Skip to main content
Log in

Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) Activity in the Human Pancreas

  • Published:
Digestive Diseases and Sciences Aims and scope Submit manuscript

Abstract

Ethanol metabolism in the pancreas occurs predominantly by way of an nonoxidative pathway to fatty acid ethyl esters but oxidative routes to acetaldehyde also may contribute to injury of pancreatic cells. Three metabolic systems are responsible for the oxidative metabolism of ethanol, among which the cytochrome P-4502E1 and alcohol dehydrogenase have been found in the pancreas. The aims of this study were to detect ADH and ALDH in the human pancreas and to assess which ADH isoenzymes are present in this organ. ADH activity was measured by the photometric method and ADH isoenzyme activity was determined using sensitive and specific substrates. ALDH activity was measured by the fluorometric method. We have shown that the activities of ADH and ALDH are present in the pancreas, although the activity of ALDH was not proportionally as low as ADH activity. The class III isoenzyme exhibited the highest activity of all ADH isoenzymes tested and it was about 7 times higher than the activity of class I. The activities of classes II and IV were low. The activities of ADH isoenzymes of classes I, II, and III in the pancreas of men were significantly higher than in women. This study demonstrates that alcohol dehydrogenase and aldehyde dehydrogenase are present in the pancreas.

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

  1. Laposata EA, Lange LG: Presence of nonoxidative ethanol metabolism in human organs commonly damaged by ethanol abuse. Science 231:497-499, 1986

    Google Scholar 

  2. Hammamoto Y, Yamada S, Hirayama C: Nonoxidative metabolism of ethanol in the pancreas; implication in alcoholic pancreatic damage. Biochem Pharmacol 39:241-245, 1990

    Google Scholar 

  3. Werner J, Laposata M, Fernandez-del Castillo C, Saghir M, Iozzo RV, Lewndrowski KB, Warshaw AL: Pancreatic injury in rats induced by fatty acid ethyl ester, a nonoxidative metabolite of alcohol. Gastroenterology 113:286-294, 1997

    Google Scholar 

  4. Haber PS, Apte MV, Applegate TL, Norton ID, Korsten MA, Pirola RC, Wilson JS: Metabolism of ethanol by rat pancreatic acinar cells. J Lab Clin Med 132:294-302, 1998

    Google Scholar 

  5. Boleda MD, Julia P, Moreno A, Pares X: Role of extrahepatic alcohol dehydrogenase in rat ethanol metabolism. Arch Biochem Biophys 274:74-81, 1989

    Google Scholar 

  6. Norton ID, Apte MV, Haber PS, McCanghan GW, Pirola RC, Wilson JS: Cytochrome P-4502E1 is present in rat pancreas and is induced by chronic ethanol administration. Gut 42:426-430, 1998

    Google Scholar 

  7. Werner J, Saghir M, Castillo CF, Warshaw AL, Laposata M: Linkage of oxidative and nonoxidative ethanol metabolism in the pancreas and toxicity of nonoxidative ethanol metabolites for pancreatic acinar cells. Surgery 129:736-744, 2001

    Google Scholar 

  8. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ: Protein measurement with the Folin phenol reagent. J Biol Chem 193:265-275, 1951

    Google Scholar 

  9. Wierzchowski J, Dafeldecker WP, Holmquist B, Vallee BL: Fluorimetric assay for isozymes of human alcohol dehydrogenase. Anal Biochem 178:57-62, 1989

    Google Scholar 

  10. Koivusalo M, Baumann M, Uotila L: Evidence for the identity of glutathionedependent formaldehyde dehydrogenase and class III alcohol dehydrogenase. FEBS Lett 257:105-109, 1989

    Google Scholar 

  11. Pestallozzi D, Buhler R, von Wartburg JP, Hess M: Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract. Gastroenterology 85:1011-1016, 1983

    Google Scholar 

  12. Skursky L, Kovar J, Stachova M: A sensitive assay for alcohol dehydrogenase activity in blood serum. Anal Biochem 89:65-71, 1979

    Google Scholar 

  13. Wierzchowski J, Wroczynski P, Laszuk K, Interewicz E: Fluorimetric detection of aldehyde dehydrogenase activity in human blood, saliva, and organ biopsies and kinetic differentiation between class I and II isozymes. Anal Biochem 245:69-78, 1997

    Google Scholar 

  14. Estival A, Clemente F, Ribef A: Ethanol metabolism by the rat pancreas. Toxicol Appl Pharmacol 61:155-165, 1981

    Google Scholar 

  15. Julia P, Farres J, Pares X: Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties. Eur J Biochem 162:179-189, 1987

    Google Scholar 

  16. Julia P, Pares X, Jörnvall H: Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases. Eur J Biochem 172:73-83, 1988

    Google Scholar 

  17. Bosron WF, Li T-K: Catalytic properties of human liver alcohol dehydrogenase isoenzymes. Enzyme 37:19-28, 1987

    Google Scholar 

  18. Jörnvall H, Höög J-O: Nomenclature of alcohol dehydrogenases. Alcohol Alcohol 30:153-161, 1995

    Google Scholar 

  19. Riveros-Rosas H, Julian-Sanchez A, Pina E: Enzymology of ethanol and acetaldehyde metabolism in mammals. Arch Med Res 28:453-471, 1997

    Google Scholar 

  20. Norton JD, Apte MV, Lux O, Haber PS, Pirola RC, Wilson JS: Chronic ethanol administration causes oxidative stress in the rat pancreas. J Lab Clin Med 131:442-446, 1998

    Google Scholar 

Download references

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Chrostek, L., Jelski, W., Szmitkowski, M. et al. Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) Activity in the Human Pancreas. Dig Dis Sci 48, 1230–1233 (2003). https://doi.org/10.1023/A:1024134520823

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1024134520823

Navigation