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• W1587467241 abstract "The bioactive dipeptide derivative anserine (beta-alanyl-1-N-methyl-L-histidine) is absorbed from the human diet in intact form at the intestinal epithelium. The purpose of this study was to investigate whether anserine is a substrate of the H(+)/peptide cotransporters 1 and 2 (PEPT1 and PEPT2). We first assessed the effects of anserine on [(14)C]glycylsarcosine ([(14)C]Gly-Sar) uptake into Caco-2 cells expressing human PEPT1 and into spontaneous hypertensive rat kidney proximal tubule (SKPT) cells expressing rat PEPT2. Anserine inhibited [(14)C]Gly-Sar uptake with K(i) values of 1.55 mM (Caco-2) and 0.033 mM (SKPT). In HeLa cells transfected with pcDNA3-hPEPT1 or pcDNA3-hPEPT2, K(i) values of 0.65 mM (hPEPT1) and 0.18 mM (hPEPT2) were obtained. We conclude from these data that anserine is recognized by PEPT1 and PEPT2. Carnosine also inhibited [(14)C]Gly-Sar uptake. Using the two-electrode, voltage-clamp technique at Xenopus laevis oocytes, strong hPEPT1-specific inward transport currents were recorded for Gly-Sar, anserine and carnosine, but not for glycine. We conclude that anserine and carnosine interact with the human intestinal peptide transporter and are transported by hPEPT1 in an active, electrogenic H(+) symport. As PEPT1 is the predominant transport system for di- and tripeptides at the intestinal epithelium, this transporter is most probably responsible for the intestinal absorption of anserine after food intake. In addition, anserine might be useful for the design of new substrates of peptide transporters, such as prodrugs, that can be administered orally." @default.
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• W1587467241 date "2010-01-08" @default.
• W1587467241 modified "2023-10-18" @default.
• W1587467241 title "The bioactive dipeptide anserine is transported by human proton-coupled peptide transporters" @default.
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• W1587467241 doi "https://doi.org/10.1111/j.1742-4658.2009.07528.x" @default.
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