Acetaldehyde oxidation inDrosophila null-mutants for alcohol dehydrogenase

Garcin, Françoise; Larochelle, Christian; Hin, Gary Lau You; Côté, Johanne

doi:10.1007/bf01970027

Cited by 8 publications

(2 citation statements)

References 15 publications

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“…While there is very little doubt that the ADH activity is produced by the protein coded at the polymorphic, much studied, Adh locus (Grell et al, 1965;Oakeshott et al, 1982), the origin of the ALDH is less clear. Two enzymes at least, the aldehyde oxidase (AO) produced by the Aldox locus and an aldehyde dehydrogenase are able to metabolize aldehydes (Sofer and Hatkoff, 1972;Garcin et al, 1985;Moxom et al, 1985). Moreover, it was also argued that, at least in larvae, ADH was also able to transform acetaldehyde into acetate (Eisses et al, 1985;Geer et al, 1985Geer et al, , 1993.…”

Section: Discussionmentioning

confidence: 98%

“…However, this enzyme does not seem to play a significant role in uitro since mutants lacking A 0 not only survive quite well in ethanol media but also can even use acetaldehyde as an energy source (David, et al, 1984). Therefore, others enzymes have been proposed to explain the in uiuo transformation of acetaldehyde into acetate (Garcin et al, 1985;Moxom et al, 1985). It was suggested that ADH was involved in the in uiuo conversion of acetaldehyde into acetate in larvae, whereas an aldehyde dehydrogenase enzyme (ALDH) (EC 1.2.1.3 ) was responsible for this conversion in adults (Eisses et al, 1985;Geer et al, 1993;Barbancho, 1992, 1993).…”

Section: Parallel Changes In Enzyme Activity and Oviposition Behaviormentioning

confidence: 94%

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Parallel changes in enzyme activity and oviposition behavior in adults ofDrosophila melanogastersubmitted to alcohols, acetaldehyde or acetone

Elamrani¹,

David²,

Idaomar

2001

Invertebrate Reproduction & Development

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Two geographic populations of D. melanogaster, French and African, whic.. differ in their frequencies at the Adh locus and their ethanol tolerance, were tested for their oviposition site preference, mortality and activities of two enzymes involved in alcohol metabolism. To investigate the oviposition choice towards ethanol, 2-propanol, acetaldehyde et acetone, females of the two populations of D. melanogaster were exposed to a choice situation opposing a medium free-alcohol to a medium supplemented with one of the tested compounds. We noticed that the avoidance of media containing one the two studied alcohols, acetaldehyde or acetone, increased during the experiment.The most repellent medium for ovipositing females was that supplemented with 2-propanol or acetone. Besides, the study of female mortality on attractant or repellent media revealed that the most repulsive media were also the most lethal. Moreover, the treatment with ethanol, 2-propanol, acetaldehyde or acetone led to a reduction in alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activities. A strong inhibition of ADH occurs (78.57%) in females a few days after the treatement with the tested products. Compared to ADH activity, ALDH activity was less reduced (5 1.78%). We suggest that fly mortality and the fly's aversion to alcoholic media might be linked to the decline of ADH and ALDH activities. The toxic effects of the used compounds appear more clearly in African flies than in French ones.

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Section: Discussionmentioning

confidence: 98%

Section: Parallel Changes In Enzyme Activity and Oviposition Behaviormentioning

confidence: 94%

Parallel changes in enzyme activity and oviposition behavior in adults ofDrosophila melanogastersubmitted to alcohols, acetaldehyde or acetone

Elamrani¹,

David²,

Idaomar

2001

Invertebrate Reproduction & Development

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The involvement of alcohol dehydrogenase and aldehyde dehydrogenase in alcohol/aldehyde metabolism in Drosophila melanogaster

Anderson

Barnett

1991

Genetica

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In this study we have examined the roles of alcohol dehydrogenase, aldehyde oxidase, and aldehyde dehydrogenase in the adaptation of Drosophila melanogaster to alcohol environments. Fifteen strains were characterized for genetic variation at the above loci by protein electrophoresis. Levels of in vitro enzyme activity were also determined. The strains examined showed considerable variation in enzyme activity for all three gene-enzyme systems. Each enzyme was also characterized for coenzyme requirements, effect of inhibitors, subcellular location, and tissue specific expression. A subset of the strains was chosen to assess the physiological role of each gene-enzyme system in alcohol and aldehyde metabolism. These strains were characterized for both the ability to utilize alcohols and aldehydes as carbon sources as well as the capacity to detoxify such substrates. The results of the above analyses demonstrate the importance of both alcohol dehydrogenase and aldehyde dehydrogenase in the in vivo metabolism of alcohols and aldehydes.

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Dietary ethanol and lipid synthesis in Drosophila melanogaster

1985

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When cultured on a defined diet, ethanol was an efficient substrate for lipid synthesis in wild-type Drosophila melanogaster larvae. At certain dietary levels both ethanol and sucrose could displace the other as a lipid substrate. In wild-type larvae more than 90% of the flux from ethanol to lipid was metabolized via the alcohol dehydrogenase (ADH) system. The ADH and aldehyde dehydrogenase activities of ADH were modulated in tandem by dietary ethanol, suggesting that ADH provided substrate for lipogenesis by degrading ethanol to acetaldehyde and then to acetic acid. The tissue activity of catalase was suppressed by dietary ethanol, implying that catalase was not a major factor in ethanol metabolism in larvae. The activities of lipogenic enzymes, sn-glycerol-3-phosphate dehydrogenase, fatty acid synthetase (FAS), and ADH, together with the triacylglycerol (TG) content of wild-type larvae increased in proportion to the dietary ethanol concentration to 4.5% (v/v). Dietary ethanol inhibited FAS and repressed the accumulation of TG in ADH-deficient larvae, suggesting that the levels of these factors may be subject to a complex feedback control.

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Acetaldehyde oxidation inDrosophila null-mutants for alcohol dehydrogenase

Cited by 8 publications

References 15 publications

Parallel changes in enzyme activity and oviposition behavior in adults ofDrosophila melanogastersubmitted to alcohols, acetaldehyde or acetone

Parallel changes in enzyme activity and oviposition behavior in adults ofDrosophila melanogastersubmitted to alcohols, acetaldehyde or acetone

The involvement of alcohol dehydrogenase and aldehyde dehydrogenase in alcohol/aldehyde metabolism in Drosophila melanogaster

Dietary ethanol and lipid synthesis in Drosophila melanogaster

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