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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Previously we showed that glycation-induced inactivation and loss of antigenicity of enzymes occur simultaneously. α-Crystallin, a major structural protein of the mammalian lens, prevents the aggregation of other proteins and protects enzyme function against post-translational modification in vitro. However, it is not known whether αcrystallin can also protect against loss of antigenicity of enzymes. Esterase activity in the lens is decreased in senile cataract and diabetes. We investigated the loss of antigenicity of esterase caused by different insults and the ability of α-crystallin to protect. Inactivation of carboxylesterase by sugars, fructose 6-phosphate (F6P) and a steroid, prednisolone-21-hemisuccinate (P-21-H), was measured spectrophotometrically in the presence and absence of α-crystallin, while loss of antigenicity was monitored simultaneously using an immunoprecipitation method. The esterase was progressively inactivated by fructose, F6P, ribose, and P 21-H. Bovine α-crystallin fully protected against inactivation of esterase by all four compounds, and also protected against loss of antigenicity of the esterase by fructose, ribose and P-21-H at a molar ratio of 1:1. The results indicated that α-crystallin, under our experimental conditions, clearly exhibited the ability to prevent loss of antigenicity and inactivation of esterase. The protective effect of αcrystallin against loss of antigenicity indicates a novel aspect of its chaperoning function.

The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid