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Am J Physiol Cell Physiol 278: C1162-C1171, 2000;
0363-6143/00 $5.00
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Vol. 278, Issue 6, C1162-C1171, June 2000

Development and polarization of cationic amino acid transporters and regulators in the human placenta

Paul T.-Y. Ayuk, Colin P. Sibley, Paul Donnai, Stephen D'Souza, and Jocelyn D. Glazier

Academic Unit of Child Health, University of Manchester and Department of Obstetrics and Gynecology, St. Mary's Hospital, Manchester M13 0JH, United Kingdom

We have investigated L-arginine transport systems in the human placental syncytiotrophoblast across gestation using purified microvillous (MVM) and basal (BM) plasma membrane vesicles. In MVM from first-trimester and term placentas, L-arginine transport was by systems y+ and y+L. In BM (term placentas), however, there was evidence for system y+L only. The Michaelis constant of system y+L was significantly lower (P < 0.05) in first-trimester compared with term MVM and lower in term MVM compared with BM (P < 0.05). There was no functional evidence for system b0+ in term MVM or BM. Cationic amino acid transporter (CAT) 1, CAT 4, and 4F2hc were detected using RT-PCR in placentas throughout gestation. rBAT was not detected in term placentas. An ~85-kDa and an ~135-kDa protein was detected by Western blotting in MVM under reducing and nonreducing conditions, respectively, consistent with the 4F2hc monomer and the 4F2hc-light chain dimer, and their expression was significantly higher (P < 0.05) in term compared with first-trimester MVM. These proteins were not detected in BM despite functional evidence for system y+L. These data suggest different roles for 4F2hc in the development and polarization of cationic amino acid transporters in the syncytiotrophoblast.

CAT 1; CAT 4; 4F2hc; rBAT; L-arginine; gestational change


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