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Titolo:
Multidrug resistance protein Mrp2 mediates ATP-dependent transport of classic renal organic anion p-aminohippurate
Autore:
Van Aubel, RAMH; Peters, JGP; Masereeuw, R; Van Os, CH; Russel, FGM;
Indirizzi:
Univ Nijmegen, Fac Med Sci, Dept Pharmacol & Toxicol 233, Med Ctr, NL-6500HB Nijmegen, Netherlands Univ Nijmegen Nijmegen Netherlands NL-6500 HB 00HB Nijmegen, Netherlands Univ Nijmegen, Fac Med Sci, Dept Cell Physiol, Med Ctr, NL-6500 HB Nijmegen, Netherlands Univ Nijmegen Nijmegen Netherlands NL-6500 HB 0 HB Nijmegen, Netherlands
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY
fascicolo: 4, volume: 279, anno: 2000,
pagine: F713 - F717
SICI:
0363-6127(200010)279:4<F713:MRPMMA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
KIDNEY PROXIMAL TUBULES; CONJUGATE EXPORT PUMP; MEMBRANE-VESICLES; INSECT CELLS; LOCALIZATION; EXPRESSION; SYSTEM; GENE;
Keywords:
proximal tubule; kidney; p-aminohippurate organic anion transport; 2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Russel, FGM Univ Nijmegen, Fac Med Sci, Dept Pharmacol & Toxicol 233, Med Ctr, POB 9101, NL-6500 HB Nijmegen, Netherlands Univ Nijmegen POB 9101 Nijmegen Netherlands NL-6500 HB rlands
Citazione:
R.A.M.H. Van Aubel et al., "Multidrug resistance protein Mrp2 mediates ATP-dependent transport of classic renal organic anion p-aminohippurate", AM J P-REN, 279(4), 2000, pp. F713-F717

Abstract

p-Aminohippurate (PAH) is widely used as a model substrate to characterizeorganic anion transport in kidney proximal tubules. The carrier responsible for uptake of PAH across the basolateral membrane has been cloned and well characterized, whereas transporters mediating PAH excretion across the brush-border (apical) membrane are yet unknown. In this study we investigatedwhether PAH is a substrate for the apical multidrug resistance protein 2 (Mrp2). Overexpression of recombinant rabbit Mrp2 in Sf9 cells significantlyincreased ATP-dependent [C-14]PAH uptake into isolated membrane vesicles compared with endogenous ATP-dependent uptake. The Michaelis-Menten constantand maximal velocity for Mrp2-mediated ATP-dependent [C-14]PAH transport were 1.9 +/- 0.8 mM and 187 +/- 29 pmol.mg(-1).min(-1), respectively. On thebasis of the inhibitory profile, the endogenous ATP-dependent PAH transporter does not appear to be an ortholog of Mrp2. Together, our results show that Mrp2 is a low-affinity ATP-dependent PAH transporter, indicating that Mrp2 might contribute to urinary PAH excretion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 14:50:11