Protein disulfide isomerase in thrombosis and vascular inflammation

Authors

  • J. Cho

    Corresponding author
    1. Departments of Pharmacology and Anesthesiology, University of Illinois College of Medicine, Chicago, IL, USA
    • Correspondence: Jaehyung Cho, Departments of Pharmacology and Anesthesiology, University of Illinois College of Medicine, 835 S. Wolcott Avenue, E403, Chicago, IL 60612, USA.

      Tel.: +1 312 355 5923; fax: +1 312 996 1225.

      E-mail: thromres@uic.edu

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  • Manuscript handled by: W. Ruf
  • Final decision: P. H. Reitsma, 13 September 2013

Summary

Protein disulfide isomerase (PDI) catalyzes disulfide bond oxidation, reduction and isomerization during protein synthesis in the endoplasmic reticulum (ER). In addition to its critical role in the ER, in vitro and in vivo studies with blocking antibodies and conditional knockout mice have demonstrated that cell surface PDI is required for thrombosis, hemostasis and vascular inflammation in a manner dependent on its isomerase activity. This review will focus on our current understanding of the pathophysiologic role of PDI in regulating integrin-mediated platelet and neutrophil functions during vascular disease.

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