (1989) The carbonic anhydrase: widening perspectives on their evolution, expression and function. BioEssays 10, 186–92.

    Google Scholar 

  • Väänänen, H. K. & Autio-Harmainen, H. (1987) Carbonic anhydrase III: a new histochemical marker for myoepithelial cells. J. Histochem. Cytochem. 35, 683–6.

    Google Scholar 

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

    Google Scholar 

  • Wilbur, K. M. & Anderson, N. G. (1948) Electrometric and colorimetric determination of carbonic anhydrase. J. Biol. Chem. 176, 147–54.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sasaki, K., Igarashi, SI., Amasaki, T. et al. Comparative immunohistolocalization of carbonic anhydrase isozymes I, II and III in the equine and bovine digestive tract. Histochem J 25, 304–311 (1993). https://doi.org/10.1007/BF00159122

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00159122

Keywords

Navigation