Skip to main content
SpringerLink
Log in

Cellular localization of the class I alcohol dehydrogenase transcript in adult rat tissues

  • Papers
  • Published:
The Histochemical Journal Aims and scope Submit manuscript

Summary

The mammalian class I alcohol dehydrogenase is the principal enzyme responsible for ethanol metabolism. While it is regarded primarily as a liver-specific enzyme, class I alcohol dehydrogenase is known to be present in a number of extrahepatic tissues. The purpose of the current study is to define the tissue and cellular distribution of the dehydrogenase transcript in four rat tissues previously shown to contain high levels of mRNA: the liver, the proximal small intestine, the colon and the testis. Localization of the transcript was examined in formalin-fixed, paraffin-embedded rat tissues by in situ hybridization using radioactively labelled antisense rat alcohol dehydrogenase RNA probe. In the liver, the dehydrogenase message is localized primarily to the perivenous hepatocytes. In the proximal small intestine and the colon, the message follows a vertical gradient of distribution along the crypt-villus and the crypt-surface epithelium axes, respectively, with the base of the crypt exhibiting the greatest concentration. In the testis, the message is localized primarily to cells in the interstitium. These findings illustrate a highly compartmentalized nature of distribution of the class I alcohol dehydrogenase transcript in the tissues studied and may help to elucidate the metabolic functions of this enzyme in these tissues.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Algar, E. M., Seeley, T. L. & Holmes, R. S. (1983) Purification and molecular properties of mouse alcohol dehydrogenase isozymes. Eur. J. Biochem. 137, 139–47.

    Google Scholar 

  • Boleda, M D., Juliá, P., Moreno, A. & Parés, X. (1989) Role of extrahepatic alcohol dehydrogenase in rat ethanol metabolism. Arch. Biochem. Biophys. 274, 74–81.

    Google Scholar 

  • Boller, K., Arpin, M., Pringault, E., Mangeat, P. & Reggio, H. (1988) Differential distribution of villin and villin mRNA in mouse intestinal epithelial cells. Differentiation 39, 51–7.

    Google Scholar 

  • Bosron, W. F. & Li, T. K. (1987) Catalytic properties of human liver alcohol dehydrogenase isoenzymes. Enzyme 37, 19–28.

    Google Scholar 

  • Buehler, R., Hess, M. & VonWartburg, J.-P. (1982) Immunohistochemical localization of human liver alcohol dehydrogenase in liver tissue, cultured fibroblasts, and HeLa cells. Am. J. Pathol. 108, 89–99.

    Google Scholar 

  • Canto, M. F., Oliva, M. M., Potter, J. J., Mezey, E. & Yang, V. W. (1992) Enhancer-site downstream binding protein activity is enriched in rat tissues that express the class I alcohol dehydrogenase gene. Biochem. Biophys. Res. Commun. 188, 684–89.

    Google Scholar 

  • Chandrasena, G., Sunitha, I., Lau, C., Nanthakumar, N. N. & Henning, S. J. (1992) Expression of sucrase-isomaltase mRNA along the villus-crypt axis in the rat small intestine. Cell Mol. Biol. 38, 243–54.

    Google Scholar 

  • Chen, L., Sidner, R. A. & Lumeng, L. (1992) Distribution of alcohol dehydrogenase and the low Km form of aldehyde dehydrogenase in isolated perivenous and periportal hepatocytes in rats. Alcoholism Clin. Exp. Res. 16, 23–9.

    Google Scholar 

  • Crabb, D. W. & Edenberg, H. J. (1986) Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence. Gene 48, 287–91.

    Google Scholar 

  • Engeland, K. & Maret, W. (1993) Extrahepatic, differential expression of four classes of human alcohol dehydrogenase. Biochem. Biophys. Res. Commun. 193, 47–53.

    Google Scholar 

  • Estonius, M., Danielsson, C., Persson, H., Jörnvall, H. & Höög, J. (1993) Distribution of alcohol and sorbitol dehydrogenases. Assessment of mRNA species in mammalian tissues. Eur. J. Biochem. 215, 497–503.

    Google Scholar 

  • Ffrench-Constant, C. & Hynes, R. O. (1988) Patterns of fibronectin gene expression and splicing during cell migration in chicken embryos. Development 104, 369–82.

    Google Scholar 

  • Iseki, S. & Kondo, H. (1990) Light microscopic localization of hepatic fatty acid binding protein mRNA in jejunal epithelia of rats using in situ hybridization, immunohistochemical, and autoradiographic techniques. J. Histochem. Cytochem. 38, 111–5.

    Google Scholar 

  • Israel, Y., Kalant, H., Orrego, H., Khanna, J. M., Videla, L. & Phillips, J. M. (1975) Experimental alcohol-induced hepatic necrosis: suppression by propylthiouracil. Proc. Natl Acad. Sci. USA 72, 1137–41.

    Google Scholar 

  • Iturriaga, H., Ugarte, G. & Israel, Y. (1980) Hepatic vein oxygenation, liver blood flow, and the rate of ethanol metabolism in recently abstinent alcoholic patients. Eur. J. Clin. Invest. 10, 211–8.

    Google Scholar 

  • Juliá, P., Farres, J. & Parés, X. (1987) Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties. Eur. J. Biochem. 162, 179–89.

    Google Scholar 

  • Kato, S., Ishii, H., Aiso, S., Yamashita, S., Ito, D. & Tsuchiya, M. (1990) Histochemical and immunohistochemical evidence for hepatic zone 3 distribution of alcohol dehydrogenase in rats. Hepatology 12, 66–9.

    Google Scholar 

  • Mezey, E. & Potter, J. J. (1983) Separation and partial characterization of multiple forms of rat liver alcohol dehydrogenase. Arch. Biochem. Biophys. 225, 787–94.

    Google Scholar 

  • Murono, E. P. & Fisher-Simpson, V. (1984) Ethanol directly increases dihydrotestosterone conversion to 5α-androstan-3β,17β-diol and 5α-androstan-3α,17β-diol in rat Leydig cells. Biochem. Biophys. Res. Commun. 121, 558–65.

    Google Scholar 

  • Oliva, M. M., Wu, T. C. & Yang, V. W. (1993) Isolation and characterization of a differentiation-dependent gene in the human colonic cell line HT29–18. Arch. Biochem. Biophys. 302, 183–92.

    Google Scholar 

  • Ouellette, A. J., Greco, R. M., James, M., Frederick, D., Naftilan, J. & Falon, J. T. (1989) Developmental regulation of cryptdin, a corticostatin/defensin precursor mRNA in mouse small intestinal crypt epithelium. J. Cell. Biol. 108, 1687–95.

    Google Scholar 

  • Parés, X., Cederlund, E., Moreno, A., Saubi, H., Höög, J.-O. & Jörnvall, H. (1992) Class IV alcohol dehydrogenase (the gastric enzyme): structural analysis of human σσ-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class. FEBS Lett. 303, 69–72.

    Google Scholar 

  • Pestalozzi, D. M., Buhler, R., VonWartburg, J. P. & Hess, M. (1983) Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract. Gastroenterology 85, 1011–6.

    Google Scholar 

  • Popper, H. & Lieber, C. S. (1980) Histogenesis of alcoholic fibrosis and cirrhosis in the baboon. Am. J. Pathol. 98, 695–716.

    Google Scholar 

  • Qulali, M., Ross, R. A. & Crabb, D. W. (1991) Estradiol induces class I alcohol dehydrogenase activity and mRNA in kidney of female rats. Arch. Biochem. Biophys. 288, 406–13.

    Google Scholar 

  • Traber, P. G. (1990) Regulation of sucrase-isomaltase gene expression along the crypt-villus axis of rat small intestine. Biochem. Biophys. Res. Commun. 173, 765–73.

    Google Scholar 

  • Trezise, A. E. O. & Buchwald, M. (1991) In vivo cell-specific expression of the cystic fibrosis transmembrane conductance regulator. Nature 353, 434–7.

    Google Scholar 

  • Voisin, T., Rouyer-Fessard, C. & Laburthe, M. (1990) Distribution of common peptide YY-neuropeptide Y receptor along rat intestinal villus-crypt axis. Am. J. Physiol. 258, G753–9.

    Google Scholar 

  • Weiser, M. M., Sykes, D. E. & Killen, P. D. (1990) Rat intestinal basement membrane synthesis. Epithelial versus nonepithelial contributions. Lab. Invest. 62, 325–30.

    Google Scholar 

  • Yamauchi, M., Potter, J. J. & Mezey, E. (1988a) Lobular distribution of alcohol dehydrogenase in the rat liver. Hepatology 8, 243–7.

    Google Scholar 

  • Yamauchi, M., Potter, J. J. & Mezey, E. (1988b) Detection and localization of immunoreactive alcohol dehydrogenase protein in the rat testis. Alcoholism Clin. Exp. Res. 12, 143–6.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Medicine, The Johns Hopkins University School of Medicine, 21205, Baltimore, MD, USA

    Thomas G. Tietjen & Vincent W. Yang

  2. Department of Gynaecology and Obstetrics, The Johns Hopkins University School of Medicine, 21205, Baltimore, MD, USA

    Corey H. Mjaatvedt

  3. Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 21205, Baltimore, MD, USA

    Vincent W. Yang

Authors
  1. Thomas G. Tietjen
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Corey H. Mjaatvedt
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Vincent W. Yang
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Tietjen, T.G., Mjaatvedt, C.H. & Yang, V.W. Cellular localization of the class I alcohol dehydrogenase transcript in adult rat tissues. Histochem J 26, 526–532 (1994). https://doi.org/10.1007/BF00157898

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00157898

Keywords

Search

Navigation