Skip to main content
Log in

Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: Evidence for a locus controlling the inducibility of the liver microsomal isozyme

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Variation in the inducibility of the liver microsomal isozyme of aldehyde dehydrogenase (designated AHD-Cy) by phenobarbital administration was observed among inbred strains and linkage testing stocks of Mus musculus. The phenotypes were inherited in a normal Mendelian fashion with two alleles showing codominance at a proposed regulatory locus (designated Ahd-3r). Strain variation was also observed for the induction of liver AHD-Cy by 17-β-oestradiol administration to ovarectimized female mice. Moreover, this enzyme was elevated in activity by the administration of high (nonphysiological) levels of progesterone. Development studies showed that the liver and kidney AHD-Cy isozyme exhibited low activities in late-stage fetal and neonatal mice and reached adult levels by approximately 6 weeks of age.

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

  • Bolt, H. M. (1979). Metabolism of estrogens—natural and synthetic. Pharmacol. Ther. 4155.

    Google Scholar 

  • Deitrich, R. A. (1971). Genetic aspects of increase in rat liver aldehyde dehydrogenase induced by phenobarbital. Science 173334.

    Google Scholar 

  • Deitrich, R. A., Collins, A. C., and Irwin, U. G. (1972). Genetic influence upon phenobarbital-induced increase in rat liver supernatant aldehyde dehydrogenase activity. J. Biol. Chem. 2477232.

    Google Scholar 

  • Eckfeldt, J. H., Mope, L., Takio, K., and Yonetani, T. (1976). Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes. J. Biol. Chem. 251236.

    Google Scholar 

  • Greenfield, N. J., and Pietruszko, R. (1977). Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes. Biochim. Biophys. Acta 48335.

    Google Scholar 

  • Holmes, R. S. (1978a). Electrophoretic analyses of alcohol dehydrogenase, aldehyde dehydrogenase, aldehyde oxidase, sorbitol dehydrogenase and xanthine oxidase from mouse tissues. Comp. Biochem. Physiol. 61B339.

    Google Scholar 

  • Holmes, R. S. (1978b). Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: Localization of Ahd-1 encoding the mitochondrial isozyme on chromosome 4. Biochem. Genet. 161207.

    Google Scholar 

  • Holmes, R. S., and Timms, G. P. (1980). Mouse aldehyde dehydrogenase genetics: positioning of Ahd-1 on chromosome 4. Anim. Blood Groups Biochem. Genet. 12.

  • Horton, A. A., and Mills, D. J. (1979). Developmental patterns of alcohol dehydrogenase and aldehyde dehydrogenases in homogenates and subcellular fractions of rat liver. Mech. Age. Dev. 11363.

    Google Scholar 

  • Horton, A. A., and Barrett, M. C. (1975). The subcellular localization of aldehyde dehydrogenase in rat liver. Arch. Biochem. Biophys. 167426.

    Google Scholar 

  • Koivulo, T., and Koivusalo, M. (1975). Different forms of rat liver aldehyde dehydrogenase and their subcellular distribution. Biochim. Biophys. Acta 3979.

    Google Scholar 

  • Lee, T. (1979). Characterization of fatty alcohol: NAD oxidoreductase from rat liver. J. Biol. Chem. 2542892

    Google Scholar 

  • Marjanen, L. (1972). Intracellular localization of aldehyde dehydrogenase in rat liver. Biochem. J. 127633.

    Google Scholar 

  • Monder, C., and Wang, P. T. (1973). Oxidation of 21-dehydrocorticosteroids to steroidal 20-oxo-21-oic acids by an aldehyde dehydrogenase of sheep adrenal. J. Biol. Chem. 2488547.

    Google Scholar 

  • Nakaysau, H., Mihara, K., and Sato, R. (1978). Purification and properties of a membrane-bound aldehyde dehydrogenase from rat liver microsomes. Biochem. Biophys. Res. Commun. 83697.

    Google Scholar 

  • Orrenus, S., Das, M., and Gnosspelius, Y. (1969). Overall biochemical effects of drug induction of liver microsomes. In Gillette, J. R., Conney, A. H., Cosmides, G. J., Estabrook, R. W., Fonts, J. R., and Mannering G. J., (eds.), Microsomes and Drug Oxidations Academic Press, New York and London.

    Google Scholar 

  • Petersen, D. R., Collins, A. C., and Deitrich, R. A. (1977). Role of liver cytosolic aldehyde dehydrogenase isozymes in control of blood acetaldehyde concentrations. J. Pharmacol. Exp. Ther. 201471.

    Google Scholar 

  • Redmond, G., and Cohen, G. (1971). Induction of liver acetaldehyde dehydrogenase. Possible role in ethanol tolerance after exposure to barbiturates. Science 171387.

    Google Scholar 

  • Siew, C., Deitrich, R. A., and Irwin, E. G. (1976). Localization and characterization of rat liver mitochondrial aldehyde dehydrogenases. Arch. Biochem. Biophys. 176638.

    Google Scholar 

  • Sjoblom, M., Pilstrom, L., and Morland, J. (1978). Activity of alcohol dehydrogenase and acetaldehyde dehydrogenases in the liver and placenta during development of the rat. Enzyme 23108.

    Google Scholar 

  • Smolen, A., Atkinson, N., and Petersen, D. R. (1980). The role of liver cytosolic aldehyde dehydrogenase in ethanol metabolism in DBA and C57BL mice. In Thurman, R. G. (ed.), Alcohol and Aldehyde Metabolizing Systems—IV Plenum Press, New York and London, pp. 627–634.

    Google Scholar 

  • Tietz, A., Lindberg, M., and Kennedy, E. P. (1964). A new pteridine-requiring enzyme system for the oxidation of glyceryl ethers. J. Biol. Chem. 2473923.

    Google Scholar 

  • Timms, G. P., and Holmes, R. S. (1981). Genetics of aldehyde dehydrogenase isozymes in the mouse: Evidence for multiple loci and localization of Ahd-2 on chromosome 19. Genetics (in press).

  • Tottmar, S. O. C., Pettersson, H., and Kiessling, K.-H. (1973). The subcellular distribution and properties of aldehyde dehydrogenases in rat liver. Biochem. J. 135577.

    Google Scholar 

  • Watanabe, T., Kanai, M., Isobe, M., and Ozawa, N. (1980). Hepatic microsomal conversion of pregnenolone to 3β,6β-trihydroxy-5α-pregnan20-one via pregnenolone α and β epoxides. Biochem. Biophys. Res. Commun. 92977.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

This research was funded in part by the Australian Research Grants Committee and the Australian Associated Brewers. GPT gratefully acknowledges a Griffith University Postgraduate Research Award.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Timms, G.P., Holmes, R.S. Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: Evidence for a locus controlling the inducibility of the liver microsomal isozyme. Biochem Genet 19, 1223–1236 (1981). https://doi.org/10.1007/BF00484575

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484575

Key words

Navigation