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J Biol Chem, Vol. 273, Issue 37, 23629-23632, September 11, 1998
,¶,
,
From the A cDNA was isolated from rat C6
glioma cells by expression cloning which encodes a novel
Na+-independent neutral amino acid transporter
designated LAT1. For functional expression in Xenopus
oocytes, LAT1 required the heavy chain of 4F2 cell surface antigen
(CD98), a type II membrane glycoprotein. When co-expressed with 4F2
heavy chain, LAT1 transported neutral amino acids with branched
or aromatic side chains and did not accept basic amino acids or acidic
amino acids. The transport via LAT1 was
Na+-independent and sensitive to a system L-specific
inhibitor 2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid. These
functional properties correspond to those of the classically characterized amino acid transport system L, a major nutrient transporter. In in vitro translation, LAT1 was shown to be
a nonglycosylated membrane protein consistent with the property of 4F2
light chain, suggesting LAT1 is at least one of the proteins formerly
referred to as 4F2 light chain. LAT1 exhibits relatively low but
significant amino acid sequence similarity to mammalian cationic amino
acid transporters and amino acid permeases of bacteria and yeasts, indicating LAT1 is a new member of the APC superfamily. Because of
highly regulated nature and high level of expression in tumor cell
lines, LAT1 is thought to be up-regulated to support the high protein
synthesis for cell growth and cell activation. The cloning of LAT1 is
expected to facilitate the research on the protein-protein interaction
in the transporter field and to provide a clue to the search for still
unidentified transporters.
Department of Pharmacology and Toxicology, Faculty of Pharmaceutical Sciences,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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