Ethanol metabolism and effects: nitric oxide and its interaction
- PMID: 18690862
- PMCID: PMC2562584
- DOI: 10.2174/157488407780598135
Ethanol metabolism and effects: nitric oxide and its interaction
Abstract
Ethanol (EtOH) in alcoholic beverages is consumed by a large number of individuals and its elimination is primarily by oxidation. The role of nitric oxide (NO) in EtOH's effects is important since NO is one of the most prominent biological factors in mammals. NO is constantly formed endogenously from L-arginine. Dose and length of EtOH exposure, and cell type are the main factors affecting EtOH effects on NO production. Either acute or chronic EtOH ingestion affects inducible NO synthase (iNOS) activity. However it seems that EtOH suppresses induced-NO production by inhibition of iNOS in different cells. On the other hand, it is clear that acute low doses of EtOH increase both the release of NO and endothelial NOS (eNOS) expression, and augment endothelium-mediated vasodilatation, whereas higher doses impair endothelial functions. EtOH selectively affects neuronal NOS (nNOS) activity in different brain cells, which may relate to various behavioral interactions. Therefore, there is an excellent chance for EtOH and NO to react with each other. Effects of EtOH on NO production and NOS activity may be important to EtOH modification of cell or organ function. Nitrosated compounds (alkyl nitrites) are often found as the interaction products, which might be one of the minor pathways of EtOH metabolism. NO also inhibits EtOH metabolizing enzymes. Furthermore, NO is involved in EtOH induced liver damage and has a role in fetal development during EtOH exposure in pregnancy. The mechanisms underlying these effects are only partially understood. Hence, the current discussion of the interaction of EtOH and NO is presented.
Figures
References
-
- Butler AR, Williams DLH. The physiological role of NO. Chem Soc Rev. 1993;1:233–41.
-
- Stuehr DJ, Griffith OW. Mammalian nitric oxide synthases. In: Meister A, editor. Advances in enzymology and related areas of molecular biology. Vol. 65. New York: John Wiley & Sons; 1992. pp. 287–346. - PubMed
-
- Morris SM., Jr Arginine metabolism in vascular biology and disease. Vasc Med. 2005;10(Suppl 1):S 83–7. - PubMed
-
- White KA, Marletta MA. Nitric oxide synthase is a cytochrome P-450 type hemoprotein. Biochemistry. 1992;31:6627–31. - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources