Human Cytosolic Sulfotransferase SULT1A3 Mediates the Sulfation of Dextrorphan
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- Yamamoto Akihiro
- Department of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki
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- Kurogi Katsuhisa
- Department of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki
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- Schiefer Isaac Thomas
- Department of Medicinal and Biological Chemistry, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus
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- Liu Ming-Yih
- National Synchrotron Radiation Research Center
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- Sakakibara Yoichi
- Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki
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- Suiko Masahito
- Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki
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- Liu Ming-Cheh
- Department of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus
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説明
<p>Dextrorphan, an active metabolite of the antitussive dextromethorphan, has been shown to be subjected to sulfation by several zebrafish cytosolic sulfotransferases (SULTs). We were interested in finding out which of the human SULT(s) is(are) capable of catalyzing the sulfation of dextrorphan, and to verify whether sulfation of dextrorphan may occur in cultured human cells and human organ cytosols. Data from the enzymatic assays showed that, of all thirteen known human SULTs, SULT1A3 displayed the strongest dextrorphan-sulfating activity. Cell culture experiments using HepG2 human hepatoma cells and Caco-2 human colon carcinoma cells incubated with [35S]sulfate together with varying concentrations of dextrorphan revealed indeed the production and release of [35S]sulfated dextrorphan in a concentration-dependent manner. Additionally, significant dextrorphan-sulfating activity was detected in human liver, small intestine and lung cytosols. Taken together, these results provided a biochemical basis for the sulfation of dextrorphan in humans.</p>
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 39 (9), 1432-1436, 2016
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390282679609192960
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- NII論文ID
- 130005262319
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- NII書誌ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 027565530
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- PubMed
- 27582324
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- PubMed
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