Sulfation of Iodothyronines by Recombinant Human Liver Steroid Sulfotransferases

作者: Xinying Li , Robert J. Anderson

DOI: 10.1006/BBRC.1999.1419

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摘要: Abstract Sulfation is an important pathway in the metabolism of thyroid hormones. Sulfated iodothyronines are elevated nonthyroidal illnesses and normal human fetal circulation. We assayed characterized COS-1 cell expressed recombinant liver dehydroepiandrosterone sulfotransferase (DHEA ST or SULT2A1) estrogen (EST SULT1E1) activities for first time with triiodothyronine (T3) as substrate. Several biochemical properties that included apparent Km values, thermal stabilities, responses to inhibitors 2,6-dichloro-4-nitrophenol NaCl were tested. SULT2A1, a member hydroxysteroid family, used 3,3′-T2 more readily than T3 3,5-T2 substrates, but had lowest value any reported SULT. SULT1E1, phenol rT3 T3, also displayed greatest specificity T4 among SULTs. SULT2A1 may contribute iodothyronine sulfation previously suspected. Potential roles both steroid sulfotransferases enhanced development invite further investigation.

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