Stimulation of cellular prion protein expression by TSH in human thyrocytes

Kazuko Yamazaki, Emiko Yamada, Yoshio Kanaji, Tetsuo Yanagisawa, Yoshiyuki Kato, Kanji Sato, Kazue Takano, Yuji Sakasegawa, Kiyotoshi Kaneko

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 languageEnglish
Pages (from-to)1034-1039
Number of pages6
JournalBiochemical and biophysical research communications
Volume305
Issue number4
DOIs
Publication statusPublished - 2003 Jun 13

Keywords

  • Prion protein
  • TSH
  • Thyroid
  • cDNA microarray

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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