The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1.

Transport of amino acid aryl amides by the intestinal H+/peptide symporter (PEPT1) was studied in Caco-2 cells and in Xenopus laevis oocytes expressing human PEPT1. Several amino acid amides were able to inhibit the uptake of [14C]glycylsarcosine in Caco-2 cells. Ala-4-nitroanilide (Ki = 0.08 mM), Phe-4-nitroanilide (Ki = 0.09 mM) and Ala-4-phenylanilide (Ki = 0.03 mM) were accepted as substrates with equal or higher affinity than natural Ala-Xaa dipeptides. Ala-anilide (Ki = 2.9 mM), Ala-7-amido-4-methylcoumarin (Ki = 0.2 mM), Ala-4-chloroanilide (Ki = 0.3 mM) and Ala-4-methylanilide (Ki = 0.3 mM) were also recognized by PEPT1 as substrates. In contrast, alanine, Ala-amide, Phe-amide, Ala-methyl ester, Ala-4-nitrobenzyl ester and Ala-methylamide were not recognized (Ki > 20 mM). In X. laevis oocytes, transport of Ala-4-nitroanilide, Ala-7-amido-4-methylcoumarin, Ala-4-methylanilide and Ala-anilide was associated with transfer of positive charge and the currents were saturable with respect to substrate concentration (K0.5 values: 0.1, 0.2, 0.8 and 3.1 mM, respectively). The currents induced by Ala-4-methylanilide were saturable with respect to the substrate concentration and influenced by the membrane potential. The affinity of the transporter for Ala-4-methylanilide was also found to be influenced by the membrane potential. We conclude that the intestinal H+/peptide cotransport system PEPT1 accepts amino acid aryl amides as substrates.[1]

References

  1. Transport of amino acid aryl amides by the intestinal H+/peptide cotransport system, PEPT1. Börner, V., Fei, Y.J., Hartrodt, B., Ganapathy, V., Leibach, F.H., Neubert, K., Brandsch, M. Eur. J. Biochem. (1998) [Pubmed]
 
WikiGenes - Universities