Sodium-dependent homo- and hetero-exchange of neutral amino acids mediated by the amino acid transporter ATB°

被引：42

作者：

Torres-Zamorano, V ^{[1
]}

Leibach, FH ^{[1
]}

Ganapathy, V ^{[1
]}

机构：

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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 245卷 / 03期

关键词：

D O I：

10.1006/bbrc.1998.8434

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 have investigated the functional characteristics of the human amino acid transporter ATB degrees using the Xenopus laevis oocyte expression system. When expressed in oocytes, ATB degrees 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 degrees. Kinetic analysis indicates that the affinity of ATB degrees for a given amino acid substrate is similar whether ATB degrees 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 degrees to function as a homo- and hetero-exchanger for its substrates. (C) 1998 Academic Press.

引用

页码：824 / 829

页数：6

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