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Vol. 294, Issue 3, 837-843, September 2000
-Glucoside
by Sodium-Dependent Glucose Transporter SGLT11
Department of Cell and Molecular Pharmacology and Experimental
Therapeutics, Medical University of South Carolina, Charleston, South
Carolina (R.A.W., T.W.); and Max-Planck-Institut für Molekulare
Physiologie, Dortmund, Germany (J.T.L., R.K.H.K.)
Although it has been suggested that the intestinal glucose transporter
may actively absorb dietary flavonoid glucosides, there is a lack of
direct evidence for their transport by this system. In fact, our
previous studies with the human Caco-2 cell model of intestinal
absorption demonstrated that a major dietary flavonoid, quercetin
4'-
-glucoside, is effluxed by apically expressed multidrug resistance-associated protein-2, potentially masking evidence for
active absorption. The objective of this study was to test the
hypothesis that quercetin 4'--glucoside is a substrate for the
intestinal sodium-dependent D-glucose cotransporter SGLT1. Cellular uptake of quercetin 4'--glucoside was examined with Caco-2
cells and SGLT1 stably transfected Chinese hamster ovary cells
(G6D3 cells). Although quercetin 4'--glucoside is not absorbed across Caco-2 cell monolayers, examination of the cells by indirect fluorescent microscopy as well as by HPLC analysis of cellular content
revealed cellular accumulation of this glucoside after apical loading.
Consistent with previous observations, the accumulation of quercetin
4'--glucoside in both Caco-2 and G6D3 cells was markedly enhanced in
the presence of multidrug resistance-associated protein inhibition.
Uptake of quercetin 4'--glucoside was greater in SGLT1-transfected
cells than in parental Chinese hamster ovary cells. Uptake of the
glucoside by Caco-2 and G6D3 cells was sodium-dependent and was
inhibited by the monovalent ionophore nystatin. In both Caco-2 and G6D3
cells, quercetin 4'--glucoside uptake was inhibited by 30 mM glucose
and 0.5 mM phloridzin. These results demonstrate for the first time
that quercetin 4'--glucoside is transported by SGLT1 across the
apical membrane of enterocytes.
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