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    <title>Iizuka-Kogo, A.</title>
    <link>http://repub.eur.nl/res/aut/54695/</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>
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    <item>
      <title>The C-terminal domain of the adenomatous polyposis coli (Apc) protein is involved in thyroid morphogenesis and function (Article)</title>
      <link>http://repub.eur.nl/res/pub/34606/</link>
      <pubDate>2011-12-01T00:00:00Z</pubDate>
      <description>Adenomatous polyposis coli (APC) is a multifunctional protein as well as a tumor suppressor. To determine the functions of the C-terminal domain of Apc, we have investigated Apc1638T/1638Tmice, which express a truncated Apc that lacks the C-terminal domain. Apc1638T/1638Tmice are tumor free and exhibit growth retardation. In the present study, we analyzed the morphology and functions of the thyroid gland in Apc1638T/1638Tmice. There was no significant difference in the basal concentration of serum thyroid hormones between Apc1638T/1638Tand Apc+/+mice. Thyroid follicle size was significantly larger in Apc1638T/1638Tmice than in Apc+/+mice. The extent of serum T4 elevation following exogenous thyroid-stimulating hormone (TSH) injection was lower in Apc1638T/1638Tmice than in Apc+/+mice. TSH also induced a greater reduction in thyroid follicle size in Apc1638T/1638Tmice than in Apc+/+mice. Analyses using immunohistochemistry and electron microscopy indicated that follicular epithelial cells in Apc1638T/1638Tmice had an enlarged rough endoplasmic reticulum of irregular shape. These results suggest that the C-terminal domain of Apc is involved in thyroid morphology and function. </description>
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