Oxidative deamination of lysine residues by polyphenols generates an equilibrium of aldehyde and 2-piperidinol products
| Autor: | Kosuke Yamaguchi, Masanori Itakura, Koji Uchida, Mitsugu Akagawa, Sei-Young Lim, Takahiro Shibata, Roma Kitazawa, Koji Nagata |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
EGCG
(-)-epigallocatechin-3-O-gallate Bt-APA N-biotinyl-5-aminopentylamine Lysine Lysyl oxidase DMSO dimethyl sulfoxide Biochemistry Aldehyde Epitope D2O heavy water Protein-Lysine 6-Oxidase TFA trifluoroacetic acid chemistry.chemical_compound Piperidines AAS α-aminoadipic-5-semialdehyde Trifluoroacetic acid mAb monoclonal antibody innate immunity Molecular Biology UPLC ultraperformance LC chemistry.chemical_classification Aldehydes ESI electrospray ionization NaBH4 sodium borohydride Polyphenols HRP horseradish peroxidase PBST PBS containing 0.05% Tween-20 food and beverages Oxidative deamination lysyl oxidation Cell Biology polyphenol ESM eggshell membrane IgM immunoglobulin M oxidative deamination of lysine innate epitope post-translational modification oxidation–reduction (redox) chemistry Cyclization Deamination PQQ pyrroloquinoline quinine Polyphenol bacteria Eggshell membrane Oxidation-Reduction Research Article |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/j.jbc.2021.101035 |
| Popis: | Polyphenols, especially catechol-type polyphenols, exhibit lysyl oxidase–like activity and mediate oxidative deamination of lysine residues in proteins. Previous studies have shown that polyphenol-mediated oxidative deamination of lysine residues can be associated with altered electrical properties of proteins and increased crossreactivity with natural immunoglobulin M antibodies. This interaction suggested that oxidized proteins could act as innate antigens and elicit an innate immune response. However, the structural basis for oxidatively deaminated lysine residues remains unclear. In the present study, to establish the chemistry of lysine oxidation, we characterized oxidation products obtained via incubation of the lysine analog N-biotinyl-5-aminopentylamine with eggshell membranes containing lysyl oxidase and identified a unique six-membered ring 2-piperidinol derivative equilibrated with a ring-open product (aldehyde) as the major product. By monitoring these aldehyde–2-piperidinol products, we evaluated the lysyl oxidase–like activity of polyphenols. We also observed that this reaction was mediated by some polyphenols, especially o-diphenolic-type polyphenols, in the presence of copper ions. Interestingly, the natural immunoglobulin M monoclonal antibody recognized these aldehyde–2-piperidinol products as an innate epitope. These findings establish the existence of a dynamic equilibrium of oxidized lysine and provide important insights into the chemopreventive function of dietary polyphenols for chronic diseases. |
| Databáze: | OpenAIRE |
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