Hepatic sinusoidal membrane transport of anionic drugs mediated by anion transporter Npt1

J Pharmacol Exp Ther. 1998 Sep;286(3):1391-6.

Abstract

The purpose of our study was to establish the localization of the anion transporter Npt1 in liver and the relevance of Npt1 to carrier-mediated hepatic transport of beta-lactam antibiotics. Immunocytochemical examination of mouse liver with antiserum for Npt1 showed basolateral (sinusoidal) membrane localization. Function of Npt1 was characterized in Xenopus laevis oocytes. Injection of in vitro-transcribed cRNA into oocytes resulted in an increased uptake of [14C]benzylpenicillin (PCG). The Npt1-mediated uptake was saturable with a Michaelis constant (Km) of 0.46 +/- 0.18 mM and a maximum rate (Vmax) of 46.6 +/- 8.5 pmol/60 min/oocyte, and the uptake of [14C]PCG was independent of Na+ and pH, but dependent on chloride ion. Npt1-mediated [14C]PCG uptake was inhibited by several beta-lactam antibiotics and probenecid. Oocytes injected with Npt1-cRNA demonstrated significantly enhanced transport activity for other anionic compounds such as [14C]faropenem, [14C]foscarnet and [3H]mevalonic acid, as well as [14C]PCG, compared with water-injected oocytes. In conclusion, Npt1 is suggested to participate in hepatic sinusoidal membrane transport of organic anions such as beta-lactam antibiotics as well as inorganic anions for the efflux from hepatocyte-to-blood direction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anion Transport Proteins
  • Anti-Bacterial Agents / pharmacokinetics*
  • Biological Transport
  • Carrier Proteins / analysis
  • Carrier Proteins / physiology*
  • Chlorides / pharmacology
  • Dose-Response Relationship, Drug
  • Hydrogen-Ion Concentration
  • Liver / metabolism*
  • Mice
  • Penicillin G / pharmacokinetics
  • Xenopus laevis

Substances

  • Anion Transport Proteins
  • Anti-Bacterial Agents
  • Carrier Proteins
  • Chlorides
  • Penicillin G