PubMed:1360010 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":188},"obj":"Sentence"},{"id":"T3","span":{"begin":189,"end":525},"obj":"Sentence"},{"id":"T4","span":{"begin":526,"end":717},"obj":"Sentence"},{"id":"T5","span":{"begin":718,"end":814},"obj":"Sentence"},{"id":"T6","span":{"begin":815,"end":1053},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":188},"obj":"Sentence"},{"id":"T3","span":{"begin":189,"end":525},"obj":"Sentence"},{"id":"T4","span":{"begin":526,"end":717},"obj":"Sentence"},{"id":"T5","span":{"begin":718,"end":814},"obj":"Sentence"},{"id":"T6","span":{"begin":815,"end":1053},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"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 P-glycoprotein."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":149,"end":162},"obj":"http://purl.obolibrary.org/obo/MAT_0000071"},{"id":"T2","span":{"begin":157,"end":162},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"},{"id":"T3","span":{"begin":306,"end":312},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"T4","span":{"begin":413,"end":419},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"T5","span":{"begin":928,"end":942},"obj":"http://purl.obolibrary.org/obo/MAT_0000494"}],"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 P-glycoprotein."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":149,"end":162},"obj":"Body_part"},{"id":"T2","span":{"begin":306,"end":312},"obj":"Body_part"},{"id":"T3","span":{"begin":413,"end":419},"obj":"Body_part"},{"id":"T4","span":{"begin":928,"end":942},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000071"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000484"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000494"}],"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 P-glycoprotein."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":5},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":109,"end":114},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":143,"end":148},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":265,"end":270},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":622,"end":627},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":922,"end":927},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9606"}],"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 P-glycoprotein."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":149,"end":162},"obj":"Body_part"},{"id":"T2","span":{"begin":198,"end":218},"obj":"Body_part"},{"id":"T3","span":{"begin":928,"end":942},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002369"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0010137"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001235"}],"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 P-glycoprotein."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":404,"end":409},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0002324"}],"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 P-glycoprotein."}