Proximal cysteine residues in proteins promote N^ε-carboxyalkylation of lysine residues by α-dicarbonyl compounds.

ABSTRACT: Advanced glycation end products (AGEs) are protein modifications resulting from the chemical reaction between lysine and arginine residues in proteins, and carbonyl compounds, including glyoxal (GO) and methylglyoxal (MGO). N^ε-carboxymethyllysine (CML) and N^ε-carboxyethyllysine (CEL), formed by glycation from GO and MGO, are among the major AGEs in tissue proteins. Incubation with GO or MGO resulted in higher CML and CEL formation in the two cysteine residues containing αA-crystallin (αAC) than in the cysteine lacking αB-crystallin (αBC). Mass spectrometric data showed K70 and K166 to be heavily modified with CML and CEL in GO- and MGO-modified αAC. In silico analysis of the structure of αAC showed K70 and K166 to be proximal to C142. Mutation or reductive alkylation

SUBMITTER: Panja S 

PROVIDER: S-EPMC11994404 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature