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J Biol Chem, Vol. 275, Issue 13, 9690-9698, March 31, 2000
From the A cDNA was isolated from the mouse brain that
encodes a novel Na+-independent neutral amino acid
transporter. The encoded protein, designated as Asc-1 (asc-type amino
acid transporter 1), was found to be structurally related to recently
identified mammalian amino acid transporters for the transport systems
L, y+L, xC The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB026688.
Identification and Characterization of a
Na+-independent Neutral Amino Acid Transporter That
Associates with the 4F2 Heavy Chain and Exhibits Substrate Selectivity
for Small Neutral D- and L-Amino Acids*
,§¶,,,,
,,, and**
Department of Pharmacology and Toxicology,
Kyorin University School of Medicine, 6-20-2 Shinkawa, Mitaka, Tokyo
181-8611, the § Department of Clinical Nutrition, School of
Medicine, Tokushima University, Kuramoto-Cho 3, Tokushima 770-8503, the
First Department of Physiology, National Defense Medical
College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, and ** PRESTO, Japan
Science and Technology Corporation, Japan
, and b0,+,
which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to
b0,+ amino acid transporter). Asc-1 required 4F2hc for its
functional expression. In Western blot analysis in the nonreducing
condition, a 118-kDa band, which seems to correspond to the
heterodimeric complex of Asc-1 and 4F2hc, was detected in the mouse
brain. The band shifted to 33 kDa in the reducing condition, confirming
that Asc-1 and 4F2hc are linked via a disulfide bond. Asc-1-mediated transport was not dependent on the presence of Na+ or
Cl. Although Asc-1 showed a high sequence homology (66%
identity at the amino acid level) to the Na+-independent
broad scope neutral amino acid transporter LAT2 (Segawa, H., Fukasawa,
Y., Miyamoto, K., Takeda, E., Endou, H., and Kanai, Y. (1999)
J. Biol. Chem. 274, 19745-19751), Asc-1 also
exhibited distinctive substrate selectivity and transport properties.
Asc-1 preferred small neutral amino acids such as Gly,
L-Ala, L-Ser, L-Thr, and
L-Cys, and 
-aminoisobutyric acid as substrates. Asc-1 also transported D-isomers of the small neutral amino
acids, in particular D-Ser, a putative endogenous modulator
of N-methyl-D-aspartate-type glutamate
receptors, with high affinity. Asc-1 operated preferentially, although
not exclusively, in an exchange mode. Asc-1 mRNA was detected in
the brain, lung, small intestine, and placenta. The functional
properties of Asc-1 seem to be consistent with those of a transporter
subserving the Na+-independent small neutral amino acid
transport system asc.
*
This work was supported in part by grants from the Ministry
of Education, Science, Sports and Culture of Japan (Grants-in-Aid for
Scientific Research and High-Tech Research Center), the Scientific Research Promotion Fund of the Japan Private School Promotion Foundation, the Japan Science and Technology Corporation, the Kato
Memorial Bioscience Foundation, the Research Fund of Mitsukoshi Health
and Welfare Foundation (1998), the Uehara Memorial Foundation, and the
Toyota Physical & Chemical Research Institute.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.
To whom correspondence should be addressed: Dept. of
Pharmacology and Toxicology, Kyorin University School of Medicine,
6-20-2 Shinkawa, Mitaka, Tokyo 181-8611, Japan. Tel.: 81-422-47-5511, Ext. 3453; Fax: 81-422-79-1321.
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