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Department of Pharmacology and Toxicology, Nijmegen Center for Molecular Life Sciences, 6500 HB, Nijmegen, The Netherlands;
*
RIKILT, Wageningen University and Research Centre, 6700 AE, Wageningen, The Netherlands; and
Small Animal Research Center, Wageningen University, 6700 HB, Wageningen, The Netherlands
2To whom correspondence should be addressed. E-mail: a.sesink{at}ncmls.kun.nl.
Quercetin has antioxidant, anti-inflammatory, antiproliferative and anticarcinogenic properties. In plant foods, quercetin occurs mainly bound to various sugars via a ß-glycosidic link. We hypothesized that lactase phlorizin hydrolase (LPH), an enzyme at the brush border membrane of intestinal cells, is involved in the in vivo intestinal uptake of quercetin-sugars. To study this, we measured the appearance of quercetin metabolites in plasma and perfusate after perfusing the jejunum and ileum with 50 µmol/L quercetin-3-glucoside in an in situ rat perfusion model. LPH was inhibited by the selective LPH inhibitor N-butyldeoxygalactonojirimycin (0, 0.5, 2 or 10 mmol/L) (n = 5 rats/group). Quercetin in plasma and perfusion buffer was determined by HPLC with CoulArray detection. Results are given as means ± SEM. In the perfusion buffer, 13.8 ± 0.7 µmol/L quercetin-3-glucoside was hydrolyzed during intestinal passage. Co-perfusion with 0.5, 2 and 10 mmol/L N-butyldeoxygalactonojirimycin resulted in 38% (P < 0.05), 50% (P < 0.01) and 67% (P < 0.01) less hydrolysis, respectively. Plasma concentrations of quercetin in the corresponding groups were 36% (P = 0.12), 55% (P < 0.01) and 75% (P < 0.01) lower than in controls (1.23 ± 0.22 µmol/L). These data suggest that LPH is a major determinant of intestinal absorption of quercetin-3-glucoside in rats.
KEY WORDS: • flavonoids • quercetin-3-glucoside • lactase phlorizin hydrolase • intestinal uptake • rats
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