Stimulation of cellular prion protein expression by TSH in human thyrocytes |
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Authors: | Yamazaki Kazuko Yamada Emiko Kanaji Yoshio Yanagisawa Tetsuo Kato Yoshiyuki Sato Kanji Takano Kazue Sakasegawa Yuji Kaneko Kiyotoshi |
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Institution: | Thyroid Disease Institute, Kanaji Hospital, Kita-ku, Tokyo 114-0015, Japan. |
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Abstract: | The cellular isoform of prion protein (PrP(C)) is a cell-surface glycosyl-phosphatidylinositol-anchored protein which is ubiquitously expressed on the cell membrane. It may function as a cell receptor or as a cell adhesion molecule. Thyroid follicles, obtained from patients with Graves' disease at thyroidectomy, were cultured in F-12/RPMI-1640 medium supplemented with 0.5% fetal bovine serum and bovine thyroid stimulating hormone (bTSH). Northern blot analyses revealed that bTSH increased the steady-state expression levels of PrP mRNA in a time- and dose-dependent manner. This increase was reproduced by dibutyryl-cAMP and 12-decanoylphorbol-13-acetate. The mRNA expression was greater in thyroid follicles in suspension culture than in thyrocytes cultured in a monolayer. These findings suggest that TSH stimulates PrP mRNA expression in thyrocytes through the protein kinase A and C pathways. The greater mRNA expression in thyroid follicles than in monolayer cells suggests that PrP(C) may be involved in structure formation or maintenance of thyroid follicles. |
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Keywords: | Prion protein Thyroid TSH cDNA microarray |
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