Lysine Uptake by Cloned hCAT-2B: Comparison with hCAT-1 and with Trophoblast Surface Membranes

Lysine Uptake by Cloned hCAT-2B: Comparison with hCAT-1 and with Trophoblast Surface Membranes To study the cationic amino-acid transporter hCAT-2B of human placenta, total RNA was harvested from primary 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 mRNA for hCAT-2B. RT-PCR yielded a 2.06 kb hCAT-2B cDNA, which was cloned. hCAT-2B cRNA injection into Xenopus laevis oocytes stimulated saturable lysine uptake (Km ~ 125 mM). In the presence of Na+, uptake was completely inhibited by L-arginine but only partially by neutral amino acids. To compare directly the interaction of hCAT-1 and hCAT-2B with neutral amino acids and sodium, we examined the inhibition of these transporters by L-leucine and L-alanine over a wide concentration range. L-Alanine and L-leucine inhibit uptake by hCAT-2B substantially less completely than uptake by hCAT-1. The interaction of hCAT-2B resembles that of system y+ in the microvillous membrane of human placenta, while that of hCAT-1 is more comparable to that of system y+ in basal membrane. The identification and characterization of the various cationic amino-acid transporters of the human placenta have the potential to increase the understanding of the cellular mechanism of transplacental transfer. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Lysine Uptake by Cloned hCAT-2B: Comparison with hCAT-1 and with Trophoblast Surface Membranes

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Publisher
Springer-Verlag
Copyright
Copyright © 2002 by Springer-Verlag New York Inc.
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-002-1001-0
Publisher site
See Article on Publisher Site

Abstract

To study the cationic amino-acid transporter hCAT-2B of human placenta, total RNA was harvested from primary 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 mRNA for hCAT-2B. RT-PCR yielded a 2.06 kb hCAT-2B cDNA, which was cloned. hCAT-2B cRNA injection into Xenopus laevis oocytes stimulated saturable lysine uptake (Km ~ 125 mM). In the presence of Na+, uptake was completely inhibited by L-arginine but only partially by neutral amino acids. To compare directly the interaction of hCAT-1 and hCAT-2B with neutral amino acids and sodium, we examined the inhibition of these transporters by L-leucine and L-alanine over a wide concentration range. L-Alanine and L-leucine inhibit uptake by hCAT-2B substantially less completely than uptake by hCAT-1. The interaction of hCAT-2B resembles that of system y+ in the microvillous membrane of human placenta, while that of hCAT-1 is more comparable to that of system y+ in basal membrane. The identification and characterization of the various cationic amino-acid transporters of the human placenta have the potential to increase the understanding of the cellular mechanism of transplacental transfer.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Sep 1, 2002

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