Abstract
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.
Original language | English |
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Pages (from-to) | 1034-1039 |
Number of pages | 6 |
Journal | Biochemical and biophysical research communications |
Volume | 305 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2003 Jun 13 |
Externally published | Yes |
Keywords
- Prion protein
- TSH
- Thyroid
- cDNA microarray
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology