Diabetic changes in the redox status of the microsomal protein folding machinery

Gábor Nardai, Krisztián Stadler, Eszter Papp, Tamás Korcsmáros, Judit Jakus, Péter Csermely

Research output: Article

38 Citations (Scopus)


Changes in assisted protein folding are largely unexplored in diabetes. In the present studies, we have identified a reductive shift in the redox status of rat liver microsomes after 4 weeks of streptozotocin-induced diabetes. This change was reflected by a significant increase in the total- and protein-sulfhydryl content, as well as in the free sulfhydryl groups of the major protein disulfide isomerases (PDIs), the 58 kDa PDI and the 57 kDa ERp57 but not other chaperones. A parallel decrease of the protein-disulfide oxidoreductase activity was detected in the microsomal fraction of diabetic livers. The oxidant of PDI, Ero1-Lα showed a more oxidized status in diabetic rats. Our results reveal major changes in the redox status of the endoplasmic reticulum and its redox chaperones in diabetic rats, which may contribute to the defective protein secretion of the diabetic liver.

Original languageEnglish
Pages (from-to)787-795
Number of pages9
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - szept. 2 2005

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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