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Query: UMLS:C1332347 (ADH)
 2,230 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The distribution of genetic variants (or gene markers) for alcohol dehydrogenase, aldehyde dehydrogenase, aldehyde oxidase, and aldehyde reductase isozymes has been examined among 12 inbred strains of mice. Electrophoretic variants are described for the major liver and stomach alcohol dehydrogenase isozymes (ADH-A2 and C2); liver, kidney, and stomach aldehyde dehydrogenase isozymes (AHD-1; AHD-2; AHD-4); a liver-specific aldehyde reductase (AHR-A2); and a liver aldehyde oxidase isozyme (AOX-2). Genetically determined activity variants were observed for a testis-specific aldehyde dehydrogenase (AHD-6); liver and kidney aldehyde reductase isozymes (AHR-3 and AHR-4); and the major liver AOX isozyme (AOX-1). These variants may serve as useful gene markers in alcohol research involving animal model studies with inbred strains in mice.
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PMID:Genetic variants of enzymes of alcohol and aldehyde metabolism. 293 67

The genetic variability of one of the liver isozymes of aldehyde oxidase (AOX-B2 or AOX-2) and the stomach isozyme of alcohol dehydrogenase (ADH-C2) has been examined among strains of mice. Evidence is presented for a fourth allele of Aox-2 and a third allele of Adh-3. The hybrid allozyme pattern for mouse liver AOX was consistent with a dimeric subunit structure for this enzyme.
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PMID:Aldehyde oxidase and alcohol dehydrogenase genetics in the mouse. New alleles for the Aox-2 and Adh-3 loci. 637 55

Electrophoretic and activity variants for the C2 isozyme of alcohol dehydrogenase (ADH-C2), the mitochondrial isozyme of aldehyde dehydrogenase (AHD-A2) and aldehyde oxidase isozymes (AOX-1; AOX-2) in inbred strains of Mus musculus were used to map the genes encoding these enzymes on the mouse genome. Adh-3 (encoding ADH-C2) was localized on chromosome 3 and was closely linked to a cis-acting regulator locus (Adh-3-t), which determined ADH-C2 activity in male reproductive tissues. Ahd-1 (encoding AHD-A2) was found on chromosome 4 near Gpd-1 (encoding the liver isozyme of glucose-6-phosphate dehydrogenase), whereas the aldehyde oxidase loci (Aox-1, Aox-2) were closely linked on chromosomes 1 near Id-1 (encoding isocitrate dehydrogenase).
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PMID:Genetic regulation of alcohol dehydrogenase, aldehyde dehydrogenase and aldehyde oxidase isozymes in the mouse. 699 77

Six Drosophila melanogaster strains were constructed from two isofemale lines. The strains had four allele combinations at the alcohol dehydrogenase (Adh) and octanol dehydrogenase (Odh) loci, while all alpha-glycerophosphate dehydrogenase (alpha Gpdh), malate dehydrogenase (Mdh), and aldehyde oxidase (Aldox) alleles were identical. Second-instar and early and late third-instar larvae were exposed to different concentrations of ethanol (0, 5, and 7.5%) and 3 days later fresh weights and the activities of ADH, ODH, alpha GPDH, and MDH were measured. Activity differences were observed between the two Adh genotypes: ADHF allozyme had considerably higher activity than ADHS. Exogenous ethanol resulted in the highest increase in ADH activity in the second- and early third-instar stages. This ADH induction depended on the allele combination at the Adh and Odh loci; e.g., in the strain having the AdhS-OdhS allele combination, increased ADH activity was observed only after exposure to 7.5% ethanol. ODH activities differed according to the Odh genotypes, in that the ODHS allozyme had a higher activity than ODHF. ODH activities did not appreciably respond to different ethanol treatments. All six strains had identical alleles at the Mdh and alpha Gpdh loci, but nevertheless, the responses of these enzymes to ethanol depended on the allele combinations at the Adh and Odh loci. alpha GPDH activity followed that of ADH in all experiments. MDH activities were not influenced by exogenous ethanol in the strains homozygous for the AdhS allele. In AdhF strains, however, exposure to 7.5% ethanol resulted in a considerable decrease in MDH activity in the second-instar larvae. Correlations among the response variables showed that ODH activities were strongly associated with fresh weight and the activities of all other enzymes, except for ADH. ADH activity, however, showed a significant correlation only with alpha GPDH activity throughout the larval life. Both MDH and ODH activities were found to be in strong negative correlation with ADH activity in the second-instar larvae. At this most sensitive life stage, the metabolic response to ethanol is highly correlated.
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PMID:Interaction between the Adh and Odh loci in response to ethanol in Drosophila melanogaster. 967 77