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Molecular Advances in Alcohol Metabolism
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Molecular Advances in Alcohol Metabolism

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Endocrinology and Metabolism".

Deadline for manuscript submissions: 20 November 2025 | Viewed by 1592

Special Issue Editor

Dr. Takeshi Haseba

E-Mail Website
Guest Editor
Department of Legal Medicine, Kanagawa Dental University, 82 Inaokacho, Yokosuka 238-8580, Japan
Interests: ADH1; ADH3; GSNOR; ALDH2; alcohol metabolism; chronic alcohol consumption; alcohol liver disease; alcohol addiction; intoxication; drunk driving

Special Issue Information

Dear Colleagues,

Alcohol metabolism (AM) is the primary internal factor that regulates the effects of alcohol, such as cell toxicity, intoxication, and dependence formation.

AM has been known to be changed by the amount of alcohol consumed, the kind of alcoholic beverage, eating and dietary ingredients, drinking history, age, organ diseases, heredity factors including sex, and so on. However, the molecular mechanisms are not yet well understood, although ADH in the liver has been recognized as the key enzyme. In humans, the ADH1B genotype (ADH1B*1 or *2) shows a different activity to modify the biological effects of alcohol, but its relationship to AM is unclear compared to the case with the ALDH2 genotype. MEOS and catalase have been proposed as candidates for a non-ADH pathway, but these hypotheses remain unproven even in subsequent experiments using KO mice. ADH3 (or 5) and ADH4 isozymes were also revealed to contribute to systemic AM in ADH3 and ADH4 KO mice experiments, but their modifications to the biological effects of alcohol are unknown.

This Special Issue, Molecular Advances in Alcohol Metabolism, welcomes reviews and articles on the latest studies on the contribution of alcohol metabolizing enzymes to AM in vivo and their relationship with the biological effects of alcohol.

A comprehensive understanding of the molecular mechanism of AM, coupled with the biological effects of alcohol, can provide the most important foundation in alcohol medical research, which aims to solve, treat, and prevent social and health problems caused by drinking.

Dr. Takeshi Haseba
Guest Editor

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Keywords

  • alcohol metabolism
  • ADH1
  • ADH3
  • ADH4
  • MEOS
  • catalase
  • ALDH2
  • pharmacology and toxicology
  • ROS
  • alcohol-related disease

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Published Papers (1 paper)

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20 pages, 806 KB  
Review
Enzymatic Control of Alcohol Metabolism in the Body—The Roles of Class I, II, III, and IV Alcohol Dehydrogenases/NADH Reoxidation System, Microsomal Ethanol Oxidizing System, Catalase/H2O2 System, and Aldehyde Dehydrogenase 2
by Takeshi Haseba
Int. J. Mol. Sci. 2025, 26(19), 9479; https://doi.org/10.3390/ijms26199479 - 27 Sep 2025
Viewed by 1136
Abstract
Alcohol metabolism in the body is a key theme in medical research on alcohol. It is primarily regulated by the alcohol dehydrogenase (ADH) and mitochondrial NADH reoxidation in the liver. Class I ADH1 is a well-known ADH isozyme and a key enzyme in [...] Read more.
Alcohol metabolism in the body is a key theme in medical research on alcohol. It is primarily regulated by the alcohol dehydrogenase (ADH) and mitochondrial NADH reoxidation in the liver. Class I ADH1 is a well-known ADH isozyme and a key enzyme in alcohol metabolism, with the lowest Kms for ethanol and the highest sensitivity to pyrazole (Pz) among the ADH isozymes. However, a Pz-insensitive metabolic pathway also plays a role in systemic alcohol metabolism, with increasing metabolic contributions at higher blood alcohol concentrations (BACs) and under chronic alcohol consumption (CAC). The Pz-insensitive pathway is referred to as the non-ADH pathway—specifically, it is a non-ADH1 pathway—and is assumed to involve the microsomal ethanol oxidizing system (MEOS) or catalase, as both enzymes are insensitive to Pz and exhibit higher Kms than ADH1. The MEOS is a favored candidate for this pathway, as its activity markedly increases with the rate of alcohol metabolism under CAC. However, the role of the MEOS in alcohol metabolism has not been proven in vivo (even under CAC conditions), nor has that of catalase. Here, we report Class III ADH3 as a new candidate in the non-ADH1 pathway, as it also has a lower sensitivity to Pz and a higher Km. It is markedly activated by lowering Km following the addition of amphiphilic substances, which increases the solution’s hydrophobicity in the reaction medium; additionally, Nile red staining demonstrates a higher solution hydrophobicity in the cytoplasm of mouse liver cells. The rate of alcohol metabolism in ADH1 knockout (Adh1−/−) mice—which depends solely on the non-ADH1 pathway—increased by more than twice under CAC and was significantly correlated with the amount of liver ADH3 protein, but not with CYP2E1 protein (a main component of the MEOS). The rate of alcohol metabolism in Adh3−/− mice lacking ADH3 decreased in a dose-dependent manner compared with wild mice. The liver ADH3 protein in wild-type mice increased in line with the ADH1 protein under CAC. These data suggest that ADH3 contributes to alcohol metabolism in vivo as a non-ADH1 pathway and to the enhancement of alcohol metabolism under CAC through activation of the ADH1/ADH3/NADH reoxidation system. In alcoholic liver diseases, ADH1 activity decreased with the progression of liver disease, while ADH3 activity increased or was maintained even in alcoholic liver cirrhosis. Therefore, the role of ADH3 in alcohol metabolism may be increased in the context of alcoholic liver diseases, complementing the reduced role of ADH1. It has also been suggested that Class II ADH2, Class IV ADH4, and aldehyde dehydrogenase (ALDH) 2 play roles in alcohol metabolism in vivo under certain limited conditions. However, ADH2 and 4 may not contribute to the enhancement of alcohol metabolism through CAC. Full article
(This article belongs to the Special Issue Molecular Advances in Alcohol Metabolism)
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