Cloning and characterization of a human brain Na+-independent transporter for small neutral amino acids that transports D-serine with high affinity

Jun Nakauchi; Hirotaka Matsuo; Do Kyung Kim; Akiteru Goto; Arthit Chairoungdua; Seok Ho Cha; Jun Inatomi; Yoshiaki Shiokawa; Kazuyoshi Yamaguchi; Isamu Saito; Hitoshi Endou; Yoshikatsu Kanai

doi:10.1016/S0304-3940(00)01169-1

Cloning and characterization of a human brain Na⁺-independent transporter for small neutral amino acids that transports D-serine with high affinity

Jun Nakauchi
, Hirotaka Matsuo
, Do Kyung Kim
, Akiteru Goto
, Arthit Chairoungdua
, Seok Ho Cha
, Jun Inatomi
, Yoshiaki Shiokawa
, Kazuyoshi Yamaguchi
, Isamu Saito
, Hitoshi Endou
, Yoshikatsu Kanai

Research output: Contribution to journal › Article › peer-review

109 Citations (Scopus)

Abstract

We isolated a cDNA for the human homologue of system asc transporter Asc-1 from 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 asc which 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 μM. 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 play significant roles in the D-serine mobilization in brain. Copyright (C) 2000 Elsevier Science Ireland Ltd.

Original language	English
Pages (from-to)	231-235
Number of pages	5
Journal	Neuroscience Letters
Volume	287
Issue number	3
DOIs	https://doi.org/10.1016/S0304-3940(00)01169-1
Publication status	Published - 30-06-2000
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Neuroscience

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10.1016/S0304-3940(00)01169-1

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Nakauchi, J., Matsuo, H., Kim, D. K., Goto, A., Chairoungdua, A., Cha, S. H., Inatomi, J., Shiokawa, Y., Yamaguchi, K., Saito, I., Endou, H., & Kanai, Y. (2000). Cloning and characterization of a human brain Na⁺-independent transporter for small neutral amino acids that transports D-serine with high affinity. Neuroscience Letters, 287(3), 231-235. https://doi.org/10.1016/S0304-3940(00)01169-1

@article{b7535982c8824c2eac7fd352e17e86bb,

title = "Cloning and characterization of a human brain Na+-independent transporter for small neutral amino acids that transports D-serine with high affinity",

abstract = "We isolated a cDNA for the human homologue of system asc transporter Asc-1 from 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 asc which 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 μM. 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 play significant roles in the D-serine mobilization in brain. Copyright (C) 2000 Elsevier Science Ireland Ltd.",

keywords = "4F2 Heavy chain, Amino acid transporter, D-Serine, Human, Human chromosome 19, N-Methyl-D-aspartate receptor, System asc",

author = "Jun Nakauchi and Hirotaka Matsuo and Kim, \{Do Kyung\} and Akiteru Goto and Arthit Chairoungdua and Cha, \{Seok Ho\} and Jun Inatomi and Yoshiaki Shiokawa and Kazuyoshi Yamaguchi and Isamu Saito and Hitoshi Endou and Yoshikatsu Kanai",

year = "2000",

month = jun,

day = "30",

doi = "10.1016/S0304-3940(00)01169-1",

language = "English",

volume = "287",

pages = "231--235",

journal = "Neuroscience Letters",

issn = "0304-3940",

publisher = "Elsevier Ireland Ltd",

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Nakauchi, J, Matsuo, H, Kim, DK, Goto, A, Chairoungdua, A, Cha, SH, Inatomi, J, Shiokawa, Y, Yamaguchi, K, Saito, I, Endou, H & Kanai, Y 2000, 'Cloning and characterization of a human brain Na⁺-independent transporter for small neutral amino acids that transports D-serine with high affinity', Neuroscience Letters, vol. 287, no. 3, pp. 231-235. https://doi.org/10.1016/S0304-3940(00)01169-1

TY - JOUR

T1 - Cloning and characterization of a human brain Na+-independent transporter for small neutral amino acids that transports D-serine with high affinity

AU - Nakauchi, Jun

AU - Matsuo, Hirotaka

AU - Kim, Do Kyung

AU - Goto, Akiteru

AU - Chairoungdua, Arthit

AU - Cha, Seok Ho

AU - Inatomi, Jun

AU - Shiokawa, Yoshiaki

AU - Yamaguchi, Kazuyoshi

AU - Saito, Isamu

AU - Endou, Hitoshi

AU - Kanai, Yoshikatsu

PY - 2000/6/30

Y1 - 2000/6/30

N2 - We isolated a cDNA for the human homologue of system asc transporter Asc-1 from 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 asc which 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 μM. 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 play significant roles in the D-serine mobilization in brain. Copyright (C) 2000 Elsevier Science Ireland Ltd.

AB - We isolated a cDNA for the human homologue of system asc transporter Asc-1 from 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 asc which 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 μM. 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 play significant roles in the D-serine mobilization in brain. Copyright (C) 2000 Elsevier Science Ireland Ltd.

KW - 4F2 Heavy chain

KW - Amino acid transporter

KW - D-Serine

KW - Human

KW - Human chromosome 19

KW - N-Methyl-D-aspartate receptor

KW - System asc

UR - https://www.scopus.com/pages/publications/0034733978

UR - https://www.scopus.com/pages/publications/0034733978#tab=citedBy

U2 - 10.1016/S0304-3940(00)01169-1

DO - 10.1016/S0304-3940(00)01169-1

M3 - Article

C2 - 10863037

AN - SCOPUS:0034733978

SN - 0304-3940

VL - 287

SP - 231

EP - 235

JO - Neuroscience Letters

JF - Neuroscience Letters

IS - 3

ER -

Cloning and characterization of a human brain Na⁺-independent transporter for small neutral amino acids that transports D-serine with high affinity

Abstract

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