Archives of Toxicology

, Volume 41, Issue 3, pp 207–214 | Cite as

Acetaldehyde level in the blood and liver aldehyde dehydrogenase activities in trichloroethylene-treated rats

  • Suehiro Nakanishi
  • Eiko Shiohara
  • Miyoko Tsukada
  • Hiromi Yamazaki
  • Keiko Okumura
Original Investigations
Received:

Abstract

The liver NAD+-dependent aldehyde dehydrogenase (AldDH) activity and the acetaldehyde level in the blood during ethanol metabolism after trichloroethylene (trichlene) exposure were studied in rats. Trichlene inhalation caused large elevations in acetaldehyde levels during ethanol metabolism and caused decreases in the activity of the AldDH with a low Km value in mitochondrial and soluble fractions of liver cells. No significant effects were found in the activity of the high Km-enzyme in mitochondrial, soluble and microsomal fractions. Time course of inhibition of the mitochondrial low Km-enzyme and that of elevations in acetaldehyde levels during ethanol metabolism after trichlene exposure were similar. These findings suggest that acetaldehyde formed from ethanol in vivo is oxidized primarily by the mitochondrial low Km-enzyme.

Key words

Trichloroethylene Ethanol metabolism Acetaldehyde Aldehyde dehydrogenases 
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Büttner, H.: Aldehyd- und Alkoholdehydrogenase-Aktivität in Leber und Niere der Ratte. Biochem. Z. 341, 300–314 (1965)Google Scholar
  2. Forsander, O. A., Hillbom, M. E., Lindros, K. O.: Influence of thyroid function on the acetaldehyde level of blood and liver of intact rats during ethanol metabolism. Acta Pharmacol. Toxicol. (Kbh.) 27, 410–416 (1969)Google Scholar
  3. Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)Google Scholar
  4. Marchner, H., Tottmar, O.: Influence of the diet on the metabolism of acetaldehyde in rats. Acta Pharmacol. Toxicol. (Kbh.) 38, 59–71 (1976)Google Scholar
  5. Matsumura, R., Masamura, E., Tsukada, M., Nakanishi, S.: Ethanol oxidation by the hepatic microsomes after prolonged ethanol treatment. Med. J. Shinshu Univ. 15, 291–292 (1971)Google Scholar
  6. Müller, G., Spassowski, M., Henschler, D.: Metabolism of trichloroethylene in man. III. Interaction of trichloroethylene and ethanol. Arch. Toxicol. (Berl.) 33, 173–189 (1975)Google Scholar
  7. Nakanishi, S., Shiohara, E., Tsukada, M., Iijima, Y.: Aldehyde dehydrogenase activities after treatment with phenobarbital in Long-Evans rats. Jap. J. Stud. Alcohol 12, 5–12 (1977)Google Scholar
  8. Parilla, R., Ohkawa, K., Lindros, K. O., Zimmerman, U.-J. P., Kobayashi, K., Williamson, J. R.: Functional compartmentation of acetaldehyde oxidation in rat liver. J. Biol. Chem. 249, 4926–4933 (1974)Google Scholar
  9. Raskin, N. H.: Alcoholism or acetaldehydism? N. Engl. J. Med. 292, 422–423 (1975)Google Scholar
  10. Tottmar, S. O. C., Pettersson, H., Kiessling, K.-H.: The subcellular distribution and properties of aldehyde dehydrogenases in rat liver. Biochem. J. 135, 577–586 (1973)Google Scholar
  11. Tottmar, S. O. C., Pettersson, H., Kiessling, K.-H.: Aldehyde dehydrogenases in rat liver. In: Alcohol and Aldehyde Metabolizing System (R. G. Thurman, T. Yonetani, J. R. Williamson, B. Chance, eds.), pp. 147–160. New York-London: Academic Press 1974Google Scholar
  12. Truitt, E. B., Jr., Walsh, M. J.: The role of acetaldehyde in the actions of alcohol. In: The Biology of Alcoholism (B. Kissin, H. Begleiter, eds.), Vol. 1, pp. 161–195. New York: Plenum Press 1971Google Scholar

Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Suehiro Nakanishi
    • 1
  • Eiko Shiohara
    • 1
  • Miyoko Tsukada
    • 1
  • Hiromi Yamazaki
    • 1
  • Keiko Okumura
    • 1
  1. 1.Department of Pharmacology, Faculty of MedicineToyama Medical and Pharmaceutical UniversityToyamaJapan

Personalised recommendations