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J Biol Chem, Vol. 274, Issue 28, 19738-19744, July 9, 1999
From the Departament de Bioquímica i Biologia Molecular and
** Departament de Fisiologia, We have identified a new
human cDNA, L-amino acid transporter-2 (LAT-2), that induces a
system L transport activity with 4F2hc (the heavy chain of the surface
antigen 4F2, also named CD98) in oocytes. Human LAT-2 is the fourth
member of the family of amino acid transporters that are subunits of
4F2hc. The amino acid transport activity induced by the co-expression
of 4F2hc and LAT-2 was sodium-independent and showed broad specificity for small and large zwitterionic amino acids, as well as bulky analogs
(e.g. BCH (2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid)). This transport activity was highly
trans-stimulated, suggesting an exchanger mechanism of
transport. Expression of tagged N-myc-LAT-2 alone in
oocytes did not induce amino acid transport, and the protein had an
intracellular location. Co-expression of N-myc-LAT-2 and
4F2hc gave amino acid transport induction and expression of N-myc-LAT-2 at the plasma membrane of the oocytes. These
data suggest that LAT-2 is an additional member of the family of 4F2 light chain subunits, which associates with 4F2hc to express a system L
transport activity with broad specificity for zwitterionic amino acids.
Human LAT-2 mRNA is expressed in kidney >>>
placenta
Identification of a Membrane Protein, LAT-2, That
Co-expresses with 4F2 Heavy Chain, an L-type Amino Acid Transport
Activity with Broad Specificity for Small and Large Zwitterionic
Amino Acids
, Serveis Científico-Tècnics, Universitat
de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain
brain, liver > spleen, skeletal muscle, heart,
small intestine, and lung. Human LAT-2 gene localizes at
chromosome 14q11.2-13 (13 cR or ~286 kb from marker D14S1349). The
high expression of LAT-2 mRNA in epithelial cells of proximal
tubules, the basolateral location of 4F2hc in these cells, and the
amino acid transport activity of LAT-2 suggest that this transporter
contributes to the renal reabsorption of neutral amino acids in the
basolateral domain of epithelial proximal tubule cells.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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