Mass spectrometric characterizations of protein carbonylation: Comparison between three different conditions, oxidation by CuII/ascorbic acid, adduction of methyl glyoxal, and adduction of 4-hydroxy-2(E)-nonenal

Maeda Kazuki, Hiroyuki Funatsu, Yuki Miyazawa, Yasushi Misawa, Takaaki Goto, Seon Hwa Lee, Tomoyuki Oe

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Oxidative stress can cause various protein modifications, mainly carbonylation. There are three major chemical ways to introduce hydrazine reactive carbonyls: (i) direct oxidation by reactive oxygen species (ROS), (ii) adduction of sugars or sugar-related aldehydes, and (iii) adduction of lipid-related aldehydes. Here, we performed a comparative study of three representative conditions: CuII/ascorbic acid (AA) (ROS), methylglyoxal (sugar-related), and 4-hydroxy-2(E)-nonenal (HNE) (lipid-related). Insulin β chain and Girard's reagent P were used as the model protein and hydrazine reagent, respectively. LC/MS analyses of reactions with HNE or CuII/AA-treated linoleic acid revealed that protein carbonylation under oxidative stress is the most efficient in the presence of polyunsaturated fatty acids.

Original languageEnglish
Pages (from-to)72-80
Number of pages9
JournalInternational Journal of Mass Spectrometry
Volume373
DOIs
Publication statusPublished - 2014 Nov 15

Keywords

  • 4-Hydroxy-2(E)-nonenal
  • Carbonylation
  • Methylglyoxal
  • Oxidative stress
  • Protein
  • Reactive oxygen species

ASJC Scopus subject areas

  • Instrumentation
  • Condensed Matter Physics
  • Spectroscopy
  • Physical and Theoretical Chemistry

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