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Am J Physiol Endocrinol Metab (October 29, 2002). doi:10.1152/ajpendo.00257.2002
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Articles in PresS, published online ahead of print October 29, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00257.2002
Submitted on June 11, 2002
Accepted on October 16, 2002

CHARACTERIZATION AND IDENTIFICATION OF STEROID SULFATE TRANSPORTERS OF ISOLATED TROPHOBLASTS AND HUMAN PLACENTAL TISSUE1

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

1 I. Frauenklinik Innenstadt, Klinikum der Universitat Munchen, Munich, Germany
2 Department of Internal Medicine, University Hospital, Zurich, Switzerland
3 Med. Klinik II GroBhadern, Klinikum der Universitat Munchen, Munich, Germany
4 Zentrum fur Physiologie und Pathophysiologie, Universitat Gottingen, Gottingen, Germany

* To whom correspondence should be addressed. E-mail: ugele{at}helios.med.uni-muenchen.

Human trophoblasts depend on the supply of external precursors such as dehydroepiandrosterone-3-sulfate (DHEA-S) and 16{alpha}-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 prot. x min)) which was superimposed by a non-saturable uptake mechanism (Kd = 1,2 µl/(mg prot. x min)). 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 17{beta}- 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 and OATP-A, -C, -8, OAT-3 and Na+-taurocholate co-transporting polypeptide (NTCP) are not or only lowly expressed in term placental tissue, freshly isolated and cultured trophoblasts. Immunohistochemistry of 1st and 3rd trimester placenta detected OAT-4 to cytotrophoblast membranes and at the basal surface of the syncytiotrophoblast. Our results indicate that uptake of steroid sulfates by isolated cytotrophoblasts 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.




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