Редактирование: CRYAA (раздел)

==Publications==

{{medline-entry
|title=Polymorphism rs7278468 is associated with Age-related cataract through decreasing transcriptional activity of the [[CRYAA]] promoter.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/26984531
|abstract=[[CRYAA]] plays critical functional roles in lens transparency and opacity, and polymorphisms near [[CRYAA]] have been associated with age-related cataract ([[ARC]]). This study examines polymorphisms in the [[CRYAA]] promoter region for association with [[ARC]] and elucidates the mechanisms of this association. Three SNPs nominally associated with [[ARC]] were identified in the promoter region of [[CRYAA]]: rs3761382 (P = 0.06, OR (Odds ratio) = 1.5), rs13053109 (P = 0.04, OR = 1.6), rs7278468 (P = 0.007, OR = 0.6). The C-G-T haplotype increased the risk for [[ARC]] overall (P = 0.005, OR = 1.8), and both alleles and haplotypes show a stronger association with cortical cataract (rs3761382, P = 0.002, OR = 2.1; rs13053109, P = 0.002, OR = 2.1; rs7278468, P = 0.0007, OR = 0.5; C-G-T haplotype, P = 0.0003, OR = 2.2). The C-G-T risk haplotype decreased transcriptional activity through rs7278468, which lies in a consensus binding site for the transcription repressor [[KLF10]]. [[KLF10]] binding inhibited [[CRYAA]] transcription, and both binding and inhibition were greater with the T rs7278468 allele. Knockdown of [[KLF10]] in HLE cells partially rescued the transcriptional activity of [[CRYAA]] with rs7278468 T allele, but did not affect activity with the G allele. Thus, our data suggest that the T allele of rs7278468 in the [[CRYAA]] promoter is associated with [[ARC]] through increasing binding of KLF-10 and thus decreasing [[CRYAA]] transcription. 
|mesh-terms=* Aged
* Aged, 80 and over
* Aging
* Alleles
* Binding Sites
* Case-Control Studies
* Cataract
* Cell Line
* Crystallins
* Early Growth Response Transcription Factors
* Female
* Genotype
* Haplotypes
* Humans
* Kruppel-Like Transcription Factors
* Linkage Disequilibrium
* Male
* Middle Aged
* Odds Ratio
* Polymorphism, Single Nucleotide
* Promoter Regions, Genetic
* Protein Binding
* RNA Interference
* RNA, Small Interfering
* Transcription, Genetic

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4794711
}}
{{medline-entry
|title=A novel mutation (F71L) in alphaA-crystallin with defective chaperone-like function associated with age-related cataract.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/19595763
|abstract=Age-related cataract ([[ARC]]) is a multifactorial disease and the leading cause of blindness worldwide. Genetic predisposition in association with other etiological factors may contribute to [[ARC]]. However, gene mutation studies on [[ARC]] are scanty. In the present work, we identified a genetic variation (F71L) in the exon-2 of [[CRYAA]] (alphaA-crystallin) gene in three unrelated female sporadic cases among 711 [[ARC]] patients but not in 265 normal non-cataractous controls by SSCP and RFLP analysis. By comparing human recombinant wild-type and F71L-alphaA-crystallin, we characterized the functional significance of this missense mutation. Chromatography, fluorescence and far- and near-UV CD studies indicated that F71L missense mutation did not significantly affect the apparent molecular mass, secondary and tertiary structures and hydrophobicity of alphaA-crystallin. While the mutant alphaA-crystallin displayed significant (35-90%) loss of chaperone-like activity (CLA) in thermal aggregation of carbonic anhydrase, betaL- and gamma-crystallins, it showed moderate (10-50%) loss in CLA in DTT-induced aggregation of insulin and lysozyme. This is the first report of an alphaA-F71L mutation being associated with [[ARC]] and suggests that [[ARC]] in individuals carrying this mutation (F71L) might be due to the overall loss of in vivo chaperone activity due to interaction with other environmental factors.
|mesh-terms=* Aging
* Amino Acid Substitution
* Base Sequence
* Case-Control Studies
* Cataract
* Chromatography, Gel
* Circular Dichroism
* DNA Mutational Analysis
* Electrophoresis, Polyacrylamide Gel
* Exons
* Female
* Genetic Predisposition to Disease
* Humans
* Light
* Male
* Middle Aged
* Molecular Sequence Data
* Mutant Proteins
* Mutation
* Protein Structure, Quaternary
* Scattering, Radiation
* Spectrometry, Fluorescence
* Time Factors
* Tryptophan
* alpha-Crystallin A Chain

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3816373
}}