The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.

ABSTRACT: Transparency in the lens is accomplished by the dense packing and short-range order interactions of the crystallin proteins in fiber cells lacking organelles. These features are accompanied by a lack of protein turnover, leaving lens proteins susceptible to a number of damaging modifications and aggregation. The loss of lens transparency is attributed in part to such aggregation during aging. Among the damaging post-translational modifications that accumulate in long-lived proteins, isomerization at aspartate residues has been shown to be extensive throughout the crystallins. In this study of the human lens, we localize the accumulation of l-isoaspartate within water-soluble protein extracts primarily to crystallin peptides in high-molecular weight aggregates and show with MS that these pe

SUBMITTER: Warmack RA 

PROVIDER: S-EPMC6690693 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature