TY - JOUR
T1 - Sulfation of resveratrol in human liver: Evidence of a major role for the sulfotransferases SULT1A1 and SULT1E1
AU - Böhmdorfer, Michaela
AU - Maier-Salamon, Alexandra
AU - Aust, Sylvia
AU - Thalhammer, Theresia
AU - Reznicek, Gottfried
AU - Kunert, Olaf
AU - Haslinger, Ernst
AU - Szekeres, Thomas
AU - Jäger, Walter
N1 - DOI: 10.1080/00498250500354253
Coden: XENOB
Affiliations: Department of Clinical Pharmacy and Diagnostics, University of Vienna, Vienna, Austria; Center for Physiology and Pathophysiology, Medical University of Vienna, Vienna, Austria; Department of Pharmacognosy, University of Vienna, Vienna, Austria; Department of Pharmaceutical Chemistry and Pharmaceutical Technology, Karl-Franzens-University Graz, Graz, Austria; Clinical Institute for Medical and Chemical Laboratory Diagnostics, Medical University of Vienna, Vienna, Austria; Department of Clinical Pharmacy and Diagnostics, University of Vienna, A-1090 Vienna, Austria
Adressen: Jaeger, W.; Department of Clinical Pharmacy and Diagnostics; University of Vienna A-1090 Vienna, Austria; email: [email protected]
Source-File: DirschHeringViernsteinScopus_iso.csv
Import aus Scopus: 2-s2.0-31544471832
Importdatum: 29.11.2006 12:38:02
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09.08.2007: Datenanforderung 1815 (Import Sachbearbeiter)
24.08.2007: Datenanforderung 1833 (Import Sachbearbeiter)
22.10.2007: Datenanforderung 1908 (Import Sachbearbeiter)
09.02.2010: Datenanforderung UNIVIS-DATEN-DAT.RA-2 (Import Sachbearbeiter)
PY - 2005
Y1 - 2005
N2 - Sulfation of resveratrol, a polyphenolic compound present in grapes and wine with anticancer and cardioprotective activities, was studied in human liver cytosol. In the presence of 3′-phosphoadenosine-5′-phosphosulfate, three metabolites (M1–3) whose structures were identified by mass spectrometry and NMR as trans-resveratrol-3-O-sulfate, trans-resveratrol-4′-O-sulfate, and trans-resveratrol-3-O-4′-O-disulfate, respectively. The kinetics of M1 formation in human liver cytosol exhibited an pattern of substrate inhibition with a Ki of 21.3 ± 8.73 µM and a Vmax/Km of 1.63 ± 0.41 µL min−1mg−1 protein. Formation of M2 and M3 showed sigmoidal kinetics with about 56-fold higher Vmax/Km values for M3 than for M2 (2.23 ± 0.14 and 0.04 ± 0.01 µL min−1 mg−1). Incubation in the presence of human recombinant sulfotransferases (SULTs) demonstrated that M1 is almost exclusively catalysed by SULT1A1 and only to a minor extent by SULT 1A2, 1A3 and 1E1, whereas M2 is selectively formed by SULT1A2. M3 is mainly catalysed by SULT1A2 and 1A3. In conclusion, the results elucidate the enzymatic pathways of resveratrol in human liver, which must be considered in humans following oral uptake of dietary resveratrol.Read More: http://informahealthcare.com/doi/abs/10.1080/00498250500354253 Œ 2005 Taylor & Francis.
AB - Sulfation of resveratrol, a polyphenolic compound present in grapes and wine with anticancer and cardioprotective activities, was studied in human liver cytosol. In the presence of 3′-phosphoadenosine-5′-phosphosulfate, three metabolites (M1–3) whose structures were identified by mass spectrometry and NMR as trans-resveratrol-3-O-sulfate, trans-resveratrol-4′-O-sulfate, and trans-resveratrol-3-O-4′-O-disulfate, respectively. The kinetics of M1 formation in human liver cytosol exhibited an pattern of substrate inhibition with a Ki of 21.3 ± 8.73 µM and a Vmax/Km of 1.63 ± 0.41 µL min−1mg−1 protein. Formation of M2 and M3 showed sigmoidal kinetics with about 56-fold higher Vmax/Km values for M3 than for M2 (2.23 ± 0.14 and 0.04 ± 0.01 µL min−1 mg−1). Incubation in the presence of human recombinant sulfotransferases (SULTs) demonstrated that M1 is almost exclusively catalysed by SULT1A1 and only to a minor extent by SULT 1A2, 1A3 and 1E1, whereas M2 is selectively formed by SULT1A2. M3 is mainly catalysed by SULT1A2 and 1A3. In conclusion, the results elucidate the enzymatic pathways of resveratrol in human liver, which must be considered in humans following oral uptake of dietary resveratrol.Read More: http://informahealthcare.com/doi/abs/10.1080/00498250500354253 Œ 2005 Taylor & Francis.
U2 - 10.1080/00498250500354253
DO - 10.1080/00498250500354253
M3 - Article
SN - 0049-8254
VL - 35
SP - 1101
EP - 1119
JO - Xenobiotica - the fate of foreign compounds in biological systems
JF - Xenobiotica - the fate of foreign compounds in biological systems
IS - 12
ER -