Oxidative deamination of serum albumins by (-)-epigallocatechin-3-O-gallate: A potential mechanism for the formation of innate antigens by antioxidants

Yukinori Hatasa, Miho Chikazawa, Mai Furuhashi, Fumie Nakashima, Takahiro Shibata, Tatsuhiko Kondo, Mitsugu Akagawa, Hiroki Hamagami, Hiroshi Tanaka, Hirofumi Tachibana, Koji Uchida

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

(-)-Epigallocatechin-3-O-gallate (EGCG), the most abundant polyphenol in green tea, mediates the oxidative modification of proteins, generating protein carbonyls. However, the underlying molecular mechanism remains unclear. Here we analyzed the EGCG-derived intermediates generated upon incubation with the human serum albumin (HSA) and established that EGCG selectively oxidized the lysine residues via its oxidative deamination activity. In addition, we characterized the EGCG-oxidized proteins and discovered that the EGCG could be an endogenous source of the electrically-transformed proteins that could be recognized by the natural antibodies. When HSA was incubated with EGCG in the phosphatebuffered saline (pH 7.4) at 37°C, the protein carbonylation was associated with the formation of EGCG-derived products, such as the protein-bound EGCG, oxidized EGCG, and aminated EGCG. The aminated EGCG was also detected in the sera from the mice treated with EGCG in vivo. EGCG selectively oxidized lysine residues at the EGCG-binding domains in HSA to generate an oxidatively deaminated product, aminoadipic semialdehyde. In addition, EGCG treatment results in the increased negative charge of the protein due to the oxidative deamination of the lysine residues. More strikingly, the formation of protein carbonyls by EGCG markedly increased its cross-reactivity with the natural IgM antibodies. These findings suggest that many of the beneficial effects of EGCG may be partly attributed to its oxidative deamination activity, generating the oxidized proteins as a target of natural antibodies.

Original languageEnglish
Article numbere0153002
JournalPloS one
Volume11
Issue number4
DOIs
Publication statusPublished - Apr 2016

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deamination
Deamination
epigallocatechin
serum albumin
Serum Albumin
Antioxidants
antigens
antioxidants
Antigens
Proteins
proteins
Protein Carbonylation
Lysine
lysine
epigallocatechin gallate
antibodies
Antibodies
endogenous sources
Carbonylation
Polyphenols

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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Oxidative deamination of serum albumins by (-)-epigallocatechin-3-O-gallate : A potential mechanism for the formation of innate antigens by antioxidants. / Hatasa, Yukinori; Chikazawa, Miho; Furuhashi, Mai; Nakashima, Fumie; Shibata, Takahiro; Kondo, Tatsuhiko; Akagawa, Mitsugu; Hamagami, Hiroki; Tanaka, Hiroshi; Tachibana, Hirofumi; Uchida, Koji.

In: PloS one, Vol. 11, No. 4, e0153002, 04.2016.

Research output: Contribution to journalArticle

Hatasa, Y, Chikazawa, M, Furuhashi, M, Nakashima, F, Shibata, T, Kondo, T, Akagawa, M, Hamagami, H, Tanaka, H, Tachibana, H & Uchida, K 2016, 'Oxidative deamination of serum albumins by (-)-epigallocatechin-3-O-gallate: A potential mechanism for the formation of innate antigens by antioxidants', PloS one, vol. 11, no. 4, e0153002. https://doi.org/10.1371/journal.pone.0153002
Hatasa, Yukinori ; Chikazawa, Miho ; Furuhashi, Mai ; Nakashima, Fumie ; Shibata, Takahiro ; Kondo, Tatsuhiko ; Akagawa, Mitsugu ; Hamagami, Hiroki ; Tanaka, Hiroshi ; Tachibana, Hirofumi ; Uchida, Koji. / Oxidative deamination of serum albumins by (-)-epigallocatechin-3-O-gallate : A potential mechanism for the formation of innate antigens by antioxidants. In: PloS one. 2016 ; Vol. 11, No. 4.
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