English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Background  αA-crystallin (CRYAA/HSPB4), a major component of all vertebrate eye lenses, is a small heat shock protein responsible for maintaining lens transparency. The R49C mutation in the αA-crystallin protein is linked with non-syndromic, hereditary human cataracts in a four-generation Caucasian family.    Methods  This study describes a mouse cataract model generated by insertion of a neomycin-resistant (neo r ) gene into an intron of the gene encoding mutant R49C αA-crystallin. Mice carrying the neo r  gene and wild-type  Cryaa  were also generated as controls. Heterozygous knock-in mice containing one wild type gene and one mutated gene for αA-crystallin (WT/R49C neo ) and homozygous knock-in mice containing two mutated genes (R49C neo /R49C neo ) were compared.    Results  By 3 weeks, WT/R49C neo  mice exhibited large vacuoles in the cortical region 100 μm from the lens surface, and by 3 months posterior and nuclear cataracts had developed. WT/R49C neo  mice demonstrated severe posterior cataracts at 9 months of age, with considerable posterior nuclear migration evident in histological sections. R49C neo /R49C neo  mice demonstrated nearly complete lens opacities by 5 months of age. In contrast, R49C mice in which the neo r  gene was deleted by breeding with CreEIIa mice developed lens abnormalities at birth, suggesting that the neo r  gene may suppress expression of mutant R49C αA-crystallin protein.    Conclusion  It is apparent that modification of membrane and cell-cell interactions occurs in the presence of the αA-crystallin mutation and rapidly leads to lens cell pathology  in vivo .

αA-crystallin R49Cneomutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice