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Titolo:
Comparison of "type I" and "type II" organic cation transport by organic cation transporters and organic anion-transporting polypeptides
Autore:
Van Montfoort, JE; Muller, M; Groothuis, GMM; Meijer, DKF; Koepsell, H; Meier, PJ;
Indirizzi:
Univ Zurich Hosp, Dept Med, Div Clin Pharmacol & Toxicol, CH-8091 Zurich, Switzerland Univ Zurich Hosp Zurich Switzerland CH-8091 CH-8091 Zurich, Switzerland Univ Groningen, Inst Drug Explorat, Dept Pharmacokinet & Drug Delivery, Groningen, Netherlands Univ Groningen Groningen Netherlands g Delivery, Groningen, Netherlands Univ Wageningen & Res Ctr, Subdept Human Nutr & Epidemiol, Nutr Metab & Genom Grp, Wageningen, Netherlands Univ Wageningen & Res Ctr Wageningen Netherlands ageningen, Netherlands Univ Wurzburg, Dept Anat, D-8700 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-8700 ept Anat, D-8700 Wurzburg, Germany
Titolo Testata:
JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
fascicolo: 1, volume: 298, anno: 2001,
pagine: 110 - 115
SICI:
0022-3565(200107)298:1<110:CO"IA">2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA-MEMBRANE VESICLES; HEPATIC-UPTAKE; RAT-LIVER; BILIARY-EXCRETION; UPTAKE SYSTEMS; MECHANISMS; DRUGS; TRIBUTYLMETHYLAMMONIUM; LOCALIZATION; HEPATOCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Meier, PJ Univ Zurich Hosp, Dept Med, Div Clin Pharmacol & Toxicol, CH-8091 Zurich, Switzerland Univ Zurich Hosp Zurich Switzerland CH-8091 urich, Switzerland
Citazione:
J.E. Van Montfoort et al., "Comparison of "type I" and "type II" organic cation transport by organic cation transporters and organic anion-transporting polypeptides", J PHARM EXP, 298(1), 2001, pp. 110-115

Abstract

Previous inhibition studies with taurocholate and cardiac glycosides suggested the presence of separate uptake systems for small "type I" (system1) and for bulky "type II" (system2) organic cations in rat hepatocytes. To identify the transport systems involved in type I and type II organic cation uptake, we compared the organic cation transport properties of the rat and human organic cation transporter 1 (rOCT1; hOCT1) and of the organic anion-transporting polypeptides 2 and A (rat Oatp2; human OATP-A) in cRNA-injectedXenopus laevis oocytes. Based on characteristic cis-inhibition patterns ofrOCT1-mediated tributylmethylammonium and Oatp2-mediated rocuronium uptake, rOCT1 and Oatp2 could be identified as the organic cation uptake systems1and 2, respectively, in rat liver. While hOCT1 exhibited similar transportproperties as rOCT1, OATP-A- but not Oatp2-mediated rocuronium uptake was inhibited by the OATP-A substrate N-methyl-quinidine, The latter substrate was also transported by rOCT1 and hOCT1, demonstrating distinct organic cation transport activities for rOCT1 and Oatp2 and overlapping organic cationtransport activities for hOCT1 and OATP-A. Finally, the data demonstrate that unmethylated quinidine is transported by rOCT1, hOCT1, and OATP-A at pH6.0, but not at pH 7.5, indicating that quinidine requires a positive charge for carrier-mediated uptake into hepatocytes, In conclusion, the studiesdemonstrate that in rat liver the suggested organic cation uptake systems1and 2 correspond to rOCT1 and Oatp2, respectively. However, the rat-based type I and II organic cation transporter classification cannot be extended without modification from rat to human.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 14:32:45