NR ANZS
AU Yamazaki,K.; Yamada,E.; Kanaji,Y.; Yanagisawa,T.; Kato,Y.; Sato,K.; Takano,K.; Sakasegawa,Y.; Kaneko,K.
TI Stimulation of cellular prion protein expression by TSH in human thyrocytes
QU Biochemical and Biophysical Research Communications 2003 Jun 13; 305(4): 1034-9
PT journal article
AB The cellular isoform of prion protein (PrPc) 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 PrPc may be involved in structure formation or maintenance of thyroid follicles.
MH Animal; Cells, Cultured; Gene Expression Profiling; Gene Expression Regulation; Graves' Disease/genetics/metabolism; Human; Mice; Oligonucleotide Array Sequence Analysis; PrPc Proteins/*biosynthesis/genetics; RNA, Messenger/biosynthesis; Support, Non-U.S. Gov't; Thyroid Gland/anatomy & histology/drug effects/*metabolism; Thyrotropin/*pharmacology; Tumor Cells, Cultured; Up-Regulation
AD Thyroid Disease Institute, Kanaji Hospital, Kita-ku, Tokyo 114-0015, Japan.
SP englisch
PO USA