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Retracted: A reduction state potentiates the glucocorticoid response through receptor protein stabilization
Author(s) -
Kitagawa Hirochika,
Yamaoka Ikuko,
Akimoto Chihiro,
Kase Ikuko,
Mezaki Yoshihiro,
Shimizu Takafumi,
Kato Shigeaki
Publication year - 2007
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2007.01131.x
Subject(s) - glucocorticoid receptor , biology , transcriptional regulation , transcription factor , glucocorticoid , cytoplasm , microbiology and biotechnology , oxidative stress , receptor , promoter , regulation of gene expression , redox , gene , gene expression , intracellular , nuclear receptor , biochemistry , endocrinology , chemistry , organic chemistry
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 (CoCl 2 ), 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.