| First Author | Böhmer C | Year | 2005 |
| Journal | Biochem J | Volume | 389 |
| Issue | Pt 3 | Pages | 745-51 |
| PubMed ID | 15804236 | Mgi Jnum | J:117499 |
| Mgi Id | MGI:3696616 | Doi | 10.1042/BJ20050083 |
| Citation | Bohmer C, et al. (2005) Characterization of mouse amino acid transporter B0AT1 (slc6a19). Biochem J 389(Pt 3):745-51 |
| abstractText | The mechanism of the mouse (m)B0AT1 (slc6a19) transporter was studied in detail using two electrode voltage-clamp techniques and tracer studies in the Xenopus oocyte expression system. All neutral amino acids induced inward currents at physiological potentials, but large neutral non-aromatic amino acids were the preferred substrates of mB0AT1. Substrates were transported with K0.5 values ranging from approx. 1 mM to approx. 10 mM. The transporter mediates Na+-amino acid co-transport with a stoichiometry of 1:1. No other ions were involved in the transport mechanism. An increase in the extracellular Na+ concentration reduced the K0.5 for leucine, and vice versa. Moreover, the K0.5 values and Vmax values of both substrates varied with the membrane potential. As a result, K0.5 and Vmax values are a complex function of the concentration of substrate and co-substrate and the membrane potential. A model is presented assuming random binding order and a positive charge associated with the ternary [Na+-substrate-transporter] complex, which is consistent with the experimental data. |
