Summary
Most ingested ethanol is eliminated from the body through oxidative metabolism in the liver. Alcohol dehydrogenase is the enzyme that is most important in the oxidation of ethanol to acetaldehyde. However, it has also been demonstrated that cytochrome P4502E1 also can contribute to this process. However, this is not the only aldehyde that is produced after chronic ethanol consumption because oxidative stress and lipid peroxidation can be induced in the liver, which results in the production of malondialdehyde and 4-hydroxy-2-nonenal. These aldehydes are highly reactive and have the ability to react with (adduct) many macromolecules to alter their structure and play a major role in the derangements of hepatic function. Therefore, the formation of these types of adducts in the liver has been proposed as key events leading to the development and/or progression of alcoholic liver disease. In this chapter, methods for the production and detection of these modified proteins will be discussed.
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Acknowledgments
The authors would like to thank Monte S. Willis, Michael J. Duryee, Karen C. Easterling, Carlos D. Hunter, and Bartlett C. Hamilton III for their valuable technical assistance. Also, we would like to thank all of those who have worked on various aspects of these procedures throughout the years, and are too numerous to mention individually. This work has been supported by The Alcohol Center at the Omaha VA Medical Center, Department of Veterans Affairs; VA Merit Reviews, Department of Veterans Affairs; and NIH/NIAAA grants, R01 AA10435 (to Thiele), R01 AA07818 (to Klassen), R01 AA04691 (to Tuma).
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Thiele, G.M., Klassen, L.W., Tuma, D.J. (2008). Formation and Immunological Properties of Aldehyde-derived Protein Adducts following Alcohol Consumption. In: Nagy, L.E. (eds) Alcohol. Methods in Molecular Biology™, vol 447. Humana Press. https://doi.org/10.1007/978-1-59745-242-7_17
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DOI: https://doi.org/10.1007/978-1-59745-242-7_17
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