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J Biol Chem, Vol. 274, Issue 34, 23740-23745, August 20, 1999
From the Department of Cell and Molecular Physiology and the
Curriculum in Neurobiology, University of North Carolina, Chapel Hill,
North Carolina 27599
A Na+-dependent
neutral and cationic amino acid transport system (B0+)
plays an important role in many cells and tissues; however, the
molecular basis for this transport system is still unknown. To identify
new transporters, the expressed sequence tag database was queried, and
cDNA fragments with sequence similarity to the Na+/Cl
Cloning and Functional Expression of a Human Na+
and Cl
-dependent Neutral and Cationic
Amino Acid Transporter B0+
-dependent neurotransmitter
transporter family were identified. Based on these sequences, rapid
amplification of cDNA ends of human mammary gland cDNA was used
to obtain a cDNA of 4.5 kilobases (kb). The open reading frame
encodes a 642-amino acid protein named amino acid transporter
B0+. Human ATB0+ (hATB0+) is a
novel member of the
Na+/Cl-dependent neurotransmitter
transporter family with the highest sequence similarity to the glycine
and proline transporters. Northern blot analysis identified transcripts
of ~4.5 kb and ~2 kb in the lung. Another tissue survey suggests
expression in the trachea, salivary gland, mammary gland, stomach, and
pituitary gland. Electrophysiology and radiolabeled amino acid uptake
measurements were used to functionally characterize the transporter
expressed in Xenopus oocytes. hATB0+ was found
to transport both neutral and cationic amino acids, with the highest
affinity for hydrophobic amino acids and the lowest affinity for
proline. Amino acid transport was Na+ and
Cl-dependent and was attenuated in the
presence of 2-aminobicyclo-[2.2.1]-heptane-2-carboxylic acid,
a system B0+ inhibitor. These characteristics are
consistent with system B0+ amino acid transport. Thus,
hATB0+ is the first cloned B0+ amino acid transporter.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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