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Lanosterol reverses protein aggregation in cataracts.

Ling Zhao¹, Xiang-Jun Chen², Jie Zhu³

¹1] Molecular Medicine Research Center, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu 610041, China [2] State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou 510060, China [3] Department of Ophthalmology and Biomaterials and Tissue Engineering Center, Institute for Engineering in Medicine, University of California San Diego, La Jolla, California 92093, USA.

|July 23, 2015

Summary

Lanosterol, a molecule found in the eye lens, prevents protein aggregation that causes cataracts. This discovery offers a potential new treatment strategy for preventing and treating this common cause of blindness.

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Characterization of Molecular Mechanisms of In vivo UVR Induced Cataract

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Published on: November 28, 2012

Area of Science:

Ophthalmology
Molecular Biology
Biochemistry

Background:

Cataracts, the leading cause of blindness, result from protein aggregation in the human lens, disrupting transparency.
Current treatments involve surgical removal of the cataractous lens, with limited understanding of underlying prevention mechanisms.
Lens transparency relies on the ordered structure of crystallin proteins, which is disrupted by altered protein interactions.

Purpose of the Study:

To investigate the role of lanosterol in preventing lens protein aggregation and cataract formation.
To identify genetic mutations affecting lanosterol synthesis and their link to congenital cataracts.
To explore lanosterol as a potential therapeutic agent for cataracts.

Main Methods:

Identified homozygous missense mutations in the lanosterol synthase (LSS) gene in families with congenital cataracts.
Assessed the catalytic function of mutated LSS and its effect on preventing crystallin aggregation.
Tested the efficacy of lanosterol and cholesterol in reducing protein aggregates in vitro, cell cultures, and ex vivo/in vivo lens models.

Main Results:

Two novel LSS mutations (W581R and G588S) were found to impair LSS catalytic function, leading to congenital cataracts.
Wild-type LSS expression prevented aggregation of cataract-causing crystallins, while mutant LSS did not.
Lanosterol treatment significantly reduced preformed protein aggregates and improved lens transparency in various models, unlike cholesterol.

Conclusions:

Lanosterol is crucial for preventing lens protein aggregation and maintaining lens transparency.
Mutations in LSS impairing lanosterol synthesis are linked to congenital cataracts.
Lanosterol represents a promising therapeutic target for novel cataract prevention and treatment strategies.