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Vol. 290, Issue 1, 289-294, July 1999
Graduate School of Pharmaceutical Sciences, The University of
Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan (J.-I.N., H.S., D.S., T.K., K.I.
and Y.S.); and College of Pharmacy, Nihon University, Narashino-Dai,
Funabashi, Chiba, Japan (M.H.)
Transport characteristics of 17
-estradiol
17-D-glucuronide (E217G), a dual
substrate of the transporters for cellular uptake (organic
anion-transporting polypeptide 1 or oatp1) and cellular excretion
(multidrug resistance-associated protein 1or MRP1), in the rat choroid
plexus were studied in vivo and in vitro. The uptake of
E217G into isolated choroid plexus was mediated by an
energy-dependent system with a Km of 3.4 µM. Together with the previous finding that oatp1 is localized on the
apical membrane of choroid plexus, these results suggest that oatp1 is
responsible for the uptake of this ligand. After
intracerebroventricular administration, elimination of
E217G from cerebrospinal fluid was probenecid sensitive
and much more rapid than that of inulin; less than 2% of the
administered E217G and 40 to 50% of inulin remained in the cerebrospinal fluid 20 min after intracerebroventricular
administration. In addition, the amount of E217G
associated with choroid plexus at 20 min was negligible, suggesting the
presence of an efficient excretion system on the basolateral membrane
of choroid plexus. Expression of MRP1 was detected in choroid plexus.
Semiquantitative reverse transcription-polymerase chain reaction and
Western blot analyses indicated that the expression level of MRP1 in
choroid plexus is about four or five times higher than that in the
lung, one of the tissues exhibiting high expression of MRP1. Together with the in vivo vectorial transport of E217G, these
results can be accounted for by assuming that there is basolateral
localization of MRP1 in choroid plexus. Combined, oatp1 and MRP1 may
synergistically mediate the efficient transcellular transport of
E217G across choroid plexus.
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