Thyroid stimulating hormone suppresses the expression and activity of cytosolic sulfotransferase 1a1 in thyrocytes

Endocrine journal

article

Yasuhiro Nakamura¹  Aya Yoshihara²  Mitsuo Kiriya²  Akira Kawashima²  Kazunari Tanigawa¹  Yuqian Luo⁴  Yoko Fujiwara²  Keiji Maruyama¹  Shigekazu Watanabe¹  Fumiko Kihara-Negishi¹  Ken Karasawa¹  Koichi Suzuki² 

[1] Faculty of Pharma-Science, Teikyo University;Department of Clinical Laboratory Science, Faculty of Medical Technology, Teikyo University;Center for Medical Education, Faculty of Medicine, Toho University;Department of Laboratory Medicine, Nanjing Drum Tower Hospital and Jiangsu Key Laboratory for Molecular Medicine, Nanjing University Medical School

关键词: Thyroid;    Sulfotransferase;    Sulfotransferase family 1A member 1 (SULT1A1);    Thyroid stimulating hormone;    FRTL-5;   

DOI  :  10.1507/endocrj.EJ22-0055

学科分类：内分泌与代谢学

来源: Japan Endocrine Society

【 摘 要 】

Sulfonation is an important step in the metabolism of dopamine, estrogens, dehydroepiandrosterone, as well as thyroid hormones. However, the regulation of cytosolic sulfotransferases in the thyroid is not well understood. In a DNA microarray analysis of rat thyroid FRTL-5 cells, we found that the mRNA expression of 10 of 48 sulfotransferases was significantly altered by thyroid stimulating hormone (TSH), with that of sulfotransferase family 1A member 1 (SULT1A1) being the most significantly affected. Real-time PCR and Western blot analyses revealed that TSH, forskolin and dibutyryl cyclic AMP significantly suppressed SULT1A1 mRNA and protein levels in a time- and concentration-dependent manner. Moreover, immunofluorescence staining of FRTL-5 cells showed that SULT1A1 is localized in the perinuclear area in the absence of TSH but is spread throughout the cytoplasm with reduced fluorescence intensity in the presence of TSH. Sulfotransferase activity in FRTL-5 cells, measured using 3'-phosphoadenosine-5'-phosphosulfate as a donner and p-nitrophenol as an acceptor substrate, was significantly reduced by TSH. These findings suggest that the expression and activity of SULT1A1 are modulated by TSH in thyrocytes.

【 授权许可】

Unknown