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. 2020 Apr 24;12(4):390. doi: 10.3390/pharmaceutics12040390

Table 1.

Kinetic parameters associated with the uptake of p-aminohippuric acid and acamprosate, substrates for OAT1, and of estrone-3-sulfate, a substrate for OAT3, in HEK293-Flp-In OAT1 and OAT3 cells, respectively. Data are reported as mean ± SEM of replicates in three cell passages obtained in 1 Lab. 1 or 2 Lab. 2.

Substrate p-Aminohippuric Acid 2 Acamprosate 1 Estrone-3-Sulfate 2
Carrier OAT1 OAT1 OAT3
Km (µM) 43 ± 13 698 ± 192 26 ± 6
Vmax (pmol∙mg protein−1∙min−1) 429 ± 39 1028 ± 99
Vmax (fmol∙cm−2∙min−1) 8.8 ± 0.7
CLT (cm/min) 5.6 × 10−9
CLT (µL∙mg protein−1∙min−1) 10 1.5
P (µL∙mg protein−1∙min−1) 0.35 ± 0.04

Vmax is the OAT1-mediated maximal uptake rate, Km is the Michaelis constant (calculated only from the saturable uptake component); CLT is the carrier-mediated clearance (Vmax/Km); P is the contribution of passive diffusion and potential effects from isotope dilution or non-specific cell binding.