Quantitation of pathways of ethanol metabolism

Havre, Pamela A.; Abrams, M A; Corrall, R. J. M.; Yu, Ling C.; Szczepanik, Patricia A.; Feldman, Howard B.; Klein, Peter; Kong, Ming; Margolis, Joseph M.; Landau, Bernard R.

doi:10.1016/0003-9861(77)90278-8

Cited by 50 publications

(3 citation statements)

References 26 publications

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“…The first three of these loci have been mapped together on chromosome 3 to a region designated as the Adh gene complex (Holmes et al 1983), which includes structural and temporal genes for the major liver and stomach isozymes of alcohol dehydrogenase (ADH). This latter enzyme catalyses the first step of alcohol metabolism in mammals (Havre et al 1977;Plapp et al 1984), and is subject to temporal gene regulation in mouse liver, with C57BL mice exhibiting a 'high activity' phenotype for liver ADH (Balak etal. 1982).…”

Section: Variant Phenotypesmentioning

confidence: 99%

Biochemical genetic variants in mice selectively bred for sensitivity or resistance to ethanol‐induced sedation

1986

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The distribution of biochemical genetic variants was examined among eight inbred strains of mice, which served as contributors to a heterogeneous stock of mice (HS), and in short-sleep (SS) and long-sleep (LS) mice, selectively bred from the HS stock for differential ethanol sensitivity. Fifteen loci for enzymes of alcohol and aldehyde metabolism, as well as 12 other biochemical loci, were investigated. Thirteen of these loci exhibited allelic variation between strains, of which six were separately fixed in the SS and LS mice. Comparisons of genetic similarity coefficients, based upon the distributions of allelic variants for the loci examined, with behavioural sensitivities (sleep-time) to an acute dose of ethanol for the inbred and selected strains of mice, indicated no correlations between these data. This suggests that this collective group of loci are not useful indicators of the genes selectively bred in the SS and LS strains, which are responsible for the differential sensitivities to acute doses of ethanol.

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Section: Variant Phenotypesmentioning

confidence: 99%

Biochemical genetic variants in mice selectively bred for sensitivity or resistance to ethanol‐induced sedation

1986

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“…Alcohol dehydrogenase (ADH; EC 1.1.1.1) is widely distributed in mammalian tissues (Holmes, 1978;Duley et al, 1985;, and is the major catalyst of ethanol oxidation in the body (Havre et al, 1977;Plapp et al, 1984). ADH is also capable of catalyzing the reversible interconversion of a wide variety of alcohols and their corresponding aldehydes and ketones, including sterols, ~o-hydroxy fatty acids, and food flavor alcohols (Pietruszko, 1979), and may function as a major detoxification mechanism for biological aldehydes.…”

Section: Introductionmentioning

confidence: 99%

Biochemical genetics of alcohol dehydrogenase isozymes in the gray short-tailed opossum (Monodelphis domestica)

1992

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Polyacrylamide gel-isoelectric focusing (PAGE-IEF) methods were used to examine the multiplicity, tissue distribution, and biochemical genetics of alcohol dehydrogenase (ADH) isozymes among gray short-tailed opossums (Monodelphis domestica). Seven ADH isozymes were resolved and distinguished on the basis of their isoelectric points, tissue distributions, and substrate and inhibitor specificities. ADH1 and ADH2 exhibited Class I properties and were observed in liver (and intestine) extracts. ADH3, ADH4, and ADH5 showed "high-Km" (possibly Class IV) properties, with ADH3 and ADH4 exhibiting high activity in cornea, ear, stomach, and esophagus extracts. ADH6 and ADH7 exhibited Class III properties, including activities as formaldehyde dehydrogenases, with each showing different tissue distribution characteristics; ADH6 was widely distributed, and ADH7 was restricted to prostate extracts. An additional form of formaldehyde dehydrogenase (FDH) was observed, which was inactive with hexenol and ethanol as substrates. Isoelectric point variants were observed for ADH3 (three forms) and for ADH4 (two forms), and the inheritance of ADH3 was studied in 15 families of M. domestica. The data were consistent with codominant inheritance of two alleles (ADH3*A and ADH3*B) at a single autosomal locus (designated ADH3) and with a model involving a dimeric ADH isozyme: ADH3 (gamma 2 isozyme, forming three dimers designated gamma 1(2), gamma 1 gamma 2, and gamma 2(2) in heterozygous individuals).

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“…These investigations have focussed on the liver alcohol-metabolizing enzymes, alcohol dehydrogenase (ADH; E.C.1.1.1.1) and aldehyde dehydrogenase (AHD; E.C. 1.2.1.3) which are responsible for eliminating 75-90 % of ingested ethanol from the body (Havre et al, 1977;Lieber, 1977;Khanna & Israel, 1980). Although significant biochemical differences have been reported between the alcohol-accepting and alcohol-avoiding mouse strains, there have been no reports which have examined the genetic segregation of behavioural phenotype with biochemical genetic markers associated with alcohol metabolism.…”

Section: Introductionmentioning

confidence: 99%

Gene markers for alcohol‐metabolizing enzymes among recombinant inbred strains of mice with differential behavioural responses towards alcohol

Holmes

Mather

Duley

1985

Animal Blood Groups and Biochemical Genetics

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The genetic variability of alcohol dehydrogenase (C, isozyme), aldehyde dehydrogenase (A, isozyme) and aldehyde oxidase (A, isozyme) has been examined among recombinant inbred strains of mice which have been previously studied concerning their differential behavioural responses towards alcohol. The results showed no correlation between biochemical phenotype for these loci and behavioural response.

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Quantitation of pathways of ethanol metabolism

Cited by 50 publications

References 26 publications

Biochemical genetic variants in mice selectively bred for sensitivity or resistance to ethanol‐induced sedation

Biochemical genetic variants in mice selectively bred for sensitivity or resistance to ethanol‐induced sedation

Biochemical genetics of alcohol dehydrogenase isozymes in the gray short-tailed opossum (Monodelphis domestica)

Gene markers for alcohol‐metabolizing enzymes among recombinant inbred strains of mice with differential behavioural responses towards alcohol

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