Sulfation of hesperetin,naringenin and apigenin by the human cytosolic sulfotransferases: a comprehensive analysis |
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| Authors: | Amal A. El Daibani Yuecheng Xi Lijun Luo Xue Mei Chunyang Zhou Shin Yasuda |
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| Affiliation: | 1. Department of Pharmacology College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, Toledo, OH, USA;2. School of Pharmacy, North Sichuan Medical College, Nanchong, Sichuan, China;3. School of Pharmacy, North Sichuan Medical College, Nanchong, Sichuan, China;4. Graduate School of Bioscience, Tokai University, Kumamoto City, Kumamoto, Japan |
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| Abstract: | AbstractPrevious studies have revealed sulfation as a major pathway for the metabolism of hesperetin, naringenin and apigenin. The current study was designed to identify the human cytosolic sulfotransferase (SULT) enzyme(s) capable of sulfating these flavonoid compounds. Of the thirteen human SULTs, six (1A1, 1A2, 1A3, 1B2, 1C4, 1E1) displayed significant sulfating activity toward hesperetin, five (1A1, 1A2, 1A3, 1B2, 1C4) displayed sulfating activity towards naringenin, and four (1A1, 1A2, 1A3, 1C4) showed sulfating activity towards apigenin. Of the four human organ specimens tested, liver and intestine cytosols displayed much higher hesperetin-, naringenin- and apigenin-sulfating activity than lung and kidney cytosols. Moreover, sulfation of hesperetin, naringenin and apigenin was shown to take place in HepG2 human hepatoma cells and Caco-2 human colon adenocarcinoma cells under cultured conditions. Taken together, these results provided a biochemical basis underlying the metabolism of hesperetin, naringenin and apigenin through sulfation in humans. | |
| Keywords: | Hesperetin naringenin apigenin sulfation cytosolic sulfotransferase SULT |
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