PMID- 10446133
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 34
DP  - 1999 Aug 20
TI  - Cloning and functional expression of a human Na(+) and Cl(-)-dependent neutral
      and cationic amino acid transporter B(0+).
PG  - 23740-5
AB  - A Na(+)-dependent neutral and cationic amino acid transport system (B(0+)) 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(-)-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
      B(0+). Human ATB(0+) (hATB(0+)) 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 approximately 4.5 kb and approximately 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. hATB(0+) 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 B(0+) inhibitor. These characteristics are consistent with system B(0+)
      amino acid transport. Thus, hATB(0+) is the first cloned B(0+) amino acid
      transporter.
FAU - Sloan, J L
AU  - Sloan JL
AD  - Department of Cell and Molecular Physiology and the Curriculum in Neurobiology,
      University of North Carolina, Chapel Hill, North Carolina 27599, USA.
FAU - Mager, S
AU  - Mager S
LA  - eng
SI  - GENBANK/AF151978
SI  - GENBANK/AF161714
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 (Carrier Proteins)
RN  - 0 (Chlorides)
RN  - 94ZLA3W45F (Arginine)
RN  - 9NEZ333N27 (Sodium)
RN  - GMW67QNF9C (Leucine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Transport Systems
MH  - Arginine/metabolism
MH  - Carrier Proteins/chemistry/*genetics/physiology
MH  - Chlorides/*pharmacology
MH  - Cloning, Molecular
MH  - Humans
MH  - Leucine/metabolism
MH  - Molecular Sequence Data
MH  - Sodium/*pharmacology
EDAT- 1999/08/14 00:00
MHDA- 1999/08/14 00:01
CRDT- 1999/08/14 00:00
PHST- 1999/08/14 00:00 [pubmed]
PHST- 1999/08/14 00:01 [medline]
PHST- 1999/08/14 00:00 [entrez]
AID - 10.1074/jbc.274.34.23740 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Aug 20;274(34):23740-5. doi: 10.1074/jbc.274.34.23740.