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The values shown in italics represent measured apparent K_t values for the transport of the indicated substrate, rather than the IC_fifty values.

The set of substrates used in the current study did not include the fluorescent OC, 4-(4-dimethylamino)styryl)-N-methylpyridinium (ASP), which has been used as a test substrate to assess selectivity of both ). In the study of MATE1 selectivity, Wittwer et al. (2013) screened 900+ compounds for inhibition of MATE1-mediated ASP transport and noted, as discussed subsequently in the present study, that cationic charge nimet Espanjan dating site and hydrophobicity were positively correlated with inhibition of MATE1 activity. Eighty-six compounds in the set of ligands used in the current study were included in the Wittwer report and Supplemental Fig. 3A compares the degree of inhibition of MPP transport reported here with the inhibition of ASP transport reported in that study. There was a clear correlation between the inhibitions produced by this common set of ligands. Although it appeared that, in general, there was a greater degree of inhibition of MPP transport than of ASP transport (particularly evident for the higher affinity inhibitors distributed toward the left side in Supplemental Fig. 3A), this probably reflected the use of a 50 µM screening concentration in our study compared with a 20 µM screening concentration in the study by Wittwer et al. (2013). For five compounds, Supplemental Fig. 3B compares the IC₅₀ values for inhibition of MPP or metformin transport that we determined to the values obtained by Wittwer et al. (2013) for inhibition of ASP transport. Within the limits of resolution provided by this small sample, there was little evidence for a systematic variation in IC₅₀ values obtained for the two substrates. (more…)