High affinity D- and L-serine transporter Asc-1: cloning and dendritic localization in the rat cerebral and cerebellar cortices

被引：54

作者：

Matsuo, H

Kanai, Y

Tokunaga, M

Nakata, T

Chairoungdua, A

Ishimine, H

Tsukada, S

Ooigawa, H

Nawashiro, H

Kobayashi, Y

Fukuda, J

Endou, H

机构：

[1] Kyorin Univ, Sch Med, Dept Pharmacol & Toxicol, Mitaka, Tokyo 1818611, Japan

[2] Natl Def Med Coll, Dept Phys 1, Tokorozawa, Saitama 3598513, Japan

[3] Japan Sci & Technol Corp, PRESTO, Mitaka, Tokyo 1818611, Japan

[4] Natl Def Med Coll, Dept Anat 2, Tokorozawa, Saitama 3598513, Japan

[5] Natl Def Med Coll, Dept Neurosurg, Tokorozawa, Saitama 3598513, Japan

来源：

NEUROSCIENCE LETTERS | 2004年 / 358卷 / 02期

基金：

日本学术振兴会;

关键词：

amino acid transporter; system asc; Asc-1; D-serine; L-serine; N-methyl-D-aspartate receptor; 3-phosphoglycerate dehydrogenase; rat;

D O I：

10.1016/j.neulet.2004.01.014

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

System asc transporter Asc-1, expressed in the brain, transports D- and L-serine with high affinity. To determine the localization of Asc-1 in the rat brain, we isolated a cDNA for the rat orthologue of Asc-1. The encoded protein designated as rAsc-1 (rat Asc-1) exhibited 98% sequence identity to mouse Asc-1 (mAsc-1). Based on amino acid sequences of rAsc-1 and mAsc-1, twopolyclonal antibodies against Asc-1 were generated and used for the immunohistochemical analysis on the cerebral and cerebellar cortices of rats and mice. Asc-1 immunoreactivity was detected in neurons, including cerebellar Purkinje neurons and pyramidal neurons in the neocortex and hippocampus. It was clearly localized in dendrites as well as somata. The localization of Asc-1 in brain suggests the significant contribution of Asc-1 to amino acid mobilization in brains including the synaptic clearance of D-serine and the neuronal uptake of L-serine that is essential for survival and dendrite growth of Purkinje neurons in particular. (C) 2004 Elsevier Ireland Ltd. All rights reserved.

引用

页码：123 / 126

页数：4

共 17 条

[1] Identification and characterization of a novel member of the heterodimeric amino acid transporter family presumed to be associated with an unknown heavy chain [J].