Sodium-dependent homo- and hetero-exchange of neutral amino acids mediated by the amino acid transporter ATB degree.
Sodium-dependent homo- and hetero-exchange of neutral amino acids mediated by the amino acid transporter ATB degree.
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DOI：
10.1006/bbrc.1998.8434
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发表时间：
1998-04
影响因子：
3.1
通讯作者：
V. Torres-zamorano;F. Leibach;V. Ganapathy
中科院分区：
文献类型：
--
作者：
V. Torres-zamorano;F. Leibach;V. Ganapathy
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.
