Expression of a non-MDR2-coded liver phosphatidylcholine membrane transport protein in Xenopus laevis oocytes.

Phosphatidylcholines (PC) are secreted into the bile via a membrane transport protein(s). Recently, evidence for ATP-dependent mdr2-encoded PC transport as well as for carrier-mediated PC transport had been reported. Therefore, we investigated whether mdr2 P-glycoprotein is involved in the transport of a water-soluble short chain phosphatidylcholine analogue L-alpha-dibutyroyl-PC (diC4PC) induced by expression of liver mRNA in Xenopus laevis oocytes. Expression of mouse and rat mdr2 cRNA did not result in diC4PC net uptake in Xenopus laevis oocytes. By contrast oocytes showed a similar carrier-mediated uptake activity for diC4PC after injection of mouse, rat and human liver total mRNA (Km 7.7, 9.6, and 11.6 mM). Antisense inhibition of mdr2 mRNA expression increased diC4PC uptake induced by total liver mRNA from mouse and rat. The present data prove the existence of a specific mRNA for a non-mdr2-coded cell membrane PC carrier in mouse, rat, and human liver which exhibits similar transport affinity for diC4PC as the PC carrier in rat liver canalicular membranes.