The gamma-crystallins and human cataracts: a puzzle made clearer.

Details

Serval ID
serval:BIB_13034
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The gamma-crystallins and human cataracts: a puzzle made clearer.
Journal
American journal of human genetics
Author(s)
Héon E., Priston M., Schorderet D.F., Billingsley G.D., Girard P.O., Lubsen N., Munier F.L.
ISSN
0002-9297
Publication state
Published
Issued date
1999
Peer-reviewed
Oui
Volume
65
Number
5
Pages
1261-7
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Abstract
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.
Keywords
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
Pubmed
Web of science
Open Access
Yes
Create date
19/11/2007 12:04
Last modification date
20/08/2019 12:41
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