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Vol. 27, Issue 8, 866-871, August 1999
Division of Clinical Pharmacology, Departments of Medicine and
Pharmacology, Vanderbilt University School of Medicine, Nashville,
Tennessee
Fexofenadine, a nonsedating antihistamine, does not undergo
significant metabolic biotransformation. Accordingly, it was
hypothesized that uptake and efflux transporters could be importantly
involved in the drug's disposition. Utilizing a recombinant vaccinia
expression system, members of the organic anion transporting
polypeptide family, such as the human organic anion transporting
polypeptide (OATP) and rat organic anion transporting polypeptides 1 and 2 (Oatp1 and Oatp2), were found to mediate
[14C]fexofenadine cellular uptake. On the other hand, the
bile acid transporter human sodium taurocholate cotransporting
polypeptide (NTCP) and the rat organic cation transporter rOCT1
did not exhibit such activity. P-glycoprotein (P-gp) was identified as
a fexofenadine efflux transporter, using the LLC-PK1 cell, a polarized
epithelial cell line lacking P-gp, and the derivative cell line
(L-MDR1), which overexpresses P-gp. In addition, oral and i.v.
administration of [14C]fexofenadine to mice lacking
mdr1a-encoded P-gp resulted in 5- and 9-fold increases
in the drug's plasma and brain levels, respectively, compared with
wild-type mice. Also, a number of drug inhibitors of P-gp were found to
be effective inhibitors of OATP. Because OATP transporters and P-gp
colocalize in organs of importance to drug disposition such as the
liver, their activity provides an explanation for the heretofore
unknown mechanism(s) responsible for fexofenadine's disposition and
suggests potentially similar roles in the disposition of other xenobiotics.
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