Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Protein Disulfide Isomerase

  • Andrea Shergalis
  • Nouri NeamatiEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101768


Historical Background

The dithiol-disulfide oxidoreductase protein disulfide isomerase (PDI) was discovered in 1963 as the first protein folding chaperone. Research groups led by Brunó Straub (Venetianer and Straub 1963) and Christian B. Anfinsen (Goldberger et al. 1963) independently made pivotal discoveries about an enzyme that reactivated reduced ribonuclease. Straub and coworkers purified the reactivating system from chicken pancreas. Anfinsen studied the system in conjunction with his Nobel-prize-winning work on ribonuclease and purified a system with similar activity from rat liver microsomes. In 1972, the enzyme was given the name protein disulfide isomerase and its official classification number, EC The newly purified protein was identified as the “ribonuclease-reactivating enzyme” and was nearly identical to glutathione-insulin transhydrogenase, causing confusion in the field (Bjelland et al. 1983). Both enzymes...

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We acknowledge financial support from the National Cancer Institute, NIH (CA193690).


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Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Department of Medicinal Chemistry, College of PharmacyTranslational Oncology Program, University of MichiganAnn ArborUSA