Aldehyde dehydrogenase in drosophila: Developmental and functional aspects

Garcin, Françoise; Hin, Gary Lau You; Côté, Johanne; Radouco-Thomas, Simone; Chawla, S. S.; Radouco-Thomas, C

doi:10.1016/0741-8329(85)90021-7

Cited by 11 publications

(9 citation statements)

References 20 publications

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“…We show the pathway of alcohol metabolism in Figure 3. In the liver, alcohol dehydrogenase (ADH), the key enzyme in alcohol metabolism, mediates the conversion of alcohol to acetaldehyde [13]. Acetaldehyde is rapidly converted to acetate by acetaldehyde dehydrogenase (ALDH) and is eventually metabolized in the muscle to carbon dioxide and water.…”

Section: Metabolism Of Alcoholmentioning

confidence: 99%

The Effect of Inflammatory Cytokines in Alcoholic Liver Disease

Kawaratani

Tsujimoto

Douhara

et al. 2013

Mediators of Inflammation

194

121

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Alcohol is the most common cause of liver disease in the world. Chronic alcohol consumption leads to hepatocellular injury and liver inflammation. Inflammatory cytokines, such as TNF-α and IFN-γ, induce liver injury in the rat model of alcoholic liver disease (ALD). Hepatoprotective cytokines, such as IL-6, and anti-inflammatory cytokines, such as IL-10, are also associated with ALD. IL-6 improves ALD via activation of the signal transducer and activator of transcription 3 (STAT3) and the subsequent induction of a variety of hepatoprotective genes in hepatocytes. IL-10 inhibits alcoholic liver inflammation via activation of STAT3 in Kupffer cells and the subsequent inhibition of liver inflammation. Alcohol consumption promotes liver inflammation by increasing translocation of gut-derived endotoxins to the portal circulation and activating Kupffer cells through the LPS/Toll-like receptor (TLR) 4 pathways. Oxidative stress and microflora products are also associated with ALD. Interactions between pro- and anti-inflammatory cytokines and other cytokines and chemokines are likely to play important roles in the development of ALD. The present study aims to conduct a systemic review of ALD from the aspect of inflammation.

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Section: Metabolism Of Alcoholmentioning

confidence: 99%

The Effect of Inflammatory Cytokines in Alcoholic Liver Disease

Kawaratani

Tsujimoto

Douhara

et al. 2013

Mediators of Inflammation

194

121

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“…The probable in situ distribution of alcohol elimination in larvae is about 60% in the fat body and 30% in the alimentary tract (Heinstra et al, 1989;Fibia, Enjuanes & Gonzfilez, 1989;Anderson, Brown & McDonald, 1991). It appears that the ADH enzyme is involved in the in vivo conversion of acetaldehyde into acetate in larvae, whereas the aldehyde dehydrogenase (ALDH, EC 1.2.1.3) enzyme is mainly responsible for this conversion in adults (Heinstra et al, 1983(Heinstra et al, , 1989Eisses et al, 1985;Geer, Langevin & McKechnie, 1985;Geer, Miller & Heinstra, 1991;Moxon et al, 1985;Garcin et al, 1983Garcin et al, , 1985Eisses, 1989;Anderson & Barnett, 1991;Leal & Barbancho, 1992Miller, Heinstra & Geer, 1992). The biotransformation of the highly toxic compound acetaldehyde has been extensively studied and debated (e.g., David et al, 1978;Deltombe-Lietaert et al, 1979;Gelfand & McDonald, 1980;David, 1988).…”

Section: Metabolic-physiology Of Alcohol Degradationmentioning

confidence: 99%

Evolutionary genetics of the Drosophila alcohol dehydrogenase gene-enzyme system

Heinstra

1993

Genetica

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Evolutionary genetics embodies a broad research area that ranges from the DNA level to studies of genetic aspects in populations. In all cases the purpose is to determine the impact of genetic variation on evolutionary change. The broad range of evolutionary genetics requires the involvement of a diverse group of researchers: molecular biologists, (population) geneticists, biochemists, physiologists, ecologists, ethologists and theorists, each of which has its own insights and interests. For example, biochemists are often not concerned with the physiological function of a protein (with respect to pH, substrates, temperature, etc.), while ecologists, in turn, are often not interested in the biochemical-physiological aspects underlying the traits they study. This review deals with several evolutionary aspects of the Drosophila alcohol dehydrogenase gene-enzyme system, and includes my own personal viewpoints. I have tried to condense and integrate the current knowledge in this field as it has developed since the comprehensive review by van Delden (1982). Details on specific issues may be gained from Sofer and Martin (1987), Sullivan, Atkinson and Starmer (1990); Chambers (1988, 1991); Geer, Miller and Heinstra (1991); and Winberg and McKinley-McKee (1992).

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“…However, there are two viewpoints with respect to the second step of the ethanol degradation pathway in D. melanogaster. According to one viewpoint, this reaction is catalysed by an ALDH enzyme (Lietaert et al, 1982;Garcin et al, 1983Garcin et al, , 1985David et al, 1984), whereas it has also been postulated that Drosophila ADH has dual catalytic properties and can oxidize acetaldehyde as well as ethanol (Heinstra et al, 1983;Eisses et al, 1985;Geer et al, 1985;Moxom et al, 1985). Unlike the mammalian ADH, the ADH of Drosophila is not a metalloenzyme, and it differs significantly in size and amino acid sequence (Jornvall et al, 1981(Jornvall et al, , 1984); consequently, the diverse properties of the ADHs are not surprising.…”

Section: Introductionmentioning

confidence: 99%

The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae

Heinstra

Geer

Seykens

et al. 1989

Biochemical Journal

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Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by electrophoretic methods. Nonetheless, in tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme. The larval fat body probably was the major site of this pathway.

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Aldehyde dehydrogenase in drosophila: Developmental and functional aspects

Cited by 11 publications

References 20 publications

The Effect of Inflammatory Cytokines in Alcoholic Liver Disease

The Effect of Inflammatory Cytokines in Alcoholic Liver Disease

Evolutionary genetics of the Drosophila alcohol dehydrogenase gene-enzyme system

The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae

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