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Titolo:
Cloning and characterization of a human brain Na+-independent transporter for small neutral amino acids that transports D-serine with high affinity
Autore:
Nakauchi, J; Matsuo, H; Kim, DK; Goto, A; Chairoungdua, A; Cha, SH; Inatomi, J; Shiokawa, Y; Yamaguchi, K; Saito, I; Endou, H; Kanai, Y;
Indirizzi:
Kyorin Univ, Sch Med, Dept Pharmacol & Toxicol, Tokyo 1818611, Japan Kyorin Univ Tokyo Japan 1818611 harmacol & Toxicol, Tokyo 1818611, Japan Kyorin Univ, Sch Med, Dept Neurosurg, Tokyo 1818611, Japan Kyorin Univ Tokyo Japan 1818611 ed, Dept Neurosurg, Tokyo 1818611, Japan Natl Def Med Coll, Dept Physiol 1, Tokorozawa, Saitama 3598513, Japan NatlDef Med Coll Tokorozawa Saitama Japan 3598513 Saitama 3598513, Japan Kyorin Univ, Sch Med, Dept Pathol, Tokyo 1818611, Japan Kyorin Univ Tokyo Japan 1818611 h Med, Dept Pathol, Tokyo 1818611, Japan Japan Sci & Technol Corp, PRESTO, Tokyo 1818611, Japan Japan Sci & TechnolCorp Tokyo Japan 1818611 RESTO, Tokyo 1818611, Japan
Titolo Testata:
NEUROSCIENCE LETTERS
fascicolo: 3, volume: 287, anno: 2000,
pagine: 231 - 235
SICI:
0304-3940(20000630)287:3<231:CACOAH>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOGENOUS D-SERINE; D-ASPARTATE; INSITU HYBRIDIZATION; NMDA RECEPTORS; RAT-BRAIN; SYSTEM; NEUROMODULATOR; GLYCOPROTEIN; RACEMASE; GLYCINE;
Keywords:
amino acid transporter; system asc; 4F2 heavy chain; D-serine; N-methyl-D-aspartate receptor; human chromosome 19; human;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Kanai, Y Kyorin Univ, Sch Med, Dept Pharmacol & Toxicol, 6-20-2 Shinkawa, Tokyo 1818611, Japan Kyorin Univ 6-20-2 Shinkawa Tokyo Japan 1818611 o 1818611, Japan
Citazione:
J. Nakauchi et al., "Cloning and characterization of a human brain Na+-independent transporter for small neutral amino acids that transports D-serine with high affinity", NEUROSCI L, 287(3), 2000, pp. 231-235

Abstract

We isolated a cDNA for the human homologue of system asc transporter Asc-1from human brain. The encoded protein designated as hAsc-1 (human Asc-1) exhibited 91 % sequence identity to mouse Asc-1. Consistent with mouse Asc-1, hAsc-1 required 4F2 heavy chain for its functional expression in Xenopus oocytes. hAsc-1 exhibited the properties of amino acid transport system ascwhich transports small neutral amino acids in a Na+-independent manner. hAsc-1 transported D-serine at high affinity with a K-m value of 22.8 mu M. In brain, 2.0 kb mRNA was highly expressed. hAsc-1 gene was mapped to human chromosome 19, region q12-q13.1. Because of the high-affinity transport with the K-m value close to the physiological concentration of D-serine, together with the high levels of expression in brain, hAsc-1 is proposed to playsignificant roles in the D-serine mobilization in brain. (C) 2000 ElsevierScience Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 14:14:35