PubMed:1360010 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/1360010","sourcedb":"PubMed","sourceid":"1360010","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/1360010","text":"Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone.\nWe expressed human MDR1 cDNA isolated from the human adrenal gland in porcine LLC-PK1 cells. A highly polarized epithelium formed by LLC-GA5-COL300 cells that expressed human P-glycoprotein specifically on the apical surface showed a multidrug-resistant phenotype and had 8.3-, 3.4-, and 6.5-fold higher net basal to apical transport of 3H-labeled cortisol, aldosterone, and dexamethasone, respectively, compared with host cells. But progesterone was not transported, although it inhibited azidopine photoaffinity labeling of human P-glycoprotein and increased the sensitivity of multidrug-resistant cells to vinblastine. An excess of progesterone inhibited the transepithelial transport of cortisol by P-glycoprotein. These results suggest that cortisol and aldosterone are physiological substrates for P-glycoprotein in the human adrenal cortex and that substances that efficiently bind to P-glycoprotein are not necessarily transported by 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