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Am J Physiol Cell Physiol 274: C603-C614, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 3, C603-C614, March 1998

Activity and protein localization of multiple glutamate transporters in gestation day 14 vs. day 20 rat placenta

James C. Matthews1,2, Mark J. Beveridge1, Marc S. Malandro2, Jeffrey D. Rothstein4, Martha Campbell-Thompson3, Jill W. Verlander3, Michael S. Kilberg2, and Donald A. Novak1

Departments of 1 Pediatrics, 2 Biochemistry and Molecular Biology, and 3 Medicine, University of Florida College of Medicine, Gainesville, Florida 32610; and 4 Department of Neurology, Johns Hopkins University, Baltimore, Maryland 21287

Concentrative absorption of glutamate by the developing placenta is critical for proper fetal development. The expression of GLAST1, GLT1, EAAC1, and EAAT4, known to be capable of D-aspartate-inhibitable and Na+-coupled glutamate transport (system X<SUP>−</SUP><SUB>AG</SUB>), was evaluated in day 14 vs. day 20 rat chorioallantoic placenta. Steady-state mRNA levels were greater at day 20 for all transporters. Immunohistochemistry determined that the expression of GLAST1, GLT1, and EAAC1 was greater throughout the day 20 placenta and was asymmetric with respect to cellular localization. EAAT4 protein was not detected. System X<SUP>−</SUP><SUB>AG</SUB> activity was responsible for most of the Na+-dependent glutamate uptake and was greater in day 20 than in day 14 apical and basal membrane subdomains of the labyrinth syncytiotrophoblast. Greater quantities of EAAC1 and GLAST1 protein were identified on day 20, and quantities were greater in basal than in apical membranes. GLT1 expression, unchanged in apical membranes, was decreased in basal membranes. These data correlate transporter mRNA and protein content with transport activity and demonstrate an increasing capacity for glutamate absorption by the developing placenta.

developmental regulation; spongiotrophoblast tissue; labyrinth tissue; system X<SUP>−</SUP><SUB>AG</SUB>; anionic amino acid transport

1 The nucleotide sequence reported in this paper resides in the GenBank/EMBL data bank with accession number U80915.

2  We consistently saw this band, whether freshly isolated or frozen membranes were used, whether 6 M urea or 10 or 100 mM dithiothreitol replaced 2-mercaptoethanol as the reducing agent, and regardless of the heating temperature (39°C, 65°C, and 100°C) and length of heating (5 and 15 min) of the samples before SDS-polyacrylamide gel electrophoresis analysis. In liver tissue homogenates and plasma membrane preparations, we detected a similar immunoreactive band of ~160 kDa (Matthews, unpublished research). Therefore, the GLAST1-immunoreactive band may represent either a placental tissue homodimer with a different glycosylation profile from that of the brain or a complex of GLAST1 protein with another unknown protein. Alternatively, the 160-kDa band for GLAST1 as well as the larger multiple bands observed for GLT1 may represent oligomer species that were induced by the oxidation of monomers during in vitro manipulations, as has been recently described (12).




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