期刊
BIOCHEMICAL JOURNAL
卷 346, 期 -, 页码 705-710出版社
PORTLAND PRESS
DOI: 10.1042/0264-6021:3460705
关键词
antiporter; glutamate transport; glutamine transport; structure-function relationships
资金
- NIA NIH HHS [1 R03-AG16951-01] Funding Source: Medline
The neutral amino acid transporter ASCT2 mediates electroneutral obligatory antiport but at the same time requires Na+ for its function. To elucidate the mechanism, ASCT2 was expressed in Xenopus laevis oocytes and transport was analysed by flux studies and two-electrode voltage clamp recordings. Flux studies with (NaCl)-Na-22 indicated that the uptake of one molecule of glutamine or alanine is accompanied by the uptake of four to seven Na+ ions. Similarly to the transport of amino acids, the Na+ uptake was mediated by an obligatory Na+ exchange mechanism that depended on the presence of amino acids but was not stoichiometrically coupled to the amino acid transport. Other cations could not replace Na+ in this transport mechanism. When NaCl was replaced by NaSCN in the transport buffer, the superfusion of oocytes with amino acid substrates resulted in large inward currents, indicating the presence of a substrate-gated anion channel in the ASCT2 transporter. The K-m for glutamine derived from these experiments is in good agreement with the K-m, derived from flux studies; it varied between 40 and 90 mu M at holding potentials of - 60 and - 20 mV respectively. The permeability of the substrate-gated anion conductance decreased in the order SCN- much greater than NO3- > I- > Cl- and also required the presence of Na+.
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