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• W2559561657 abstract "Cataract, the leading cause of blindness worldwide, is caused by the apoptosis of lens epithelial cells (LECs). αA-crystallin is a major structural protein of the lens. However, the antiapoptotic function of αA-crystallin in lens stem cells remains unclear. In this study, primary LECs were isolated from postnatal 3-5 days of SD rats and transfected by Sendai virus loaded with four factors, OCT3/4, Sox2, c-Myc, and Klf4, to induced pluripotent stem cells (iPSCs). LEC-iPSC-like cells were identified by immunofluorescent staining. CryαA-specific shRNA lentivirus was used to knockdown αA-crystallin in LEC-derived iPSC-like cells, which were treated with tert-Butyl hydroperoxide. The apoptosis of LEC-iPSC-like cells was examined by flow cytometry. We reprogrammed LECs and obtained embryonic stem cell-like colonies. LEC-iPSC-like cells with normal karyotype expressed pluripotent markers such as SSEA-4, TRA-1-60, and TRA-1-81. Knockdown of αA-crystallin increased the apoptosis of LEC-iPSC-like cells and rendered them less resistant to oxidation stress induced by tert-Butyl hydroperoxide. In conclusion, LECs could be reprogrammed into iPSC-like cells and αA-crystallins could protect LEC-iPSC-like cells from oxidation stress-induced apoptosis." @default.
• W2559561657 created "2016-12-08" @default.
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• W2559561657 date "2016-10-01" @default.
• W2559561657 modified "2023-09-25" @default.
• W2559561657 title "Alpha-A-Crystallin Protects Lens Epithelial Cell-Derived iPSC-Like Cells Against Apoptosis Induced by Oxidative Stress" @default.
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• W2559561657 doi "https://doi.org/10.1089/cell.2016.0017" @default.
• W2559561657 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27696911" @default.
• W2559561657 hasPublicationYear "2016" @default.
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