Article
A novel mutation impairing the tertiary structure and stability of γC-crystallin (CRYGC) leads to cataract formation in humans and zebrafish lens.
Human mutation - 1 Feb 2012
Li Xiao-Qiao, Cai Hong-Chen, Zhou Shi-Yi, Yang Ju-Hua, Xi Yi-Bo, Gao Xiao-Bo, Zhao Wei-Jie, Li Peng, Zhao Guang-Yu, Tong Yi, Bao Fan-Chen, Ma Yan, Wang Sha, Yan Yong-Bin, Lu Cai-Ling, Ma Xu
Abstract excerpt
Congenital cataract is one of the leading causes of human blindness. In this study, we identified a novel, heterozygous c.385G<T mutation in CRYGC that resulted in the substitution of a highly conserved glycine by cysteine at codon 129 (p.Gly129Cys) in a three-generation Chinese family with autosomal dominant congenital nuclear cataract by sequencing candidate genes. Using zebrafish as a model, we demonstrated...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Base Sequence
- Cataract
- Child
- Female
- Humans
- Male
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Pedigree