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Titolo:
Molecular mechanisms of organic cation transport in OCT2-expressing Xenopus oocytes
Autore:
Okuda, M; Urakami, Y; Saito, H; Inui, K;
Indirizzi:
Kyotoapanv, Fac Med, Kyoto Univ Hosp, Dept Pharm,Sakyo Ku, Kyoto 6068507, J Kyoto Univ Kyoto Japan 6068507 sp, Dept Pharm,Sakyo Ku, Kyoto 6068507, J
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
fascicolo: 2, volume: 1417, anno: 1999,
pagine: 224 - 231
SICI:
0005-2736(19990304)1417:2<224:MMOOCT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPITHELIAL-CELL LINE; RENAL BRUSH-BORDER; BASOLATERAL MEMBRANE-VESICLES; GRADIENT-DEPENDENT TRANSPORT; CARRIER-MEDIATED TRANSPORT; FUNCTIONAL EXPRESSION; KIDNEY; TETRAETHYLAMMONIUM; LLC-PK1; PH;
Keywords:
organic cation transporter; OCT1; OCT2; renal tubular secretion; (Xenopus oocyte);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Inui, K Kyotoapanv, Fac Med, Kyoto Univ Hosp, Dept Pharm,Sakyo Ku, Kyoto 6068507, J Kyoto Univ Kyoto Japan 6068507 Pharm,Sakyo Ku, Kyoto 6068507, J
Citazione:
M. Okuda et al., "Molecular mechanisms of organic cation transport in OCT2-expressing Xenopus oocytes", BBA-BIOMEMB, 1417(2), 1999, pp. 224-231

Abstract

The molecular mechanisms of organic cation transport by rat OCT2 was examined in the Xenopus oocyte expression system. When extracellular Na+ ions were replaced with K+ ions, uptake of tetraethylammonium (TEA) by OCT2-expressing oocytes was decreased, suggesting that TEA uptake by OCT2 is dependenton membrane potential. Kinetic analysis revealed that the decreased TEA uptake by ion substitution was caused at least in part by decreased substrateaffinity. Acidification of extracellular buffer resulted in decreased uptake of TEA, whereas TEA efflux from OCT1- and OCT2-expressing oocytes was not stimulated by inward proton gradient, in consistent with basolateral organic cation transport in the kidney. Inhibition of TEA uptake by various organic cations revealed that apparent substrate spectrum of OCT2 was similar with that of OCT1. However. the affinity of procainamide to OCT1 was higherthan that to OCT2. Uptake of 1-methyl-4-phenylpyridinium was stimulated byOCT2 as well as OCT1. but uptake of levofloxacin. a zwitterion, was not stimulated by both OCTs. These results suggest that OCT2 is a multispecific organic cation transporter with the characteristics comparable to those of the basolateral organic cation transporter in the kidney. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 12:08:02