Primary structure, functional characteristics and tissue expression pattern of human ATA2, a subtype of aminoacid transport system A

被引：129

作者：

Hatanaka, T

Huang, W

Wang, HP

Sugawara, M

Prasad, PD

Leibach, FH

Ganapathy, V ^{[1
]}

机构：

[1] Med Coll Georgia, Dept Biochem & Mol Biol, Augusta, GA 30912 USA

[2] Med Coll Georgia, Dept Obstet & Gynecol, Augusta, GA 30912 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2000年 / 1467卷 / 01期

关键词：

amino acid transport; system A; primary structure; stoichiometry; substrate specificity; human;

D O I：

10.1016/S0005-2736(00)00252-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We report here on the primary structure and functional characteristics of the protein responsible for the system A amino acid transport activity that is known to be expressed in most human tissues. This transporter, designated ATA? for amino acid transporter A2, was cloned from the human hepatoma cell line HepG2. Human ATA2 (hATA2) consists of 506 amino acids and exhibits a high degree of homology to rat ATA2. hATA2-specific mRNA is ubiquitously expressed in human tissues. When expressed in mammalian cells, hATA2 mediates Na+-dependent transport of alpha-(methylamino)isobutyric acid, a specific model substrate for system A. The transporter is specific for neutral amino acids. It is pH-sensitive and Li+-intolerant. The Na+-amino acid stoichiometry is 1:1. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：1 / 6

页数：6

共 18 条

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