Abstract
The expression and functionality of
P-glycoprotein (P-gp) was assessed in Calu-3 cell monolayers cultured at an air-liquid interface. Net secretory transport of the established P-glycoprotein substrate 3H-digoxin was abolished at 4°C but was only marginally affected by the metabolic inhibitor sodium azide and unaffected by the specific P-gp antibody inhibitor UIC2. Results suggest that P-gp does not play a major role in the trafficking of 3H-digoxin in Calu-3 cells.
P-glycoprotein (P-gp) was assessed in Calu-3 cell monolayers cultured at an air-liquid interface. Net secretory transport of the established P-glycoprotein substrate 3H-digoxin was abolished at 4°C but was only marginally affected by the metabolic inhibitor sodium azide and unaffected by the specific P-gp antibody inhibitor UIC2. Results suggest that P-gp does not play a major role in the trafficking of 3H-digoxin in Calu-3 cells.
Original language | English |
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Publication status | Published - 2011 |
Event | UKPharmSci 2011 - Nottingham, United Kingdom Duration: 31 Aug 2011 → 2 Sept 2011 |
Conference
Conference | UKPharmSci 2011 |
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Country/Territory | United Kingdom |
City | Nottingham |
Period | 31/08/11 → 2/09/11 |