PMID- 10391915
OWN - NLM
STAT- MEDLINE
DCOM- 19990805
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 28
DP  - 1999 Jul 9
TI  - 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.
PG  - 19738-44
AB  - 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 >> brain, liver > spleen, skeletal muscle, heart, small intestine,
      and lung. Human LAT-2 gene localizes at chromosome 14q11.2-13 (13 cR or
      approximately 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.
FAU - Pineda, M
AU  - Pineda M
AD  - Departament de Bioquimica i Biologia Molecular, Universitat de Barcelona, Avda.
      Diagonal 645, 08028 Barcelona, Spain.
FAU - Fernandez, E
AU  - Fernandez E
FAU - Torrents, D
AU  - Torrents D
FAU - Estevez, R
AU  - Estevez R
FAU - Lopez, C
AU  - Lopez C
FAU - Camps, M
AU  - Camps M
FAU - Lloberas, J
AU  - Lloberas J
FAU - Zorzano, A
AU  - Zorzano A
FAU - Palacin, M
AU  - Palacin M
LA  - eng
SI  - GENBANK/AF135828
SI  - GENBANK/AF135829
SI  - GENBANK/AF135830
SI  - GENBANK/AF135831
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Amino Acid Transport Systems)
RN  - 0 (Amino Acids)
RN  - 0 (Antigens, CD)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Fusion Regulatory Protein-1)
RN  - 0 (Membrane Proteins)
RN  - 0 (RNA, Messenger)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Transport Systems
MH  - Amino Acids/metabolism
MH  - Animals
MH  - Antigens, CD/*genetics
MH  - Base Sequence
MH  - Carrier Proteins/chemistry/*genetics
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - Fusion Regulatory Protein-1
MH  - Gene Expression Regulation
MH  - Humans
MH  - Kinetics
MH  - Membrane Proteins/chemistry/*genetics
MH  - Microinjections
MH  - Molecular Sequence Data
MH  - Oocytes/metabolism
MH  - RNA, Messenger/metabolism
MH  - Sequence Alignment
MH  - Xenopus laevis
EDAT- 1999/07/03 00:00
MHDA- 1999/07/03 00:01
CRDT- 1999/07/03 00:00
PHST- 1999/07/03 00:00 [pubmed]
PHST- 1999/07/03 00:01 [medline]
PHST- 1999/07/03 00:00 [entrez]
AID - 10.1074/jbc.274.28.19738 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 9;274(28):19738-44. doi: 10.1074/jbc.274.28.19738.