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

doi:10.1016/S0006-291X(03)00801-5

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 journal › Article › peer-review

4 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1034-1039
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	305
Issue number	4
DOIs	https://doi.org/10.1016/S0006-291X(03)00801-5
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

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10.1016/S0006-291X(03)00801-5

Cite this

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title = "Stimulation of cellular prion protein expression by TSH in human thyrocytes",

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.",

keywords = "Prion protein, TSH, Thyroid, cDNA microarray",

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

note = "Funding Information: This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan (15590985), the Ministry of Health, Labour and Welfare of Japan (14161301), and CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation (34100).",

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pages = "1034--1039",

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T1 - Stimulation of cellular prion protein expression by TSH in human thyrocytes

AU - Yamazaki, Kazuko

AU - Yamada, Emiko

AU - Kanaji, Yoshio

AU - Yanagisawa, Tetsuo

AU - Kato, Yoshiyuki

AU - Sato, Kanji

AU - Takano, Kazue

AU - Sakasegawa, Yuji

AU - Kaneko, Kiyotoshi

N1 - Funding Information: This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan (15590985), the Ministry of Health, Labour and Welfare of Japan (14161301), and CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation (34100).

PY - 2003/6/13

Y1 - 2003/6/13

N2 - 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.

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.

KW - Prion protein

KW - TSH

KW - Thyroid

KW - cDNA microarray

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Stimulation of cellular prion protein expression by TSH in human thyrocytes

Abstract

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ASJC Scopus subject areas

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