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• W2580818401 abstract "In this study, we aimed to obtain a comprehensive account of the human cytosolic sulfotransferases (SULTs) that are capable of sulfating 6-O-desmethylnaproxen (O-DMN), a major metabolite of naproxen. Of the 13 known human SULTs tested, 7 (SULT1A1, SULT1A2, SULT1A3, SULT1B1, SULT1C2, SULT1C4, and SULT1E1) displayed O-DMN-sulfating activity, when analyzed using an elevated substrate concentration (500 μmol·L −1 ) together with 14 μmol·L −1 of the sulfate donor, 3′-phosphoadenosine-5′-phosphosulfate (PAPS). At 10 μmol·L −1 O-DMN concentration, however, only SULT1A1 and SULT1A3 displayed detectable activity, with the former being nearly 2 orders of magnitude more active than the latter. A pH-dependence study indicated that SULT1A1 exhibited a broad pH optimum spanning pH 5.5–7. Kinetic parameters of the sulfation of O-DMN by SULT1A1 were determined. The production and release of sulfated O-DMN was demonstrated using cultured human HepG2 hepatoma cells and Caco-2 colon carcinoma cells. Moreover, assays using human organ specimens revealed that the O-DMN-sulfating activities present in the cytosols of liver and small intestine (at 502.5 and 497.2 pmol·min −1 ·(mg protein) −1 , respectively) were much higher than those detected for the cytosols of lung and kidney. Taken together, these results provided relevant information concerning the sulfation of O-DMN both in vitro and in vivo." @default.
• W2580818401 created "2017-02-03" @default.
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• W2580818401 date "2017-06-01" @default.
• W2580818401 modified "2023-09-24" @default.
• W2580818401 title "A reappraisal of the 6-<i>O</i>-desmethylnaproxen-sulfating activity of the human cytosolic sulfotransferases" @default.
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• W2580818401 doi "https://doi.org/10.1139/cjpp-2016-0403" @default.
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