| First Author | van Helvoort A | Year | 1996 |
| Journal | Cell | Volume | 87 |
| Issue | 3 | Pages | 507-17 |
| PubMed ID | 8898203 | Mgi Jnum | J:235270 |
| Mgi Id | MGI:5795830 | Doi | 10.1016/s0092-8674(00)81370-7 |
| Citation | van Helvoort A, et al. (1996) MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87(3):507-17 |
| abstractText | The human MDR1 P-glycoprotein (Pgp) extrudes a variety of drugs across the plasma membrane. The homologous MDR3 Pgp is required for phosphatidylcholine secretion into bile. After stable transfection of epithelial LLC-PK1 cells, MDR1 and MDR3 Pgp were localized in the apical membrane. At 15 degrees C, newly synthesized short-chain analogs of various membrane lipids were recovered in the apical albumin-containing medium of MDR1 cells but not control cells. MDR inhibitors and energy depletion reduced apical release. MDR3 cells exclusively released a short-chain phosphatidylcholine. Since no vesicular secretion occurs at 15 degrees C, the short-chain lipids must have been translocated by the Pgps across the plasma membrane before extraction into the medium by the lipid-acceptor albumin. |
