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Background  Age-related cataract (ARC) is the leading cause of visual impairment worldwide, and α-crystallin ( CRYAA ) is the predominant structural protein involved in the maintenance of lens clarity and refractive properties. We previously demonstrated that  CRYAA  genes undergo epigenetic repression in the lens epithelia in ARC. We further analyze the underlying mechanism in the current study.    Methods  The transcription factor binding sites of the CpG island of  CRYAA  promoter were predicted by TESS website. An electrophoretic mobility shift assay (EMSA) was used to analyze the impact of the methylation of CpG sites on transcription factors. Human lens epithelial B-3 (HLE B-3) Cells were treated with demethylation agent zebularine in the concentrations of 0 (PBS as control), 10 μM, 20 μM, 50 μM, 100 μM and 200 μM, respectively. After treatment in the above concentrations for 24 h, 48 h and 72 h, respectively,  CRYAA  mRNA expression levels were detected by Quantitative Real-Time RT-PCR.    Results  The methylation of the CpG site of the  CRYAA  promoter decreased the DNA-binding capacity of transcription factor Sp1. Zebularine increased  CRYAA  expression in HLE B-3 Cells in a dose- dependent and time- dependent pattern.    Conclusions  The evidence presented suggests that the methylation of the CpG sites of the  CRYAA  promotor directly affect Sp1 binding, leading to down expression of  CRYAA  in human lens epithelial cells. Zebularine treatment could restore  CRYAA  expression in a dose- dependent and time- dependent pattern.    Electronic supplementary material  The online version of this article (doi:10.1186/s12886-016-0309-y) contains supplementary material, which is available to authorized users.

CpG site methylation in CRYAA promoter affect transcription factor Sp1 binding in human lens epithelial cells