FKBP51 prevents oxidative stress-induced cell death and stimulates cell proliferation

DE LEO S.A.; CAMISAY M.F.; MAZAIRA G.I.; GALIGNIANA M.D.; DISERTANTE INVITADO: ERLEJMAN A.G.

Montevideo

Simposio; Thiol Metabolism and Redox Regulation of Cellular Functions Symposium and Course.; 2015

Institut Pasteur de Montevideo

FKBP51 (FK506-Binding Protein 51-kDa) was primarily described as regulator of steroid-receptor trafficking and biological activity. Here we studied its role in cell proliferation and cell viability. When HEK293-51 (a cell line stably expressing FKBP51) were treated with H2O2 or staurosporine, a significant increase of cell viability was evidenced compared to the parent cell line (HEK293-WT), while FKBP52 (a highly FKBP51 homolog) overexpression decreased cell viability. Upon H2O2 treatment, FKBP51 translocated from mitochondria to nuclei, a relocalization that was prevented by glutathione. Cell viability (MTT assay and cell viability count) was significantly increased in HEK293-51 cells compared to WT cells or empty vector-transfected cells, whereas the overexpression of FKBP52 itself showed no significant effect. We propose that FKBP51 itself plays a stimulating role on cell proliferation, and deleterious stimuli promote its rapid nuclear relocalization to protect cells, an effect that is opposed by FKBP52.