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• W2809051650 abstract "Human OATP1B1 is highly expressed at the basolateral membrane of the hepatocyte. It plays an important role in the sodium-independent transport of bile acids and bile salts and contributes to the systemic clearance of many drugs. In this study, the interaction of at least one representative of all major chemical classes of bile acids and bile salts, which include the bile acid chenodeoxycholate (CDC), monovalent (amidated) bile salts glycochenodeoxycholate (GCDC), taurochenodeoxycholate (TCDC) and taurocholate (TC), a sulfated bile acid 3-sulfo-chenodeoxycholate (3S-CDC) and a divalent (amidated and sulfated) bile salt 3-sulfo-glycolithocholate (3S-GLC) were tested with OATP1B1 overexpressed in HEK293 cells. All bile acid derivatives except for CDC showed an efficient transport by OATP1B1. 3S-GLC gave the lowest KM (0.708 ± 0.125 μM) and 3S-CDC showed the highest Vmax value (158 ± 87.3 pmol/mg protein/min). The ranking of Clint values (3S-GLC > 3S-CDC > TCDC > GCDC > TC) also showed a preference for sulfated derivatives. In summary, human OATP1B1 transports sulfate esters of bile acids and bile salts more efficiently than monovalent bile salts." @default.
• W2809051650 created "2018-06-29" @default.
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• W2809051650 date "2018-10-01" @default.
• W2809051650 modified "2023-10-09" @default.
• W2809051650 title "Human OATP1B1 (SLCO1B1) transports sulfated bile acids and bile salts with particular efficiency" @default.
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• W2809051650 doi "https://doi.org/10.1016/j.tiv.2018.06.018" @default.
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