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.