Article: article from journal or magazin.
The gamma-crystallins and human cataracts: a puzzle made clearer.
American journal of human genetics
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Despite the fact that cataracts constitute the leading cause of blindness worldwide, the mechanisms of lens opacification remain unclear. We recently mapped the aculeiform cataract to the gamma-crystallin locus (CRYG) on chromosome 2q33-35, and mutational analysis of the CRYG-genes cluster identified the aculeiform-cataract mutation in exon 2 of gamma-crystallin D (CRYGD). This mutation occurred in a highly conserved amino acid and could be associated with an impaired folding of CRYGD. During our study, we observed that the previously reported Coppock-like-cataract mutation, the first human cataract mutation, in the pseudogene CRYGE represented a polymorphism seen in 23% of our control population. Further analysis of the original Coppock-like-cataract family identified a missense mutation in a highly conserved segment of exon 2 of CRYGC. These mutations were not seen in a large control population. There is no direct evidence, to date, that up-regulation of a pseudogene causes cataracts. To our knowledge, these findings are the first evidence of an involvement of CRYGC and support the role of CRYGD in human cataract formation.
Amino Acid Sequence, Cataract, Crystallins, DNA Mutational Analysis, Female, Haplotypes, Humans, Male, Models, Molecular, Molecular Sequence Data, Pedigree, Polymerase Chain Reaction, Polymorphism, Genetic, Promoter Regions, Genetic, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid
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