Abstract
The effect of isopropanol ingestion on a further tolerance to ethanol and isopropanol, and its relationship with the Adh locus, have been studied using Drosophila melanogaster selected for tolerance to ethanol. For this purpose, AdhF AdhF, AdhF AdhS and AdhS AdhS flies were independently pretreated with 2 per cent isopropanol and then further exposed to solutions of 10 per cent ethanol or of 2 per cent isopropanol. Afterwards, the ability to tolerate both alcohols, and the ADH activities of the surviving flies were compared with those of flies not pretreated with isopropanol. After isopropanol ingestion, the flies of all three Adh genotypes shown much higher sensitivity to ethanol than to isopropanol although the opposite results were observed in flies not pretreated with isopropanol. Isopropanol treatment decreased the ADH activity in flies of all three genotypes within a range varying from 73 per cent (females FF) to 93 per cent (males FS), the remaining ADH activity being between 2 to 3 times higher in FF than in FS and SS flies. The reduction in ADH activity was associated with the phenomenon of ADH isozyme interconversion. After the isopropanol pretreatment, the most isopropanol tolerant flies (FF) were also the most ADH active ones. Therefore, the adaptative significance of the isozyme conversion is questioned.
Similar content being viewed by others
Article PDF
References
Anderson, S M, and McDonald, J F. 1981. A method for determining the in vivo stability of Drosophila alcohol dehydrogenase (E.C.1.1.1.1.). Biochem Genet, 19, 411–419.
Atrian, S, and Gonzàlez-Duarte, R. 1985. An aldo-keto reductase activity in Drosophila melanogaster and Drosophila hydei: A possible function in alcohol metabolism. Comp Biochem Physiol, 81B, 949–952.
Ayala, F J, Powell, J R, Tracey, M L, Mourão, C A, and Pérez-Salas, S. 1972. Enzyme variability in the Drosophila willistoni group. IV. Genie variation in natural populations of Drosophila willistoni. Genetics, 70, 113–139.
Barbancho, M, Sánchez-Cañete, F J S, Dorado, G, and Pineda, M. 1987. Relation between tolerance to ethanol and alcohol dehydrogenase (ADH) activity in Drosophila melanogaster: Selection, genotype and sex effects. Heredity, 58, 443–450.
Batterham, P, Lovett, J A, Starmer, W T, and Sullivan, D T. 1983. Differential regulation of duplicate alcohol dehydrogenase genes in Drosophila mojavensis. Dev Biol, 96, 346–354.
Chambers, G K, McDonald, J F, McElresh, M, and Ayala, F J. 1978. Alcohol oxidizing enzymes in 13 Drosophila species. Biochem Genet, 16, 757–767.
David, J R, Bocquet, C, Arens, M F, and Fouillet, P. 1976. Biological role of alcohol dehydrogenase in the tolerance of Drosophila melanogaster to aliphatic alcohols: Utilization of an ADH-null mutant. Biochem Genet, 14, 989–997.
David, J R, Bocquet, C, Van Herrewege, J, Fouillet, P, and Arens, M F. 1978. Alcohol metabolism in Drosophila melanogaster: Uselessness of the most active aldehyde oxidase produced by the Aldox locus. Biochem Genet, 16, 203–211.
David, J R, Daly, K, and Van Herrewege, J. 1984. Acetal-dehyde utilization and toxicity in Drosophila adults lacking alcohol dehydrogenase or aldehyde oxidase. Biochem Genet, 22, 1015–1029.
David, J R, Van Herrewege, J, De Scheemaeker-Louis, M, and Pla, E. 1981. Drosophila alcohol dehydrogenase: Detoxification of isopropanol and acetone, substances not used in energy metabolism. Heredity, 47, 263–268.
Day, T H, Hillier, P C, and Clarke, B. 1974. Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochem Genet, 11, 141–153.
Van Delden, W, Kamping, A, and Van Dijk, H. 1975. Selection at the alcohol dehydrogenase locus in Drosophila melanogaster. Experientia, 31, 418–420.
Deltombe-Lietaert, M C, Delcour, J, Lenelle-Monfort, N, and Elens, A. 1979. Ethanol metabolism in Drosophila melanogaster. Experientia, 35, 579–581.
Dorado, G, and Barbancho, M. 1984. Differential responses in Drosophila melanogaster to environmental ethanol: Modification of fitness components at the Adh locus. Heredity, 53, 309–320.
Fontdevila, A, Santos, M, and González, R. 1980. Genotype-isopropanol interaction in the Adh locus in Drosophila buzzatii. Experientia, 36, 398–400.
Gelfand, L J, and McDonald, J F. 1983. Relationship between alcohol dehydrogenase (ADH) activity and behavioral response to environmental alcohol in five Drosophila species. Behav Genet, 13, 281–293.
Gonzàlez-Duarte, R, and Atrian, S. 1986. Metabolic response to alcohol ingestion in Drosophila hydei. Heredity, 56, 123–128.
Gonzàlez-Duarte, R, and Vilageliu, Li. 1985. Metabolic response to ethanol and isopropanol in D. funebris and D. immigrans. Comp Biochem Physiol, 80C, 189–193.
Heinstra, P W H, Eisses, K Th, Schoonen, W G E J, Aben, W, De Winter, A J, Horst, Aben W, De Winter, A J, Van Der Horst, D J, Van Marrewijk, W J A, Beenakkers, A M Th, Scharloo, W, and Thörig, G E W. 1983. A dual function of alcohol dehydrogenase in Drosophila. Genetica, 60, 129–137.
Van Herrewege, J, David, J R, and Grantham, R. 1980. Dieatry utilization of aliphatic alcohols by Drosophila. Experientia, 36, 846–847.
Jacobson, K B, Murphy, J B, and Hartman, F C. 1970. Isozymes of Drosophila alcohol dehydrogenase. I. Isolation and interconversion of different forms. J Biol Chem, 245, 1075–1083.
Jacobson, K B, Murphy, J B, Knopp, J A, and Ortiz, J R. 1972. Multiple forms of Drosophila alcohol dehydrogenase. III. Conversion of one form to another by nicotinamide adenine dinucleotide or acetone. Arch Biochem Biophys, 149, 22–35.
McDonald, F J, and Avise, J C. 1976. Ecidence for the adaptative significance of enzyme activity levels: Interspecific variation in α-GPDH and ADH in Drosophila. Biochem Genet, 14, 347–355.
Morgan, P. 1975. Selection acting directly on an enzyme polymorphism. Heredity, 35, 124–127.
Oakeshott, J G. 1976. Biochemical differences between alcohol dehydrogenases of Drosophila melanogaster. Aust J Biol Sci, 29, 365–373.
Papel, I, Henderson, M, Van Herrewege, J, David, J, and Sofer, W. 1979. Drosophila alcohol dehydrogenase activity in vitro and in vivo: Effects of acetone feeding. Biochem Genet, 17, 553–563.
Sánchez-Cañete, F J S, Dorado, G, and Barbancho, M. 1986. Ethanol and isopropanol detoxification associated with the Adh locus of Drosophila melanogaster. Heredity, 56, 167–175.
Schwartz, M, O'Donnell, J, and Sofer, W. 1979. Origin of the multiple forms of alcohol dehydrogenase from Drosophila melanogaster. Arch Biochem Biophys, 194, 365–378.
Schwartz, M, and Sofer, W. 1976. Diet-induced alterations in distribution of multiple forms of alcohol dehydrogenase in Drosophila. Nature, 263, 129–131.
Vilageliu, Li, and Gonzàlez-Duarte, R. 1980. Effect of ethanol and isopropanol on the activity of alcohol dehydrogenase, viability and life-span in Drosophila melanogaster and Drosophila funebris. Experientia, 36, 828–829.
Vilageliu, Li, and Gonzàlez-Duarte, R. 1984. Alcohol dehydrogenase from Drosophila funebris and Drosophila immigrans: Molecular and evolutionary aspects. Biochem Genet, 22, 797–815.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Guillén, E., Sánchez-Cañete, F., Garrido, J. et al. Intergenotypic effect of isopropanol ingestion in the further detoxification of ethanol and isopropanol in Drosophila melanogaster. Heredity 59, 405–411 (1987). https://doi.org/10.1038/hdy.1987.149
Received:
Issue date:
DOI: https://doi.org/10.1038/hdy.1987.149
This article is cited by
-
Tolerance to 1-pentene-3-ol and to 1-pentene-3-one in relation to alcohol dehydrogenase (ADH) and aldo keto reductase (AKR) activities inDrosophila melanogaster
Biochemical Genetics (1990)
-
ADH activity and ethanol tolerance in third chromosome substitution lines in Drosophila melanogaster
Heredity (1989)
-
Participation of Drosophila melanogaster alcohol dehydrogenase (ADH) in the detoxification of 1-pentene-3-ol and 1-pentene-3-one
Heredity (1988)
