<?xml version='1.0' encoding='UTF-8'?>
<OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd">
  <responseDate>2026-03-16T00:11:34Z</responseDate>
  <request metadataPrefix="jpcoar_2.0" identifier="oai:ehime-u.repo.nii.ac.jp:02002274" verb="GetRecord">https://ehime-u.repo.nii.ac.jp/oai</request>
  <GetRecord>
    <record>
      <header>
        <identifier>oai:ehime-u.repo.nii.ac.jp:02002274</identifier>
        <datestamp>2023-10-13T05:26:06Z</datestamp>
        <setSpec>664</setSpec>
      </header>
      <metadata>
        <jpcoar:jpcoar xmlns:datacite="https://schema.datacite.org/meta/kernel-4/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcndl="http://ndl.go.jp/dcndl/terms/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:jpcoar="https://github.com/JPCOAR/schema/blob/master/2.0/" xmlns:oaire="http://namespace.openaire.eu/schema/oaire/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:rioxxterms="http://www.rioxx.net/schema/v2.0/rioxxterms/" xmlns:xs="http://www.w3.org/2001/XMLSchema" xmlns="https://github.com/JPCOAR/schema/blob/master/2.0/" xsi:schemaLocation="https://github.com/JPCOAR/schema/blob/master/2.0/jpcoar_scm.xsd">
          <dc:title xml:lang="en">Lactate dehydrogenase enhances immunoglobulin production by human hybridoma and human peripheral blood lymphocytes</dc:title>
          <jpcoar:creator>
            <jpcoar:creatorName xml:lang="en">TAKENOUCHI, Satoshi</jpcoar:creatorName>
            <jpcoar:affiliation>
              <jpcoar:affiliationName xml:lang="en">Faculty of Agriculture, Ehime University</jpcoar:affiliationName>
            </jpcoar:affiliation>
          </jpcoar:creator>
          <jpcoar:creator>
            <jpcoar:creatorName xml:lang="en">SUGAHARA, Takuya</jpcoar:creatorName>
            <jpcoar:affiliation>
              <jpcoar:affiliationName xml:lang="en">Faculty of Agriculture, Ehime University</jpcoar:affiliationName>
            </jpcoar:affiliation>
          </jpcoar:creator>
          <jpcoar:subject subjectScheme="NDC">464</jpcoar:subject>
          <jpcoar:subject subjectScheme="NDC">491.4</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">hybridoma</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">immunoglobulin production</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">lactate dehydrogenase</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">peripheral blood lymphocytes</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">serum-free culture</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">immunostimulation</jpcoar:subject>
          <jpcoar:subject subjectScheme="Other">IgM</jpcoar:subject>
          <datacite:description xml:lang="en">Lactate dehydrogenase (LDH) derived from rabbit muscle enhanced IgM production by human-human hybridoma HB4C5 cells 12.4-fold at 320 μg/ml under serum-free condition. LDHs from pig muscle and pig heart also accelerated IgM production 8.4- and 6.4-fold, respectively. The immunoglobulin production stimulating activity of LDH was not accompanied with activation of cell proliferation. LDH from rabbit muscle facilitated IgM and IgG production by human peripheral blood lymphocytes. This means LDH stimulates immunoglobulin production not only by the specified hybridoma cell line, but also by unspecified immunoglobulin producers. LDH from rabbit muscle enhanced IgM production of transcription-suppressed HB4C5 cells treated with actinomycin D. The IPSF effect of LDH was slightly weakened by sodium fluoride (translation inhibitor) treatment of HB4C5. Moreover, the amount of intracellular IgM of monensin-treated HB4C5 cells was obviously enhanced by LDH. This result means that the IPSF effect of LDH is irrelevant to the post-translation activity of target cells. It is expected from these findings that LDH from rabbit muscle accelerates the translation step to enhance immunoglobulin productivity. The immunoglobulin production stimulating activity of LDH was inhibited by colchicine, endocytosis inhibitor. This fact suggests that it is necessary for LDH to be taken by target cells for acting as IPSF.</datacite:description>
          <dc:publisher xml:lang="en">Springer</dc:publisher>
          <datacite:date dateType="Issued">2003-09</datacite:date>
          <dc:language>eng</dc:language>
          <dc:type rdf:resource="http://purl.org/coar/resource_type/c_6501">journal article</dc:type>
          <oaire:version rdf:resource="http://purl.org/coar/version/c_ab4af688f83e57aa">AM</oaire:version>
          <jpcoar:identifier identifierType="URI">https://ehime-u.repo.nii.ac.jp/records/2002274</jpcoar:identifier>
          <jpcoar:relation>
            <jpcoar:relatedIdentifier identifierType="PMID">19002935</jpcoar:relatedIdentifier>
          </jpcoar:relation>
          <jpcoar:relation>
            <jpcoar:relatedIdentifier identifierType="DOI">10.1023/B:CYTO.0000015838.06536.de</jpcoar:relatedIdentifier>
          </jpcoar:relation>
          <jpcoar:sourceIdentifier identifierType="NCID">AA10678299</jpcoar:sourceIdentifier>
          <jpcoar:sourceIdentifier identifierType="ISSN">0920-9069</jpcoar:sourceIdentifier>
          <jpcoar:sourceTitle xml:lang="en">Cytotechnology</jpcoar:sourceTitle>
          <jpcoar:volume>42</jpcoar:volume>
          <jpcoar:issue>3</jpcoar:issue>
          <jpcoar:pageStart>133</jpcoar:pageStart>
          <jpcoar:pageEnd>143</jpcoar:pageEnd>
          <jpcoar:file>
            <jpcoar:URI>https://ehime-u.repo.nii.ac.jp/record/2002274/files/AA10678299_42_133-143.pdf</jpcoar:URI>
            <jpcoar:mimeType>application/pdf</jpcoar:mimeType>
          </jpcoar:file>
        </jpcoar:jpcoar>
      </metadata>
    </record>
  </GetRecord>
</OAI-PMH>
