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Endocrinology Vol. 138, No. 6 2227-2232
Copyright © 1997 by The Endocrine Society

ARTICLES

Regulation by Thyroid-Stimulating Hormone of Sodium/Iodide Symporter Gene Expression and Protein Levels in FRTL-5 Cells

Takahiko Kogai, Toyoshi Endo, Tsukasa Saito, Asako Miyazaki, Akio Kawaguchi and Toshimasa Onaya

Third Department of Internal Medicine, Yamanashi Medical University, Yamanashi 409–38, Japan

Address all correspondence and requests for reprints to: Dr. T. Onaya, Third Department of Internal Medicine, Yamanashi Medical University, Tamaho, Yamanashi 409–38, Japan. E-mail: onayat{at}res.yamanashi-med.ac.jp

To investigate the mechanism of I- transport stimulation by TSH, we studied the effects of TSH on Na+/I- symporter (NIS) messenger RNA (mRNA) and protein levels in FRTL-5 cells and correlated these with I- transport activity. When 1 mU/ml TSH was added to quiescent FRTL-5 cells, a 12-h latency was observed before the onset of increased I- transport activity, which reached a maximum [~27 times basal (5H medium) levels] at 72 h. In contrast, Northern blot analysis, using rat NIS complementary DNA as a probe, revealed that addition of TSH to these cells significantly increased NIS mRNA at 3–6 h, reaching a maximum after 24 h (~5.9 times basal levels). Forskolin and (Bu)2cAMP mimicked this stimulatory effect on both the I- transport activity and mRNA levels. D-ribofranosylbenzimidazole, a transcription inhibitor, almost completely blocked TSH-induced stimulation of I- transport and NIS mRNA levels. Western blot analysis demonstrated that TSH increased NIS protein levels at 36 h, reaching a maximum at 72 h, in parallel with the kinetics of TSH-induced I- transport activity. However, it also showed that the amount of NIS protein already present in FRTL-5 cell membranes before the addition of TSH was about one third of the maximum level induced by TSH. These results indicate that stimulation of I- transport activity by TSH in thyrocytes is partly due to a rapid increase in NIS gene expression, followed by a relatively slow NIS protein synthesis. However, the existence of an abundant amount of protein in quiescent FRTL-5 cells with very low I- transport activity also suggests that this activity is controlled by another TSH-regulated factor(s).




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