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Thomas Walle - One of the best experts on this subject based on the ideXlab platform.

  • efflux of dietary flavonoid quercetin 4 β glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

  • efflux of dietary flavonoid quercetin 4 beta glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

Richard A Walgren - One of the best experts on this subject based on the ideXlab platform.

  • efflux of dietary flavonoid quercetin 4 β glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

  • efflux of dietary flavonoid quercetin 4 beta glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

George E Lindenmayer - One of the best experts on this subject based on the ideXlab platform.

  • efflux of dietary flavonoid quercetin 4 β glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

  • efflux of dietary flavonoid quercetin 4 beta glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

Karl J Karnaky - One of the best experts on this subject based on the ideXlab platform.

  • efflux of dietary flavonoid quercetin 4 β glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

  • efflux of dietary flavonoid quercetin 4 beta glucoside across human intestinal caco 2 cell monolayers by apical multidrug resistance associated protein 2
    Journal of Pharmacology and Experimental Therapeutics, 2000
    Co-Authors: Richard A Walgren, Karl J Karnaky, George E Lindenmayer, Thomas Walle
    Abstract:

    Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-Beta-Glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-Beta-Glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-Beta-Glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-Beta-Glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

Lingyi Kong - One of the best experts on this subject based on the ideXlab platform.

  • preparative isolation and purification of chemical constituents from the root of polygonum multiflorum by high speed counter current chromatography
    Journal of Chromatography A, 2006
    Co-Authors: Shun Yao, Lingyi Kong
    Abstract:

    High-speed counter-current chromatography methods, combined with solvent partition, were applied to the systematic separation and purification of chemical components from Chinese medicinal herb Polygonum multiflorum extract. The aim of this paper is summing up the rules of solvent system selection for diverse fractions of herbal extract, and establishing the systematic pattern to screen the bioactive constituents rapidly. Nine compounds including emodin, chrysophanol, rhein, 6-OH-emodin, emodin-8-beta-D-glucoside, polygonimitin B, 2,3,5,4'-tetrahydroxystilbene-2-beta-D-glucoside, gallic acid and an unknown glycoside, which differed in quantity and polarity remarkably, were obtained. The purities of them were all above 97% as determined by high-performance liquid chromatography (HPLC), and their structures were identified by 1H NMR and electrospray ionization mass spectrometry (ESI-MS). The results demonstrated that HSCCC is a speedy and efficient technique for systematic isolation of bioactive components from traditional medicinal herbs.