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Others believe that Et OH is simply a “pro-drug” and the rewarding properties of Et OH are dependent on the action of the metabolites/byproducts of Et OH within the brain. doi: 10.1016/S0024-3205(96)00597-8 Pubmed Abstract | Pubmed Full Text | Cross Ref Full Text Hald, J., Jacobsen, E., and Larsen, V. Formation of acetaldehyde in the organism in relation to dosage of antabuse (tetraethylthiuramdisulphide) and to alcohol-concentration in blood.

Preclinical research indicated that antabuse rendered ACD detectable in the breath of rabbits following Et OH exposure and research aimed at the identification of the metabolic pathway of Et OH began (Hald et al., 1949a,b).

The mesolimbic dopamine system originates in the ventral tegmental area (VTA) and projects to forebrain regions that include the nucleus accumbens (Acb) and the medial prefrontal cortex (m PFC) and is thought to be the neurocircuitry governing the rewarding properties of drugs of abuse. Pubmed Abstract | Pubmed Full Text Hipolito, L., Marti-Prats, L., Sanchez-Catalan, M.

Within this neurocircuitry there is convincing evidence that; (1) biologically active metabolites of alcohol can directly or indirectly increase the activity of VTA dopamine neurons, (2) alcohol and alcohol metabolites are reinforcing within the mesolimbic dopamine system, (3) inhibiting the alcohol metabolic pathway inhibits the biological consequences of alcohol exposure, (4) alcohol consumption can be reduced by inhibiting/attenuating the alcohol metabolic pathway in the mesolimbic dopamine system, (5) alcohol metabolites can alter neurochemical levels within the mesolimbic dopamine system, and (6) alcohol interacts with alcohol metabolites to enhance the actions of both compounds.

Following consumption, Et OH undergoes a number of reactions as it is metabolized. doi: 10.1016/20 Pubmed Abstract | Pubmed Full Text | Cross Ref Full Text Font, L., Miquel, M., and Aragon, C.

The primary pathway through which Et OH is eliminated from the body involves the action of the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes (for review see: Deehan et al., 2013).

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