Glycation-mediated protein crosslinking and stiffening in mouse lenses are inhibited by carboxitin in vitro.

ABSTRACT: Proteins in the eye lens have negligible turnover and therefore progressively accumulate chemical modifications during aging. Carbonyls and oxidative stresses, which are intricately linked to one another, predominantly drive such modifications. Oxidative stress leads to the loss of glutathione (GSH) and ascorbate degradation; this in turn leads to the formation of highly reactive dicarbonyl compounds that react with proteins to form advanced glycation end products (AGEs). The formation of AGEs leads to the crosslinking and aggregation of proteins contributing to lens aging and cataract formation. To inhibit AGE formation, we developed a disulfide compound linking GSH diester and mercaptoethylguanidine, and we named it carboxitin. Bovine lens organ cultured with carboxitin showed higher lev

SUBMITTER: Nandi SK 

PROVIDER: S-EPMC8119300 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature