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    <title>Pintar, J.E.</title>
    <link>http://repub.eur.nl/res/aut/920/</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>Generation of antisera to mouse insulin-like growth factor binding proteins (IGFBP)-1 to -6: comparison of IGFBP protein and messenger ribonucleic acid localization in the mouse embryo (Article)</title>
      <link>http://repub.eur.nl/res/pub/9202/</link>
      <pubDate>1999-01-01T00:00:00Z</pubDate>
      <description>The insulin-like growth factor (IGF) system is an important regulator of
          fetal growth and differentiation. IGF bioavailability is modulated by IGF
          binding proteins (IGFBPs). We have generated six different antisera,
          directed to synthetic peptide fragments of mouse IGFBP-1 through -6. The
          specificity of the produced antisera was demonstrated by enzyme-linked
          immunosorbent assay, Western blotting, and by immunohistochemistry on
          sections of mouse embryos of 13.5 days post coitum. Specificity for the
          IGFBP-2 through -6 antisera also was confirmed immunohistochemically in
          liver and lung of corresponding gene deletion (knock-out) mutant mice and
          wild-type litter mates. Immunohistochemistry and messenger RNA (mRNA) in
          situ hybridization on sections of mouse embryos of 13.5 days post coitum
          revealed tissue-specific expression patterns for the six IGFBPs. The only
          site of IGFBP-1 protein and mRNA production was the liver. IGFBP-2, -4,
          and -5 protein and mRNA were detected in various organs and tissues.
          IGFBP-3 and -6 protein and mRNA levels were low. In several tissues, such
          as lung, liver, kidney, and tongue, more than one IGFBP (protein and mRNA)
          could be detected. Differences between mRNA and protein localization were
          extensive for IGFBP-3, -5, and -6, suggesting that these IGFBPs are
          secreted and transported. These results confirm the different spatial
          localization of the IGFBPs, on the mRNA and protein level. The overlapping
          mRNA and protein localization for IGFBP-2 and -4, on the other hand, may
          indicate that these IGFBPs also function in an auto- or paracrine manner.</description>
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