Retraction:A reduction state potentiates the glucocorticoid response through receptor protein stabilization

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Abstract

The intracellular redox state regulates all biological processes including gene expression. The glucocorticoid receptor (GR), a hormone-dependent transcription factor, is affected by the redox state. GR translocation from the cytoplasm to the nucleus is regulated by oxidative stress. The molecular mechanism of how the redox state affects GR transcriptional regulation, however, has not been clarified. We identified a deoxidizing agent, cobalt chloride (CoCl2), that potentiates the GR transcriptional effects by stabilizing endogenously expressed GR protein as well as exogenously over-expressed one without affecting GR mRNA level. Consequent GR protein stabilization enhanced co-factor recruitments on the target gene promoters. These results support the existence of a novel redox-dependent mechanism of GR transcriptional regulation mediated by receptor protein stabilization. © 2007 The Authors Journal compilation © 2007 by the Molecular Biology Society of Japan/Blackwell Publishing Ltd.

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Kitagawa, H., Yamaoka, I., Akimoto, C., Kase, I., Mezaki, Y., Shimizu, T., & Kato, S. (2007). Retraction:A reduction state potentiates the glucocorticoid response through receptor protein stabilization. Genes to Cells. Blackwell Publishing Ltd. https://doi.org/10.1111/j.1365-2443.2007.01131.x

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