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Am J Physiol Endocrinol Metab 284: E390-E398, 2003. First published October 29, 2002; doi:10.1152/ajpendo.00257.2002
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Vol. 284, Issue 2, E390-E398, February 2003

Characterization and identification of steroid sulfate transporters of human placenta

Bernhard Ugele1, Marie V. St-Pierre2, Monika Pihusch3, Andrew Bahn4, and Peer Hantschmann1

1 I. Frauenklinik Innenstadt and 3 Medizinische Klinik II Großhadern, Klinikum der Universität München, D-80337 Munich; and 4 Zentrum für Physiologie und Pathophysiologie, D-37073 Gottingen, Germany; and 2 Division of Clinical Pharmacology, Department of Internal Medicine, University Hospital, CH-8091 Zürich, Switzerland

Human trophoblasts depend on the supply of external precursors, such as dehydroepiandrosterone-3-sulfate (DHEA-S) and 16alpha -OH-DHEA-S, for synthesis of estrogens. The aim of the present study was to characterize the uptake of DHEA-S by isolated mononucleated trophoblasts (MT) and to identify the involved transporter polypeptides. The kinetic analysis of DHEA-35S uptake by MT revealed a saturable uptake mechanism (Km = 26 µM, Vmax = 428 pmol · mg protein-1 · min-1), which was superimposed by a nonsaturable uptake mechanism (diffusion constant = 1.2 µl · mg protein-1 · min-1). Uptake of [3H]DHEA-S by MT was Na+ dependent and inhibited by sulfobromophthalein (BSP), steroid sulfates, and probenecid, but not by steroid glucuronides, unconjugated steroids, conjugated bile acids, ouabain, p-aminohippurate (PAH), and bumetanide. MT took up [35S]BSP, [3H]estrone-sulfate, but not 3H-labeled ouabain, estradiol-17beta -glucuronide, taurocholate, and PAH. RT-PCR revealed that the organic anion-transporting polypeptides OATP-B, -D, -E, and the organic anion transporter OAT-4 are highly expressed, and that OATP-A, -C, -8, OAT-3, and Na+-taurocholate cotransporting polypeptide (NTCP) are not or are only lowly expressed in term placental tissue and freshly isolated and cultured trophoblasts. Immunohistochemistry of first- and third-trimester placenta detected OAT-4 on cytotrophoblast membranes and at the basal surface of the syncytiotrophoblast. Our results indicate that uptake of steroid sulfates by isolated MT is mediated by OATP-B and OAT-4 and suggest a physiological role of both carrier proteins in placental uptake of fetal-derived steroid sulfates.

estrogen synthesis; isolated trophoblasts; organic anion transporter; dehydroepiandrosterone sulfate


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