Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.

ABSTRACT: As small heat shock proteins, α-crystallins function as molecular chaperones and inhibit the misfolding and aggregation of β/γ-crystallins. Genetic mutations of CRYAA are associated with protein aggregation and cataract occurrence. One possible process underlying cataract formation is that endoplasmic reticulum stress (ERS) induces the unfolded protein response (UPR), leading to apoptosis. However, the pathogenic mechanism related to this remains unexplored. Here, we successfully constructed a cataract-causing CRYAA (Y118D) mutant mouse model, in which the lenses of the CRYAA-Y118D mutant mice showed severe posterior rupture, abnormal morphological changes, and aberrant arrangement of crystallin fibers. Histological analysis was consistent with the clinical pathological characterist

SUBMITTER: Jia ZK 

PROVIDER: S-EPMC8175955 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature