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PMID: 9305579 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Epitope characterization of malondialdehyde-acetaldehyde adducts using an enzyme-linked immunosorbent assay.

Chemical research in toxicology ·Vol. 10 ·No. 9 ·1997-09-00 ·Pages 978-86

Xu D, Thiele GM, Kearley ML, Haugen MD, Klassen LW, Sorrell MF, Tuma DJ

Abstract

Malondialdehyde (MDA) and acetaldehyde react together with proteins in a synergistic manner and form hybrid protein adducts, designated as MAA adducts. In a previous study, a polyclonal antibody specific for MAA-protein adducts was used in an immunoassay to detect the presence of MAA adducts in livers of ethanol-fed rats. In the present study, the specific epitope recognized by the antibody was defined and the chemistry of MAA adduct formation was further characterized. When several synthetic analogs were tested for their ability to inhibit antibody binding in a competitive ELISA, the results indicated that the major determinant of antibody binding was a highly fluorescent cyclic adduct composed of two molecules of MDA and one of acetaldehyde. The structure of this adduct was shown to be a 4-methyl-1,4-dihydropyridine-3,5-dicarbaldehyde derivative of an amino group of a protein. Examination of MAA adduct formation with a variety of proteins indicated that in addition to this specific fluorescent adduct, MAA adducts were also comprised of other nonfluorescent products. The amount of fluorescent epitopes present on a given protein was the major determinant of antibody binding as assessed in a competitive ELISA, although the efficiency of inhibition of antibody binding by these fluorescent epitopes on MAA-adducted proteins varied depending upon the particular protein. However, when these MAA-adducted proteins were hydrolyzed with Pronase, the concentration of these modified proteins necessary to achieve 50% inhibition of antibody binding in a competitive ELISA fell into a much narrower range of values, indicating that protein hydrolysis equalized the accessibility of the antibody to bind the epitope on these various derivatized proteins. In summary, a cyclic fluorescent adduct of defined structure has been identified as the epitope recognized by our MAA adduct antibody. In addition to this specific adduct, MAA adducts are also comprised of other nonfluorescent products.

MeSH Terms
Acetaldehyde/chemical synthesis,chemistry Animals Antibody Specificity Biotin/chemistry Central Nervous System Depressants/pharmacology Enzyme-Linked Immunosorbent Assay Epitopes/analysis,immunology Ethanol/pharmacology Liver/drug effects,immunology Malondialdehyde/chemical synthesis,chemistry Rabbits Rats
Chemicals
Central Nervous System Depressants Epitopes Ethanol Malondialdehyde Biotin Acetaldehyde
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Xu D
Department of Veterans Affairs Alcohol Research Center, University of Nebraska Medical Center, Omaha 68105, USA.
Thiele G M
Kearley M L
Haugen M D
Klassen L W
Sorrell M F
Tuma D J
Article Info
Journal
Chemical research in toxicology
Abbr.
Chem Res Toxicol
ISSN
0893-228X
Published
1997-09-00
Pages
978-86
Language
English
Region
United States
NLM ID
8807448
Subset
IM
Grants
NIAAA NIH HHS · AA04961 · United States
NIAAA NIH HHS · AA07818 · United States
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