Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.

ABSTRACT:

Purpose

Crystallins are major functional and structural proteins in mammalian lens. Their expression, distribution, and protein-protein interaction affect lens development and fiber cell differentiation. Mutated crystallins lead to structural and functional changes of lens structure and could lead to opacity formation and cataract development. The purpose of this study was to investigate the biological effects of the cataract-causing G98R mutation on the alphaA-crystallin (CRYAA) protein and to test the capability of chemical chaperone trimethylamine N-oxide (TMAO) to reverse such effects.

Methods

Myc/His-tagged, human, full-length, wild-type (WT) or G98R CRYAA was expressed in human lens epithelial B3 cells and treated or not treated with TMAO. Triton X-100 (Tx) solubility

SUBMITTER: Gong B 

PROVIDER: S-EPMC2796635 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature