Preferential formation of Nω-(carboxyethyl)arginine from methylglyoxal and its accumulation in human lens proteins

Clicks: 6
ID: 321219
2026
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Steady

Ranked #19 of 36 articles by views in The Journal of Biochemistry

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Methylglyoxal (MGO), a highly reactive dicarbonyl compound generated mainly by glycolysis, is a major precursor of advanced glycation end products (AGEs). Although lysine-derived AGEs, such as Nε-(carboxyethyl)lysine (CEL), have been widely used as markers of MGO-mediated protein modification, increasing evidence suggests that MGO preferentially modifies arginine residues. However, the biochemical significance of arginine-derived AGEs remains poorly understood because of limited analytical and immunochemical methods for their detection. In this study, we investigated the formation and quantitative significance of Nω-(carboxyethyl)arginine (CEA), an underexplored MGO-derived arginine adduct. CEA was chemically synthesized and structurally characterized by NMR and mass spectrometry. Analysis of human tissues revealed that CEA accumulated at high levels in cataractous lenses, comparable to MG-H1 and higher than CEL levels. A monoclonal antibody specific for CEA was developed and validated using ELISA, showing no cross-reactivity with related AGEs. CEA was generated in a time-dependent manner in bovine serum albumin incubated with MGO, whereas CEL formation was minimal. CEA levels were higher than those of CEL in MGO-modified proteins, indicating its preferential formation under physiological conditions. These findings indicate that CEA is a reliable marker for evaluating MGO-mediated protein degeneration and dicarbonyl stress in vitro and in vivo.
Reference Key
openalex_W7168713297 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Himeno Takahashi, Mime Nagai, Tsuyoshi Ikeda, Ken Hoshiyama, Takao Hirano, Toshinori Murata, Ryoji Nagai
Journal The Journal of Biochemistry
Year 2026
DOI
10.1093/jb/mvag053
URL
https://doi.org/10.1093/jb/mvag053
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.