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J. Biol. Chem., Vol. 275, Issue 22, 16473-16477, June 2, 2000
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From the Departments of We report here on the cloning and functional
characterization of the protein responsible for the system A amino acid
transport activity that is known to be expressed in most mammalian
tissues. This transporter, designated ATA2 for amino acid transporter
A2, was cloned from rat skeletal muscle. It is distinct from the
neuron-specific glutamine transporter (GlnT/ATA1). Rat ATA2 consists of
504 amino acids and bears significant homology to GlnT/ATA1 and system
N (SN1). ATA2-specific mRNA is ubiquitously expressed in rat
tissues. When expressed in mammalian cells, ATA2 mediates
Na+-dependent transport of
Cloning of an Amino Acid Transporter with Functional
Characteristics and Tissue Expression Pattern Identical to That of
System A*
,,,,, and¶
Biochemistry and Molecular
Biology and § Medicine, Medical College of Georgia,
Augusta, Georgia 30912
-(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. When expressed in Xenopus laevis oocytes, transport of neutral amino acids via ATA2 is associated with
inward currents. The substrate-induced current is
Na+-dependent and pH-sensitive. The amino acid
transport system A is particularly known for its adaptive and hormonal
regulation, and therefore the successful cloning of the protein
responsible for this transport activity represents a significant step
toward understanding the function and expression of this transporter in
various physiological and pathological states.
*
This work was supported by National Institutes of Health
Grants DA10045 and HD33347.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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