{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,5]],"date-time":"2026-04-05T10:21:06Z","timestamp":1775384466676,"version":"3.50.1"},"reference-count":38,"publisher":"American Physiological Society","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Endocrinology and Metabolism"],"published-print":{"date-parts":[[2003,2,1]]},"abstract":"<jats:p>Human trophoblasts depend on the supply of external precursors, such as dehydroepiandrosterone-3-sulfate (DHEA-S) and 16\u03b1-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-<jats:sup>35<\/jats:sup>S uptake by MT revealed a saturable uptake mechanism ( K<jats:sub>m<\/jats:sub>= 26 \u03bcM, V<jats:sub>max<\/jats:sub>= 428 pmol \u00b7 mg protein<jats:sup>\u22121<\/jats:sup>\u00b7 min<jats:sup>\u22121<\/jats:sup>), which was superimposed by a nonsaturable uptake mechanism (diffusion constant = 1.2 \u03bcl \u00b7 mg protein<jats:sup>\u22121<\/jats:sup>\u00b7 min<jats:sup>\u22121<\/jats:sup>). Uptake of [<jats:sup>3<\/jats:sup>H]DHEA-S by MT was Na<jats:sup>+<\/jats:sup>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 [<jats:sup>35<\/jats:sup>S]BSP, [<jats:sup>3<\/jats:sup>H]estrone-sulfate, but not<jats:sup>3<\/jats:sup>H-labeled ouabain, estradiol-17\u03b2-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<jats:sup>+<\/jats:sup>-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.<\/jats:p>","DOI":"10.1152\/ajpendo.00257.2002","type":"journal-article","created":{"date-parts":[[2015,3,3]],"date-time":"2015-03-03T19:41:39Z","timestamp":1425411699000},"page":"E390-E398","source":"Crossref","is-referenced-by-count":139,"title":["Characterization and identification of steroid sulfate transporters of human placenta"],"prefix":"10.1152","volume":"284","author":[{"given":"Bernhard","family":"Ugele","sequence":"first","affiliation":[{"name":"I. 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