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J. Biol. Chem., Vol. 275, Issue 31, 23707-23717, August 4, 2000
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From the Departments of We have cloned the human Na+-
and H+-coupled amino acid transport system N (hSN1) from
HepG2 liver cells and investigated its functional characteristics.
Human SN1 protein consists of 504 amino acids and shows high homology
to rat SN1 and rat brain glutamine transporter (GlnT). When expressed
in mammalian cells, the transport function of human SN1 could be
demonstrated with glutamine as the substrate in the presence of LiCl
(instead of NaCl) and cysteine. The transport activity was saturable,
pH-sensitive, and specific for glutamine, histidine, asparagine, and
alanine. Analysis of Li+ activation kinetics showed a
Li+:glutamine stoichiometry of 2:1. When expressed in
Xenopus laevis oocytes, the transport of glutamine or
asparagine via human SN1 was associated with inward currents under
voltage-clamped conditions. The transport function, monitored as
glutamine- or asparagine-induced currents, was saturable,
Na+-dependent, Li+-tolerant, and
pH-sensitive. The transport cycle was associated with the involvement
of more than one Na+ ion. Uptake of asparagine was directly
demonstrable in these oocytes by using radiolabeled substrate, and this
uptake was inhibited by membrane depolarization. In addition,
simultaneous measurement of asparagine influx and charge influx in the
same oocyte yielded an asparagine:charge ratio of 1. These data
suggest that SN1 mediates the influx of two Na+ and one
amino acid substrate per transport cycle coupled to the efflux of one
H+, rendering the transport process electrogenic.
Primary Structure, Genomic Organization, and Functional and
Electrogenic Characteristics of Human System N 1, a Na+-
and H+-coupled Glutamine Transporter*
,,,,,§,, and§¶
Biochemistry and Molecular
Biology, and § Obstetrics and Gynecology, Medical College of
Georgia, Augusta, Georgia 30912
*
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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