Elevated expression of PDI family proteins during differentiation of mouse F9 teratocarcinoma cells

Osamu Miyaishi, Ken Ichi Kozaki, Ken Ichi Iida, Ken Ichi Isobe, Yoshio Hashizume, Shinsuke Saga

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19 Citations (Scopus)


We investigated the expression of protein disulfide isomerase family proteins (PDI, ERp61, and ERp72) in mouse F9 teratocarcinoma cells during differentiation induced by treatment with retinoic acid and dibutyryl cAMP. Each member of this family was expressed at a constitutive level in undifferentiated F9 cells. During differentiation of F9 cells to parietal or visceral endodermal cells the protein level of all these enzymes increased, although the extent of this increase in both protein and mRNA levels varied among the enzymes. Certain proteins were found to be coimmunoprecipitated with PDI, ERp61, and ERp72 in the presence of a chemical crosslinker. Type IV collagen was significantly coprecipitated with PDI whereas laminin was equally coprecipitated with the three proteins. Furthermore, 210 kDa protein characteristically coprecipitated with ERp72. Thus, the induction of PDI family proteins during the differentiation of F9 cells and their association with different proteins may implicate specific functions of each member of this family despite the common redox activity capable of catalyzing the disulfide bond formation.

Original languageEnglish
Pages (from-to)436-445
Number of pages10
JournalJournal of Cellular Biochemistry
Issue number4
Publication statusPublished - Mar 15 1998


  • Dibutyryl cAMP
  • Differentiation
  • Mouse
  • PDI family proteins
  • Retinoic acid

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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