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Nicotinamide Adenine Dinucleotide Phosphate-Dependent Cytosolic T₃ Binding Protein as a Regulator for T₃-Mediated Transactivation

Department of Aging Medicine and Geriatrics (J.-i.M., S.S., T.I., A.K., T.T., T.M., K.I., K.H.), Shinshu University School of Medicine, 3-1-1, Asahi, Matsumoto, 390-8621, Japan; and Iida Municipal Hospital (M.K.), 438, Yawata, Iida, 395-0814, Japan

Address all correspondence and requests for reprints to: Satoru Suzuki, M.D., Ph.D., Department of Aging Medicine and Geriatrics, Shinshu University School of Medicine, 3-1-1, Asahi, Matsumoto, Nagano, 390-8621, Japan. E-mail: . soutaro{at}hsp.md.shinshu-u.ac.jp

Nicotinamide adenine dinucleotide phosphate (NADPH)- dependent cytosolic T₃ binding protein (CTBP) plays a role in the regulation of nuclear transport of T₃ in vitro. However, it is not known whether CTBP regulates the T₃ action. In this study, we examined the effects of CTBP on cellular translocation of T₃ and on transcriptional activation using established CTBP-expressing CHO or GH3 cells.

The expression of CTBP increased cellular and nuclear uptake of T₃ in the CTBP-expressing cells. The efflux rate was decreased by induction of CTBP. Efflux from nuclei also inhibited by induction of CTBP.

Expression of CTBP suppressed the T₃-regulated luciferase activity in GH3 cells. Suppression was observed to be related to the expression level of CTBP. T₃ induction of rat GH mRNA was lower in the cells expressing CTBP than that in CTBP-null cells.

These results suggest that CTBP regulates the T₃-induced gene expression, with which an increase in the nuclear content of the T₃ is associated. Because we observed that a part of CTBP could be transported into nuclei and that acceptor protein for CTBP is present in nuclei as previously reported, interaction of CTBP with certain proteins, including transcription factors or nuclear T₃ receptor, may contribute to the regulation.

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