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Updated: Aug 29, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
Published on: September 7, 2021
[Change of alpha-crystallin acting as molecular chaperone activity with ageing]
Hong Yan1, Yanninan Hui, Jiangguo Fan
1Department of Ophthalmology, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, China.
Purpose:
To evaluate the molecular chaperone function of alpha-crystallin with ageing.
Methods:
alpha-Crystallin of newborn, adult and old rabbits lenses in both of cortex and nucleus were separated by chromatography on Sephacryl S-300HR. The protection of alpha-crystallin against thermal aggregation of catalase and beta L-crystallin (60 degrees C), inactivation of catalase by fructose(37 degrees C) and heat stress(60 degrees C) were measured spectrophotometrically.
Results:
Protection of alpha-crystallin against aggregation and inactivation using four methods showed a similar pattern. The protective ability in cortex was greatly higher than in nucleus of different-aged lenses, and alpha H-crystallin was less than alpha L-crystallin in both cortex and nucleus. There was no statistically decrease with age of chaperone function of both alpha H-crystallin and alpha L-crystallin in the cortex, whereas alpha L-crystallin in the nucleus was compromised.
Conclusion:
alpha-Crystallin in the nucleus shows age-related decrease in chaperone function, which may be responsible for cataract formation.
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