Abstract
Rat bile phosphatidylcholine was structurally characterized and quantified by electrospray mass spectrometry using a triple quadrupole instrument. All results were obtained by direct analysis of an unprocessed total lipid extract from rat bile. Structural characterization of phosphatidylcholine was achieved by collision-induced dissociation of [M + Cl]−ions observed in the negative-ion electrospray mass spectrum. Quantification of phosphatidylcholine was performed in the positive-ion mode using precursor ion scanning ofm/z184 and dimyristoyl-phosphatidylcholine as internal standard. Using this new methodology, the effect of cyclosporin A on biliary phosphatidylcholine excretion in the rat was investigated. After intravenous administration of cyclosporin A (25 mg/kg body wt) the phosphatidylcholine level in bile was reduced to about 30% of the control level. This suggests an inhibition by cyclosporin A of the translocation of phosphatidylcholine across the hepatocyte canalicular membrane which is mediated by the Mdr2 P-glycoprotein.
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