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.
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