The human MDR3 P-glycoprotein promotes translocation of phosphatidylcholine through the plasma membrane of fibroblasts from transgenic mice
Autor: | Ben Roelofsen, Johanna L.P.M. Timmermans-Hereijgers, Piet Borst, Wim J. van Blitterswijk, Alexander J. Smith, Alfred H. Schinkel, Karel W. A. Wirtz, Jaap J.M. Smit |
---|---|
Rok vydání: | 1994 |
Předmět: |
Genetically modified mouse
Transgene Biophysics Mice Transgenic Vimentin P-glycoprotein Biochemistry Choline Mice chemistry.chemical_compound Structural Biology Phosphatidylcholine Genetics Animals Secretion ATP Binding Cassette Transporter Subfamily B Member 1 Carbon Radioisotopes Promoter Regions Genetic Molecular Biology biology Cell Membrane Wild type Biological Transport Cell Biology Flippase Fibroblasts Molecular biology Kinetics chemistry Liposomes Phosphatidylcholines MDR3 biology.protein |
Zdroj: | FEBS Letters. 354:263-266 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(94)01135-4 |
Popis: | The mouse mdr2 P-glycoprotein (P-gp) and its human MDR3 homologue are present in high concentrations in the canalicular membrane of hepatocytes. Mice lacking this protein are unable to secrete phosphatidylcholine (PC) into bile, suggesting that this P-gp is a PC translocator. We have tested this in fibroblasts from transgenic mice expressing the MDR3 gene under a vimentin promoter. Transgenic and control fibroblasts were incubated with [14C]choline to label PC. When the labeled cells were incubated with a PC transfer protein and acceptor liposomes, transfer of radioactive PC was enhanced in transgenic cells relative to the wild type controls. We conclude that the MDR3 P-glycoprotein is able to promote the transfer of PC from the inner to the outer leaflet of the plasma membrane, supporting the idea that this protein functions as a PC flippase. |
Databáze: | OpenAIRE |
Externí odkaz: |