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Titolo:
Characterization of bile acid transport mediated by multidrug resistance associated protein 2 and bile salt export pump
Autore:
Akita, H; Suzuki, H; Ito, K; Kinoshita, S; Sato, N; Takikawa, H; Sugiyama, Y;
Indirizzi:
Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyo Ku, Tokyo 1130033, Japan Univ Tokyo Tokyo Japan 1130033 ceut Sci, Bunkyo Ku, Tokyo 1130033, Japan Teikyo Univ, Sch Med, Dept Med, Itabashi Ku, Tokyo 1730003, Japan Teikyo Univ Tokyo Japan 1730003 t Med, Itabashi Ku, Tokyo 1730003, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
fascicolo: 1, volume: 1511, anno: 2001,
pagine: 7 - 16
SICI:
0005-2736(20010309)1511:1<7:COBATM>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPLETE SULFATION; BILIARY-SECRETION; RAT-LIVER; CHOLESTASIS; MRP; COTRANSPORTER; LOCALIZATION; GLUTATHIONE; EXCRETION; MEMBRANE;
Keywords:
multidrug resistance-associated protein; bile salt export pump; bile acid; canalicular membrane vesicle;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Suzuki, H Univ Tokyo, Grad Sch Pharmaceut Sci, Bunkyo Ku, 7-3-1 Hongo, Tokyo 1130033, Japan Univ Tokyo 7-3-1 Hongo Tokyo Japan 1130033 Tokyo 1130033, Japan
Citazione:
H. Akita et al., "Characterization of bile acid transport mediated by multidrug resistance associated protein 2 and bile salt export pump", BBA-BIOMEMB, 1511(1), 2001, pp. 7-16

Abstract

Biliary excretion of certain bile acids is mediated by multidrug resistance associated protein 2 (Mrp2) and the bile salt export pump (Bsep). In the present study, the transport properties of several bile acids were characterized in canalicular membrane vesicles (CMVs) isolated from Sprague-Dawley (SD) rats and Eisai hyperbilirubinemic rats (EHBR) whose Mrp2 function is hereditarily defective and in membrane vesicles isolated from Sf9 cells infected with recombinant baculovirus containing cDNAs encoding Mrp2 and Bsep. ATP-dependent uptake of [H-3]taurochenodeoxycholate sulfate (TCDC-S) (K-m=8.8 muM) and [H-3]taurolithocholate sulfate (TLC-S) (K-m=1.5 muM) was observed in CMVs from SD rats, but not from EHBR. In addition, ATP-dependent uptake of [H-3]TLC-S (K-m=3.9 M) and [H-3]taurocholate (TC) (K-m=7.5 muM) was also observed in Mrp2 and Bsep-expressing Sf9 membrane vesicles, respectively. TCDC-S and TLC-S inhibited the ATP-dependent TC uptake into CMVs from SDrats with IC50 values of 4.6 muM and 1.2 muM, respectively. In contrast, the corresponding values for Sf9 cells expressing Bsep were 59 and 62 muM, respectively, which were similar to those determined in CMVs from EHBR (68 and 33 muM, respectively). By co-expressing Mrp2 with Bsep in Sf9 cells, IC50 values for membrane vesicles from these cells shifted to values comparable with those in CMVs from SD rats (4.6 and 1.2 muM) Moreover, in membrane vesicles where both Mrp2 and Bsep are co-expressed, preincubation with the sulfated bile acids potentiated their inhibitory effect on Bsep-mediated TC transport. These results can be accounted for by assuming that the sulfatedbile acids trans-inhibit the Bsep-mediated transport of TC. (C) 2001 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 16/07/20 alle ore 05:41:31