PMID- 10485994
OWN - NLM
STAT- MEDLINE
DCOM- 19991021
LR  - 20141120
IS  - 0022-2631 (Print)
IS  - 0022-2631 (Linking)
VI  - 171
IP  - 1
DP  - 1999 Sep 1
TI  - Identification of three cationic amino acid transporters in placental
      trophoblast: cloning, expression, and characterization of hCAT-1.
PG  - 55-62
AB  - The concentrative transfer of amino acids from maternal to fetal blood is
      essential to fetal growth and metabolism. Cationic amino acids are transported
      across the placental microvillous and basal membranes by multiple pathways which 
      act to mediate maternal/fetal transport. To identify the cationic amino acid
      transporters of human placenta, total RNA was harvested from cultured trophoblast
      and from the BeWo choriocarcinoma cell line, b30 clone, and used for reverse
      transcription (RT) and polymerase chain reaction (PCR). Primers based on
      published sequences identified expression of mRNAs for hCATs-1, -2B, and -4.
      RT-PCR yielded a 2.1 kb hCAT-1 cDNA which was cloned. hCAT-1 cRNA injection into 
      Xenopus laevis oocytes stimulated saturable lysine uptake (K(m) approximately 100
      microM). In the presence of Na(+), uptake was inhibited by leucine, homoserine,
      and alanine but not by valine and glutamate. These transport characteristics are 
      comparable to those of system y(+) in placental basal membrane, but differ from
      those of the same system in microvillous membrane. The identification, cloning,
      and characterization of multiple human placental cationic amino acid transporters
      has the potential to facilitate molecular investigation of transport by the
      maternal- and fetal-facing membranes of placental trophoblast and increase
      understanding of the mechanism of transplacental amino acid transfer.
FAU - Kamath, S G
AU  - Kamath SG
AD  - The Edward Mallinckrodt Department of Pediatrics, St. Louis Children's Hospital, 
      Washington University School of Medicine, St. Louis, MO 63110, USA.
FAU - Furesz, T C
AU  - Furesz TC
FAU - Way, B A
AU  - Way BA
FAU - Smith, C H
AU  - Smith CH
LA  - eng
GR  - HD-07562/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Membr Biol
JT  - The Journal of membrane biology
JID - 0211301
RN  - 0 (Amino Acid Transport Systems, Basic)
RN  - 0 (Amino Acids)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cations)
RN  - 0 (Membrane Proteins)
RN  - 0 (Recombinant Proteins)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Amino Acid Transport Systems, Basic
MH  - Amino Acids/*metabolism
MH  - Animals
MH  - Carrier Proteins/*genetics/*metabolism
MH  - Cations
MH  - Cloning, Molecular
MH  - Female
MH  - Gene Expression
MH  - Humans
MH  - In Vitro Techniques
MH  - Lysine/metabolism
MH  - Membrane Proteins/*genetics/*metabolism
MH  - Oocytes/metabolism
MH  - Pregnancy
MH  - Recombinant Proteins/metabolism
MH  - Trophoblasts/*metabolism
MH  - Tumor Cells, Cultured
MH  - Xenopus laevis
EDAT- 1999/09/15 00:00
MHDA- 1999/09/15 00:01
CRDT- 1999/09/15 00:00
PHST- 1999/09/15 00:00 [pubmed]
PHST- 1999/09/15 00:01 [medline]
PHST- 1999/09/15 00:00 [entrez]
AID - JMEMB9006R [pii]
PST - ppublish
SO  - J Membr Biol. 1999 Sep 1;171(1):55-62.