Literature DB >> 17103337

Characterization of the uptake mechanism for a novel loop diuretic, M17055, in Caco-2 cells: involvement of organic anion transporting polypeptide (OATP)-B.

Tomohiro Nishimura1, Yoshiyuki Kubo, Yukio Kato, Yoshimichi Sai, Takuo Ogihara, Akira Tsuji.   

Abstract

PURPOSE: M17055 is under development as a novel loop diuretic for oral administration. To investigate the molecular mechanism of its gastrointestinal absorption, we initially aimed to clarify the mechanism of uptake of M17055 by Caco-2 cells, focusing on possible involvement of OATP-B (SLCO2B1), which is localized in the apical membranes of human intestinal epithelial cells.
MATERIALS AND METHODS: The uptake of [14C]M17055 by Caco-2 cells cultured on multi-well dishes was measured after cultivation for 14 days. Uptake of [14C]M17055 by HEK293 cells stably expressing OATP-B (HEK293/OATP-B cells) was also examined.
RESULTS: M17055 uptake by Caco-2 cells was saturable, and was inhibited by various organic anions, including other loop diuretics, and several bile acids. Uptake of M17055 by HEK293/OATP-B cells was much higher than that by mock cells. The inhibitory profiles of various organic anions and the estimated Km values for M17055 uptake were similar in Caco-2 and HEK293/OATP-B cells. Moreover, the values of inhibition constants of several inhibitors for M17055 uptake were comparable in the two cell lines.
CONCLUSION: Our data suggest that OATP-B plays a major role in the uptake of the novel loop diuretic M17055 from apical membranes in Caco-2 cells.

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Year:  2006        PMID: 17103337     DOI: 10.1007/s11095-006-9127-x

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.580


  35 in total

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Authors:  I J Hidalgo; R T Borchardt
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3.  Absorption of montelukast is transporter mediated: a common variant of OATP2B1 is associated with reduced plasma concentrations and poor response.

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