Formation and Immunological Properties of Aldehyde-derived Protein Adducts following Alcohol Consumption
Abstract
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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Ethanol metabolism primarily occurs in the liver in three major steps: ethanol oxidation to acetaldehyde, acetaldehyde metabolism to acetate, and acetate catabolism to H2O and CO2.
“Ethanol metabolism primarily occurs in the liver in three major steps: (1) ethanol oxidation to acetaldehyde, (2) acetaldehyde metabolism to acetate, and (3) acetate catabolism to H2O and CO2132–134.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [133]
Catalase may participate in ethanol oxidation in the presence of H2O2 but appears to play no major role in hepatic ethanol metabolism under physiological conditions due to limited H2O2 supply.
“Catalase present in peroxisomes may participate in ethanol oxidation in the presence of H2O2132–134, although this enzyme appears to play no major role in hepatic ethanol metabolism under physiological conditions due to the limited supply of H2O2135.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [133]
Cytosolic ADH is a major enzyme that catalyzes oxidative metabolism of ethanol to acetaldehyde by using NAD+ converted to NADH.
“Cytosolic ADH is a major enzyme that catalyzes the oxidative metabolism of ethanol to acetaldehyde by using the cofactor nicotinamide adenine dinucleotide (NAD+) converted to NADH132–134.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [133]
Acetate produced is further degraded to CO2 and H2O, ending the final step of ethanol oxidation in the liver.
“Finally, the acetate that is produced is further degraded to CO2 and H2O, ending the final step of ethanol oxidation in the liver132–134.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [133]
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Continuous cultures of fused cells secreting antibody of predefined specificity
Köhler, G., & Milstein, C. (1975) · Nature · doi:10.1038/256495a0 · Cited by 17,200 · see citing works
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works
Epstein, F. H., Steinberg, D. I., Parthasarathy, S., Carew, T. E., Khoo, J. C., & Witztum, J. L. (1989) · New England Journal of Medicine · doi:10.1056/nejm198904063201407 · Cited by 6,425 · see citing works
Stadtman, E. R. (1992) · Science · doi:10.1126/science.1355616 · Cited by 2,701 · see citing works
Book ReviewAmbulatory Pediatric Care
Steinberg, J. B. (1989) · New England Journal of Medicine · doi:10.1056/nejm198901053200122 · Cited by 2,121 · see citing works
Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
Habeeb, A. F. S. A. (1966) · Analytical Biochemistry · doi:10.1016/0003-2697(66)90275-2 · Cited by 2,040 · see citing works
Malondialdehyde-Altered Protein Occurs in Atheroma of Watanabe Heritable Hyperlipidemic Rabbits
Haberland, M. E., Fong, D., & Cheng, L. (1988) · Science · doi:10.1126/science.2455346 · Cited by 748 · see citing works
Friedman, M. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf030490p · Cited by 650 · see citing works
Palinski, W., Ylä‐Herttuala, S., Rosenfeld, M. E., Butler, S. W., Socher, S. S., Parthasarathy, S., Curtiss, L. K., & Witztum, J. L. (1990) · Arteriosclerosis An Official Journal of the American Heart Association Inc · doi:10.1161/01.atv.10.3.325 · Cited by 616 · see citing works
Groves, W. E., Davis, F. C., & Sells, B. H. (1968) · Analytical Biochemistry · doi:10.1016/0003-2697(68)90307-2 · Cited by 450 · see citing works
Acetaldehyde adducts with hemoglobin.
Stevens, V. J., Fantl, W. J., Newman, C. B., Sims, R. V., Cerami, A., & Peterson, C. M. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110043 · Cited by 328 · see citing works
The intralobular distribution of ethanol-inducible P450IIE1 in rat and human liver
Tsutsumi, M., Lasker, J. M., Shimizu, M., Rosman, A. S., & Lieber, C. S. (1989) · Hepatology · doi:10.1002/hep.1840100407 · Cited by 315 · see citing works
Israel, Y., Hurwitz, E., Niemelä, O., & Arnon, R. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.20.7923 · Cited by 264 · see citing works
Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload.
Houglum, K., Filip, M., Witztum, J. L., & Chojkier, M. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114934 · Cited by 254 · see citing works
Tuma, D. J., Thiele, G. M., Xu, D., Klassen, L. W., & Sorrell, M. F. (1996) · Hepatology · doi:10.1002/hep.510230431 · Cited by 245 · see citing works
Self-citationTuma, D. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00742-0 · Cited by 211 · see citing works
Self-citationAcetaldehyde adducts with proteins: Binding of [14C]acetaldehyde to serum albumin
Donohue, T. M., Tuma, D. J., & Sorrell, M. F. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90406-x · Cited by 209 · see citing works
Self-citationIntroduction—serial review: alcohol, oxidative stress and cell injury
Cederbaum, A. I. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00741-9 · Cited by 191 · see citing works
Distribution of ethanol-induced protein adducts in vivo: relationship to tissue injury,
Niemelä, O. J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00744-4 · Cited by 181 · see citing works
Covalent Binding of Acetaldehyde to Proteins: Participation of Lysine Residues
Tuma, D. J., Newman, M. R., Donohue, T. M., & Sorrell, M. F. (1987) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1987.tb00178.x · Cited by 155 · see citing works
Self-citationCovalent protein adducts in the liver as a result of ethanol metabolism and lipid peroxidation.
Niemelä, O. J., Parkkila, S., Ylä‐Herttuala, S., Halsted, C. H., Jl, W., Lança, A. J., & Israel, Y. (1994) · PubMed · Cited by 147 · see citing works
Parameters affecting the immunogenicity of microencapsulated tetanus toxoid
Esparza, I., & Kissel, T. (1992) · Vaccine · doi:10.1016/0264-410x(92)90094-z · Cited by 119 · see citing works
Clot, P., Bellomo, G., Tabone, M., Aricò, S., & Albano, E. (1995) · Gastroenterology · doi:10.1016/0016-5085(95)90025-x · Cited by 115 · see citing works
Reaction of acetaldehyde with hemoglobin.
George, R. C. S., & Hoberman, H. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62688-8 · Cited by 109 · see citing works
Detection of circulating antibodies to malondialdehyde-acetaldehyde adducts in ethanol-fed rats
Xu, D., Thiele, G. M., Beckenhauer, J. L., Klassen, L. W., Sorrell, M. F., & Tuma, D. J. (1998) · Gastroenterology · doi:10.1016/s0016-5085(98)70148-9 · Cited by 87 · see citing works
Self-citationEthanol-derived immunoreactive species formed by free radical mechanisms.
Moncada, C., Torres, V., Varghese, G., Albano, E., & Israel, Y. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09814-1 · Cited by 77 · see citing works
Elucidation of Reaction Scheme Describing Malondialdehyde−Acetaldehyde−Protein Adduct Formation
Tuma, D. J., Kearley, M. L., Thiele, G. M., Worrall, S., Haver, A. C., Klassen, L. W., & Sorrell, M. F. (2001) · Chemical Research in Toxicology · doi:10.1021/tx000222a · Cited by 71 · see citing works
Self-citationLieber, C. S. (1988) · Seminars in Liver Disease · doi:10.1055/s-2008-1040528 · Cited by 69 · see citing works
Hemodynamic changes in patients developing effective hypovolemia after total paracentesis
Vila, M. C., Sola, R. L., Balaguer, L. M., Andreu, M. G., Coll, S., Gana, J., Marquez, J., Palá, J., Bory, F., Pons, S., et al. (1998) · Journal of Hepatology · doi:10.1016/s0168-8278(98)80288-2 · Cited by 63 · see citing works
Xu, D., Thiele, G. M., Kearley, M. L., Haugen, M. D., Klassen, L. W., Sorrell, M. F., & Tuma, D. J. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970069t · Cited by 58 · see citing works
Self-citationWillis, M. S., Klassen, L. W., Tuma, D. J., Sorrell, M. F., & Thiele, G. M. (2002) · Alcoholism: Clinical and Experimental Research · doi:10.1111/j.1530-0277.2002.tb02436.x · Cited by 56 · see citing works
Self-citationAlcoholic liver disease. Pathology and pathogenesis
McGill, D. B. (1995) · Gastroenterology · doi:10.1016/0016-5085(95)90784-x · Cited by 54 · see citing works
Preferential covalent binding of acetaldehyde to the α-chain of purified rat liver tubulin†
Jennett, R. B., Sorrell, M. F., Saffari-Fard, A., Ockner, J. L., & Tuma, D. J. (1989) · Hepatology · doi:10.1002/hep.1840090109 · Cited by 53 · see citing works
Self-citationNiemelä, O. J., Parkkila, S., Pasanen, M., Viitala, K., Villanueva, J. A., & Halsted, C. H. (1999) · Hepatology · doi:10.1002/hep.510300413 · Cited by 43 · see citing works
Rk, G., & Siber, G. R. (1995) · Journal of Immunological Methods · doi:10.1016/0022-1759(94)00331-p · Cited by 39 · see citing works
The formation and stability of imidazolidinone adducts from acetaldehyde and model peptides
Fowles, L., Beck, E. J., Worrall, S., SHANLEY, B. C., & de Jersey, J. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)02408-5 · Cited by 38 · see citing works
Parkkila, S., Niemelä, O. J., Britton, R. S., Brown, K. E., Ylä‐Herttuala, S., O’Neill, R., & Bacon, B. R. (1996) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1996.270.2.g376 · Cited by 33 · see citing works
Covalent binding of acetaldehyde to hepatic proteins: role in alcoholic liver injury.
Tuma, D. J., & Sorrell, M. F. (1985) · PubMed · Cited by 26 · see citing works
Self-citationMattila, P. S. (1985) · Journal of Immunological Methods · doi:10.1016/0022-1759(85)90056-0 · Cited by 16 · see citing works
Cominacini, L., Garbin, U., Santis, A. D., Campagnola, M., Davoli, A., Pasini, A. F., Faccini, G., Pasqualini, E., Bertozzo, L., Micciolo, R., et al. (1996) · Journal of Lipid Mediators and Cell Signalling · doi:10.1016/0929-7855(95)00011-9 · Cited by 14 · see citing works
Monoclonal and polyclonal antibodies recognizing acetaldehyde–protein adducts
Thiele, G. M., Tuma, D. J., Miller, J. A., Wegter‐McNelly, K., McDonald, T. L., & Klassen, L. W. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00251-2 · Cited by 12 · see citing works
Self-citationImmunity to tetanus: tetanus antitoxin and anti-BIIb in human sera
German-Fattal, M., Bizzini, B., & German, A. (1987) · Journal of Biological Standardization · doi:10.1016/0092-1157(87)90025-4 · Cited by 11 · see citing works
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Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,561 · see citing works
Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works
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Gu, X., & Manautou, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002110 · Cited by 389 · see citing works
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Setshedi, M., Wands, J. R., & de la Monte, S. M. (2010) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.3.3.12288 · Cited by 365 · see citing works
Focus on: Alcohol and the immune system.
Molina, P. E., Happel, K. I., Zhang, P., Kolls, J. K., & Nelson, S. (2010) · Europe PMC (PubMed Central) · Cited by 205 · see citing works
Thiele, G. M., Duryee, M. J., Anderson, D. R., Klassen, L. W., Mohring, S. M., Young, K. A., Benissan‐Messan, D., Sayles, H. R., Dusad, A., Hunter, C. D., et al. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38969 · Cited by 162 · see citing works
Self-citationDuryee, M. J., Klassen, L. W., Schaffert, C. S., Tuma, D. J., Hunter, C. D., Garvin, R. P., Anderson, D. R., & Thiele, G. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.001 · Cited by 110 · see citing works
Self-citationAcetaldehyde-Mediated Neurotoxicity: Relevance to Fetal Alcohol Spectrum Disorders
Tong, M., Longato, L., Nguyen, Q.-G., Chen, W. C., Spaisman, A., & de la Monte, S. M. (2011) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2011/213286 · Cited by 106 · see citing works
D'Souza, N. B., Kovacs, E. J., Witte, P. D., Spies, C., Littleton, J. M., de Villiers, W. J. S., Lott, A. J., Plackett, T. P., Lanzke, N., & Meadows, G. G. (2010) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2010.01234.x · Cited by 100 · see citing works
Hebecker, M., Alba‐Domínguez, M., Roumenina, L. T., Reuter, S., Hyvärinen, S., Dragon‐Durey, M., Jokiranta, T. S., Sánchez‐Corral, P., & Józsi, M. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300269 · Cited by 67 · see citing works
Grönwall, C., Amara, K., Hardt, U., Krishnamurthy, A., Stéen, J., Engström, M., Sun, M. Y., Ytterberg, A. J., Zubarev, R. A., Scheel‐Toellner, D., et al. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.06.004 · Cited by 67 · see citing works
Biomarkers of alcohol misuse: recent advances and future prospects
Jastrzębska, I., Zwolak, A., Szczyrek, M., Wawryniuk, A., Skrzydło-Radomańska, B., & Daniluk, J. (2016) · Gastroenterology Review · doi:10.5114/pg.2016.60252 · Cited by 58 · see citing works
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Torok, N. J. (2015) · Biomolecules · doi:10.3390/biom5042978 · Cited by 36 · see citing works
Hyvärinen, S., Uchida, K., Varjosalo, M. T., Jokela, R., & Jokiranta, T. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.527416 · Cited by 35 · see citing works
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Afifiyan, N. F., Tillman, B. C., French, B. A., Masouminia, M., Samadzadeh, S., & French, S. W. (2017) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2017.01.011 · Cited by 17 · see citing works
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Lomzenski, H. E., Thiele, G. M., Duryee, M. J., Chen, S., Ye, F., Anderson, D. R., Mikuls, T. R., & Ormseth, M. J. (2022) · Scientific Reports · doi:10.1038/s41598-022-14954-9 · Cited by 11 · see citing works
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Kandi, S., Deshpande, N., Pinnelli, V. B. K., Devaki, R., Rao, P. H., & Ramana, K. V. (2014) · American Journal of Medical Sciences and Medicine · doi:10.12691/ajmsm-2-3-3 · Cited by 7 · see citing works
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Nissinen, A. E. T. (2011) · Cited by 6 · see citing works
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Danielsson, J. (2014) · Tampere University Institutional Repository (Tampere University) · Cited by 1 · see citing works
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Wang, Y., Shen, Y., Zhou, H., Hao, X., Sun, S., Hu, Z., Li, W., Sun, L., Peng, Y., & Zheng, J. (2026) · Drug Metabolism and Disposition · doi:10.1016/j.dmd.2026.100291
- Authors
- Thiele, G. M., Klassen, L. W., & Tuma, D. J.
- Affiliations
- United States Department of Veterans Affairs (US)
- ORCID
- Thiele, Geoffrey M.
- Venue
- Methods in Molecular Biology™
- Publisher
- Humana Press
- Published
- 2008
- Volume
- 447
- Pages
- 235-257
- ISSN
- 1064-3745 (ISSN-L)
- 1940-6029
- OpenAlex
- W2408376914
- Cited by
- 33
- References
- 43
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 1 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 1
- FWCI
- 9.06
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Methods in molecular biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01aa007818-06)
- National Institute on Alcohol Abuse and Alcoholism (R01AA010435, R01 AA10435, R01 AA04691, R01AA07818)
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- ethanol consumption, acetaldehyde, alcohol dehydrogenase, CYP2E1, malondialdehyde, 4-hydroxynonenal, lipid peroxidation, oxidative stress, alcoholic liver disease, immunological properties
- MeSH terms
- Acetaldehyde, Alcohol Drinking, Ethanol, Aldehydes, Animals, Antibodies, Antibodies, Monoclonal, Antibody Specificity, Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Humans, Immunologic Techniques, Liver, Liver Diseases, Alcoholic, Malondialdehyde, Proteins, Rabbits, T-Lymphocytes, Blotting, Western, Biomarkers, Oxidative Stress, Models, Animal, Immunoprecipitation, Mice
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