<?xml version="1.0" encoding="UTF-8" standalone="no" ?>
<rss version="2.0">
  <channel>
    <title>Pabel, U.</title>
    <link>http://repub.eur.nl/res/aut/7009/</link>
    <description>List of Publications</description>
    <language>en</language>
    <image>
      <url>http://repub.eur.nl/static-eur/img/logo.png</url>
      <title>RePub, Erasmus University Rotterdam</title>
      <link>http://repub.eur.nl</link>
    </image>
    <item>
      <title>Sulfation of thyroid hormone by estrogen sulfotransferase (Article)</title>
      <link>http://repub.eur.nl/res/pub/9136/</link>
      <pubDate>1999-01-01T00:00:00Z</pubDate>
      <description>Sulfation is one of the pathways by which thyroid hormone is inactivated.
          Iodothyronine sulfate concentrations are very high in human fetal blood
          and amniotic fluid, suggesting important production of these conjugates in
          utero. Human estrogen sulfotransferase (SULT1E1) is expressed among other
          tissues in the uterus. Here we demonstrate for the first time that SULT1E1
          catalyzes the facile sulfation of the prohormone T4, the active hormone T3
          and the metabolites rT3 and 3,3'-diiodothyronine (3,3'-T2) with preference
          for rT3 approximately 3,3'-T2 &gt; T3 approximately T4. Thus, a single enzyme
          is capable of sulfating two such different hormones as the female sex
          hormone and thyroid hormone. The potential role of SULT1E1 in fetal
          thyroid hormone metabolism needs to be considered.</description>
    </item>
  </channel>
</rss>