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        <identifier>oai:www.ideals.illinois.edu:2142/82541</identifier>
        <datestamp>2023-07-11</datestamp>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Glaser, Michael</dc:contributor>
          <dc:creator>Chan, Jonah R.</dc:creator>
          <dc:date>2015-09-25T20:45:46Z</dc:date>
          <dc:date>2015-09-25T20:45:46Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>2000</dc:date>
          <dc:date>2000</dc:date>
          <dc:description>In conjunction to the previous study, the platelet-derived growth factor (PDGF) A-chain was detected as two distinct splice variants in Schwann cell/neuronal co-cultures. Both PDGF A-chain isoforms were characterized and examined throughout the myelination process. The mRNA for the long form PDGF A-chain was found to be induced during myelin synthesis and was localized to the DRG neurons. Using an antibody generated against the exon 6 peptide, observations suggest that the splice variant is localized to the surface of axons and to certain Schwann cells that are elongated and ensheathing axons. Since the long form PDGF A-chain is thought to be retained on cellular surfaces by the binding of the basic carboxy-terminal to membrane associated heparan sulfate proteoglycans (HSPG), surface competition experiments were performed with heparin and the basic peptide encoded by exon 6. Heparin and the exon 6 peptide were both found to dramatically inhibit the initiation of myelin formation. While these results are still preliminary, they seem to suggest that the splice variant of the PDGF A-chain/HSPG complex functions as a novel neuronal signal that may regulate steroid biosynthesis in Schwann cells and ultimately lead to the initiation of myelin synthesis.</dc:description>
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  Previous issue date: 2000</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 83822
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>129 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000.</dc:description>
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          <dc:identifier>(MiAaPQ)AAI9971042</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Chemistry, Biochemistry</dc:subject>
          <dc:title>The Regulation and Mechanism of Myelin Synthesis Involving Endogenous Steroid Hormones</dc:title>
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            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
            <department>Neuroscience</department>
            <discipline>Neuroscience</discipline>
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