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Titolo:
Na+-coupled transport of L-carnitine via high-affinity carnitine transporter OCTN2 and its subcellular localization in kidney
Autore:
Tamai, I; China, K; Sai, Y; Kobayashi, D; Nezu, J; Kawahara, E; Tsuji, A;
Indirizzi:
Kanazawa Univ, Fac Pharmaceut Sci, Kanazawa, Ishikawa 9200934, Japan Kanazawa Univ Kanazawa Ishikawa Japan 9200934 wa, Ishikawa 9200934, Japan Japan Sci & Technol Corp, CREST, Kanazawa, Ishikawa, Japan Japan Sci & Technol Corp Kanazawa Ishikawa Japan nazawa, Ishikawa, Japan Mol Med Inc, Chugai Res Inst, Ibaraki, Osaka 3004101, Japan Mol Med Inc Ibaraki Osaka Japan 3004101 st, Ibaraki, Osaka 3004101, Japan Kanazawa Univ, Fac Med, Kanazawa, Ishikawa 9200934, Japan Kanazawa Univ Kanazawa Ishikawa Japan 9200934 wa, Ishikawa 9200934, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
fascicolo: 2, volume: 1512, anno: 2001,
pagine: 273 - 284
SICI:
0005-2736(20010606)1512:2<273:NTOLVH>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ORGANIC CATION TRANSPORTER; PLASMA-MEMBRANE VESICLES; VISCERAL STEATOSIS MICE; DEPENDENT TRANSPORT; TISSUE DISTRIBUTION; MOLECULAR-CLONING; RAT-KIDNEY; DEFICIENCY; MUTATIONS; GENE;
Keywords:
membrane transport; carnitine; OCTN2; electrogenic transport; sodium dependent transport; membrane vesicle;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Tsuji, A Kanazawa Univ, Fac Pharmaceut Sci, 13-1 Takara Machi, Kanazawa, Ishikawa 9200934, Japan Kanazawa Univ 13-1 Takara Machi Kanazawa Ishikawa Japan 9200934 n
Citazione:
I. Tamai et al., "Na+-coupled transport of L-carnitine via high-affinity carnitine transporter OCTN2 and its subcellular localization in kidney", BBA-BIOMEMB, 1512(2), 2001, pp. 273-284

Abstract

The mechanism of Na+-dependent transport of L-carnitine via the carnitine/organic cation transporter OCTN2 and the subcellular localization of OCTN2 in kidney were studied. Using plasma membrane vesicles prepared from HEK293cells that were stably transfected with human OCTN2, transport of L-carnitine via human OCTN2 was characterized. Uptake of L-[H-3]carnitine by the OCTN2-expressing membrane vesicles was significantly increased in the presence of an inwardly directed Na+ gradient, with an overshoot, while such transient uphill transport was not observed in membrane vesicles from cells thatwere mock transfected with expression vector pcDNA3 alone. The uptake of L-[H-3]carnitine was specifically dependent on Na+ and the osmolarity effectshowed that Na+ significantly influenced the transport rather than the binding. Changes of inorganic anions in the extravesicular medium and of membrane potential by valinomycin altered the initial uptake activity of L-carnitine by OCTN2. In addition, the flues of L-carnitine and Na+ were coupled with 1:1 stoichiometry. Accordingly, it was clarified that Na+ is coupled with flux of L-carnitine and the flux is an electrogenic process. Furthermore, OCTN2 was localized on the apical membrane of renal tubular epithelial cells. These results clarified that OCTN2 is important for the concentrative reabsorption of L-carnitine after glomerular filtration in the kidney. (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 09/07/20 alle ore 01:06:29