Cleavage C-terminal to Asp leads to covalent crosslinking of long-lived human proteins.

ABSTRACT: With age, long-lived proteins in the human body deteriorate, which can have consequences both for aging and disease. The aging process is often associated with the formation of covalently crosslinked proteins. Currently our knowledge of the mechanism of formation of these crosslinks is limited. In this study, proteomics was used to characterize sites of covalent protein-protein crosslinking and identify a novel mechanism of protein-protein crosslinking in the adult human lens. In this mechanism, Lys residues are crosslinked to C-terminal Asp residues that are formed by non-enzymatic protein truncation. Ten different crosslinks were identified in major lens proteins such as αA-crystallin, αB-crystallin and AQP0. Crosslinking in AQP0 increased significantly with age and also increased signif

SUBMITTER: Wang Z 

PROVIDER: S-EPMC9227964 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature