Thyroid stimulating hormone suppresses the expression and activity of cytosolic sulfotransferase 1a1 in thyrocytes
Thyroid stimulating hormone suppresses the expression and activity of cytosolic sulfotransferase 1a1 in thyrocytes
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DOI：
10.1507/endocrj.ej22-0055
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发表时间：
2022-06-09
影响因子：
2
通讯作者：
Suzuki, Koichi
中科院分区：
文献类型：
--
作者：
Nakamura, Yasuhiro;Yoshihara, Aya;Suzuki, Koichi
磺化是多巴胺、雌激素、脱氢表雄酮以及甲状腺激素代谢的重要步骤。然而，在甲状腺细胞溶质磺基转移酶的调节还没有得到很好的理解。在大鼠甲状腺FRTL-5细胞的DNA微阵列分析中，我们发现促甲状腺激素（TSH）显著改变了48种磺基转移酶中的10种的mRNA表达，其中磺基转移酶家族1A成员1（SULT 1A 1）受到的影响最显著。实时PCR和Western blot分析显示，TSH，毛喉素和双丁酰环磷酸腺苷显着抑制SULT 1A 1 mRNA和蛋白水平的时间和浓度依赖性的方式。此外，FRTL-5细胞的免疫荧光染色显示，SULT 1A 1在不存在TSH的情况下定位于核周区域，但在存在TSH的情况下以降低的荧光强度遍布细胞质。用3 '-磷酸腺苷-5'-磷酸硫酸盐作为供体，对硝基苯酚作为受体底物，测定FRTL-5细胞中的磺基转移酶活性，TSH显著降低。这些结果表明，SULT 1A 1的表达和活性的调节TSH在甲状腺细胞。
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.