<?xml version="1.0" encoding="UTF-8"?>
<collection xmlns="http://www.loc.gov/MARC21/slim">
 <record>
  <leader>     caa a22        4500</leader>
  <controlfield tag="001">397494505</controlfield>
  <controlfield tag="003">CHVBK</controlfield>
  <controlfield tag="005">20180308164517.0</controlfield>
  <controlfield tag="007">cr unu---uuuuu</controlfield>
  <controlfield tag="008">161202e199501  xx      s     000 0 eng  </controlfield>
  <datafield tag="024" ind1="7" ind2="0">
   <subfield code="a">10.1093/oxfordjournals.jbchem.a124709</subfield>
   <subfield code="2">doi</subfield>
  </datafield>
  <datafield tag="035" ind1=" " ind2=" ">
   <subfield code="a">(NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124709</subfield>
  </datafield>
  <datafield tag="245" ind1="0" ind2="0">
   <subfield code="a">Involvement of Pertussis Toxin-Sensitive Mechanism in Retinoic Acid-Induced Differentiation of Human Leukemic HL-60 Cells</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Yoshiharu Ohoka, Kenji Kontani, Taroh Iiri, Hiroshi Nishina, Toshiaki Katada]</subfield>
  </datafield>
  <datafield tag="520" ind1="3" ind2=" ">
   <subfield code="a">Retinoic acid-induced differentiation of human leukemic HL-60 cells is accompanied with the early induction of an ecto-enzyme of NAD+ glycohydrolase (NADase), which has recently been identified as human leukocyte cell surface antigen CD38 [Kontani, K. et al. (1993) J. Biol. Chem. 268, 16895-16898]. The terminal cell differentiation attendant upon the cell growth arrest was, but the early induction of CD38 NADase activity was not, inhibited by prior treatment of HL-60 cells with pertussis toxin, which catalyzed ADP-ribosylation of the membrane-bound αβγ-trimeric GTP-binding proteins. The prior treatment was, however, not essential for the toxin-induced inhibition of the cell differentiation; the inhibition by the addition of pertussis toxin was still observed even after retinoic acid-induced expression of CD38 antigen. This suggested that a pertussis toxin-sensitive mechanism was involved in a late process of cell differentiation. Indeed, HL-60 cells appeared to secrete a differentiation-supporting factor in response to retinoic acid, since the cell differentiation was accelerated and potentiated upon culture of the cells in a conditioned medium prepared from retinoic acid-treated cells. The action of the differentiation-supporting factor was destroyed by heating and markedly attenuated in pertussis toxin-pretreated HL-60 cells. Thus, the whole process of the retinoic acid-induced cell differentiation appeared to consist of two distinguishable periods in terms of sensitivity to pertussis toxin; the toxin-insensitive early period characterized by the induction of CD38 NADase activity and the toxin-sensitive late period in which the secretion of a differentiation-supporting factor might be involved.</subfield>
  </datafield>
  <datafield tag="540" ind1=" " ind2=" ">
   <subfield code="a">© 1995 BY THE JOURNAL OF BIOCHEMISTRY</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Regular Papers</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">CD38 antigen</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">cell differentiation</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">GTP-binding proteins</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">pertussis toxin</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">retinoic acid</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Ohoka</subfield>
   <subfield code="D">Yoshiharu</subfield>
   <subfield code="u">Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Kontani</subfield>
   <subfield code="D">Kenji</subfield>
   <subfield code="u">Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Iiri</subfield>
   <subfield code="D">Taroh</subfield>
   <subfield code="u">Department of Life Science, Tokyo Institute of Technology, Midori-ku, Yokohama 227, Hongo, Bunkyo-ku, Tokyo 113</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Nishina</subfield>
   <subfield code="D">Hiroshi</subfield>
   <subfield code="u">Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Katada</subfield>
   <subfield code="D">Toshiaki</subfield>
   <subfield code="u">Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="773" ind1="0" ind2=" ">
   <subfield code="t">The Journal of Biochemistry</subfield>
   <subfield code="d">Oxford University Press</subfield>
   <subfield code="g">117/1(1995-01), 190-196</subfield>
   <subfield code="x">0021-924X</subfield>
   <subfield code="q">117:1&lt;190</subfield>
   <subfield code="1">1995</subfield>
   <subfield code="2">117</subfield>
   <subfield code="o">jbchem</subfield>
  </datafield>
  <datafield tag="856" ind1="4" ind2="0">
   <subfield code="u">https://doi.org/10.1093/oxfordjournals.jbchem.a124709</subfield>
   <subfield code="q">text/html</subfield>
   <subfield code="z">Onlinezugriff via DOI</subfield>
  </datafield>
  <datafield tag="908" ind1=" " ind2=" ">
   <subfield code="D">1</subfield>
   <subfield code="a">research-article</subfield>
   <subfield code="2">jats</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">856</subfield>
   <subfield code="E">40</subfield>
   <subfield code="u">https://doi.org/10.1093/oxfordjournals.jbchem.a124709</subfield>
   <subfield code="q">text/html</subfield>
   <subfield code="z">Onlinezugriff via DOI</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Ohoka</subfield>
   <subfield code="D">Yoshiharu</subfield>
   <subfield code="u">Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Kontani</subfield>
   <subfield code="D">Kenji</subfield>
   <subfield code="u">Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Iiri</subfield>
   <subfield code="D">Taroh</subfield>
   <subfield code="u">Department of Life Science, Tokyo Institute of Technology, Midori-ku, Yokohama 227, Hongo, Bunkyo-ku, Tokyo 113</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Nishina</subfield>
   <subfield code="D">Hiroshi</subfield>
   <subfield code="u">Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Katada</subfield>
   <subfield code="D">Toshiaki</subfield>
   <subfield code="u">Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">773</subfield>
   <subfield code="E">0-</subfield>
   <subfield code="t">The Journal of Biochemistry</subfield>
   <subfield code="d">Oxford University Press</subfield>
   <subfield code="g">117/1(1995-01), 190-196</subfield>
   <subfield code="x">0021-924X</subfield>
   <subfield code="q">117:1&lt;190</subfield>
   <subfield code="1">1995</subfield>
   <subfield code="2">117</subfield>
   <subfield code="o">jbchem</subfield>
  </datafield>
  <datafield tag="900" ind1=" " ind2="7">
   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">CC BY-NC-4.0</subfield>
   <subfield code="u">http://creativecommons.org/licenses/by-nc/4.0</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="898" ind1=" " ind2=" ">
   <subfield code="a">BK010053</subfield>
   <subfield code="b">XK010053</subfield>
   <subfield code="c">XK010000</subfield>
  </datafield>
  <datafield tag="949" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="F">NATIONALLICENCE</subfield>
   <subfield code="b">NL-oxford</subfield>
  </datafield>
 </record>
</collection>
