Sodium-dependent homo- and hetero-exchange of neutral amino acids mediated by the amino acid transporter ATB degree.
We have investigated the functional characteristics of the human amino acid transporter ATB degree using the Xenopus laevis oocyte expression system. When expressed in oocytes, ATB degree mediates the uptake of neutral amino acids in an Na(+)-dependent manner. In addition, this transporter is able to mediate the efflux of intracellular neutral amino acids in exchange with extracellular neutral amino acids. This homo- and hetero-exchange of amino acids is absolutely Na(+)-dependent and conforms strictly to the substrate specificity of ATB degree. Kinetic analysis indicates that the affinity of ATB degree for a given amino acid substrate is similar whether ATB degree catalyzes the influx of the amino acid or the amino acid-induced efflux of intracellular amino acids. These results demonstrate for the first time the ability of ATB degree to function as a homo- and hetero-exchanger for its substrates.
Torres-Zamorano
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V
Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912-2100, USA.
Leibach
F H
FH
Ganapathy
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V
D026905:Amino Acid Transport Systems; D026923:Amino Acid Transport Systems, Basic; D026921:Amino Acid Transport Systems, Neutral; D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D012964:Sodium / Q000378:metabolism*; D013379:Substrate Specificity; D014982:Xenopus laevis
D026905:Amino Acid Transport Systems; D026923:Amino Acid Transport Systems, Basic; D026921:Amino Acid Transport Systems, Neutral; D000596:Amino Acids; D002352:Carrier Proteins; C489857:SLC3A1 protein, human; D012964:Sodium