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

Takahiro Hatanaka; Wei Huang; Haiping Wang; Mitsuru Sugawara; Puttur D. Prasad; Frederick H. Leibach; Vadivel Ganapathy

doi:10.1016/S0005-2736(00)00252-2

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

Takahiro Hatanaka, Wei Huang, Haiping Wang, Mitsuru Sugawara, Puttur D. Prasad, Frederick H. Leibach, Vadivel Ganapathy

Biochemistry and Molecular Biology

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

136 Scopus citations

Abstract

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 ATA2 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 α-(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.

Original language	English (US)
Pages (from-to)	1-6
Number of pages	6
Journal	Biochimica et Biophysica Acta - Biomembranes
Volume	1467
Issue number	1
DOIs	https://doi.org/10.1016/S0005-2736(00)00252-2
State	Published - Jul 31 2000

Keywords

Amino acid transport
Human
Primary structure
Stoichiometry
Substrate specificity
System A

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

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10.1016/S0005-2736(00)00252-2

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title = "Primary structure, functional characteristics and tissue expression pattern of human ATA2, a subtype of amino acid transport system A",

abstract = "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 ATA2 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 α-(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.",

keywords = "Amino acid transport, Human, Primary structure, Stoichiometry, Substrate specificity, System A",

author = "Takahiro Hatanaka and Wei Huang and Haiping Wang and Mitsuru Sugawara and Prasad, {Puttur D.} and Leibach, {Frederick H.} and Vadivel Ganapathy",

note = "Funding Information: This work was supported by National Institutes of Health Grants DA10045 and HD33347.",

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T1 - Primary structure, functional characteristics and tissue expression pattern of human ATA2, a subtype of amino acid transport system A

AU - Hatanaka, Takahiro

AU - Huang, Wei

AU - Wang, Haiping

AU - Sugawara, Mitsuru

AU - Prasad, Puttur D.

AU - Leibach, Frederick H.

AU - Ganapathy, Vadivel

N1 - Funding Information: This work was supported by National Institutes of Health Grants DA10045 and HD33347.

PY - 2000/7/31

Y1 - 2000/7/31

N2 - 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 ATA2 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 α-(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.

AB - 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 ATA2 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 α-(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.

KW - Amino acid transport

KW - Human

KW - Primary structure

KW - Stoichiometry

KW - Substrate specificity

KW - System A

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

Abstract

Keywords

ASJC Scopus subject areas

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