Alcoholism and the Hyperactive Child Syndrome

Goodwin, Donald W.; Schulsinger, Fini; Hermansen, Leif; Guze, Samuel B.; Winokur, G.

doi:10.1097/00005053-197505000-00004

Cited by 219 publications

(48 citation statements)

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“…Parental alcoholism and offspring ADHD Specific to this report, an association between parental alcoholism and child hyperactivity has been noted for many years (Goodwin et al 1975 ;Stewart et al 1980). An early review (Barkley, 1990) revealed that 14-25 % of parents of ADHD children were alcoholic and that non-alcohol-dependent parents of ADHD children typically consumed more alcohol than parents of non-ADHD children.…”

Section: Introductionmentioning

confidence: 62%

Maternal alcohol use disorder and offspring ADHD: disentangling genetic and environmental effects using a children-of-twins design

et al. 2006

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Section: Introductionmentioning

confidence: 62%

Maternal alcohol use disorder and offspring ADHD: disentangling genetic and environmental effects using a children-of-twins design

et al. 2006

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“…List o f Tables Table 1 Alcohol (N LSY ) Q uestions Table 2 Resulting Factors Table 3 Descriptive Statistics Table 4 DF Analysis Results Table 5 Distributions (C otton, 1979;Goodwin, 1972;Goodwin, 1994;Schuckit, 1985). Specifically, Schuckit (1985) reported, .…”

mentioning

confidence: 99%

Genetic and Environmental Influences on Alcohol Use: Df Analysis of Nlsy Kinship Data

Buster

Rodgers

2000

J. Biosoc. Sci.

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This manuscript has been reproduced fix>m the m icrofilm m aster. U M I films the text directly fi'om th e original or copy su bm itted. Thus, som e thesis and dissertation copies are in typewriter A ce, w h ile oth ers m ay be fi'om aity type o f com puter printer. In the unlikely event that th e author did not send U M I a com plete manuscript and th ere are missing pages, these will b e n o te d . A lso, if unauthorized copyright material had to be removed, a n o te will indicate the deletion. Photographs included in th e original manuscript have b e e n reproduced xerographically in this copy. H igher quality 6" x 9" b la c k and w hite photographic prints are available for dxs^ photographs o r illustrations appearing in th is copy fo r an additional charge. C o n tact U M I directly to order.

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“…Yet, the complexity of the problem and lack of fundamental knowledge have left few but such pragmatic alternatives, since biological determinants have remained elusive and obscure, much as they have been postulated (3). A more biologically oriented view has gained considerable support in recent years from increasingly convincing evidence indicating a genetic predisposition in some individuals for the consumption of alcohol (4) and for alcoholism (5,6). On this basis, the delineation of the genetic variability of the enzymes of ethanol metabolism has become an important objective of alcoholism research.…”

mentioning

confidence: 99%

Isolation of II-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism?

Li¹,

Bosron²,

Dafeldecker³

et al. 1977

Proc. Natl. Acad. Sci. U.S.A.

125

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Human liver alcohol dehydrogenase (alcohol: NAD + oxidoreductase, EC 1.1.1.1), homogeneous by physicochemical criteria, has been available in quantity only recently [Lange, L. G. & Vallee, B. L. (1976) Biochemistry 15, 4681-4686]. Until now, the biochemical basis of human alcohol metabolism had to be extrapolated from the properties and behavior of enzymes from other species, primarily horses and yeast. The biological determinants of human alcoholism have remained obscure, although recent evidence indicates a genetic predisposition, requiring delineation. A functionally distinct form of human liver alcohol dehydrogenase (ADH), which we have designated II-ADH, is provocative since, thus far, it seems to be unique to human beings. It has a high K m for ethanol and is remarkably insensitive (apparent K I , 500 μM) to pyrazole and its derivatives, which are usually potent ADH inhibitors ( K I , 1 μM), a property that is the basis for the isolation of II-ADH. The affinity resin 4-[3-( N -6-aminocaproyl)aminopropyl]pyrazole-Sepharose binds all other known forms of ADH but not II-ADH, thereby separating it selectively by affinity chromatography. In turn, this has led to the establishment of its identity with that enzyme form which was previously known as the anodic band and characterized by a high K m for ethanol (20 mM at pH 7.5). The remarkable insensitivity of II-ADH to pyrazole inhibition has also permitted quantitation of its role in hepatic ethanol oxidation. At 5 mM ethanol, a saturating concentration for virtually all other forms of ADH, II-ADH contributes less than 15% to total ethanol oxidation. However, at intoxicating concentrations, e.g., 60 mM, it can account for as much as 40% of the total ethanol oxidation rate of liver, indicating a seemingly unique role for this enzyme form in ethanol elimination. Thus far, we have found the amount of II-ADH varies from liver to liver of individuals and is considerably more labile than the other molecular forms, phenomena whose inter- or independence requires further study. The isolation of human II-ADH advances efforts to recognize and understand biochemical mechanisms that may be biological determinants of alcoholism and alcohol-related disease states, now generally approached and managed largely as psychosocial disorders.

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Alcoholism and the Hyperactive Child Syndrome

Cited by 219 publications

References 0 publications

Maternal alcohol use disorder and offspring ADHD: disentangling genetic and environmental effects using a children-of-twins design

Maternal alcohol use disorder and offspring ADHD: disentangling genetic and environmental effects using a children-of-twins design

Genetic and Environmental Influences on Alcohol Use: Df Analysis of Nlsy Kinship Data

Isolation of II-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism?

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