IMR Press / FBL / Volume 23 / Issue 9 / DOI: 10.2741/4663

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


Contribution of activated beta3 integrin in the PDI release from endothelial cells

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1 Department of Cytobiology and Proteomics, Medical University of Lodz, Lodz, Poland
2 Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland
3 Laboratory of Transcriptional Regulation, Institute of Medical Biology PAS, Lodz, Poland
4 Department of Medicine, SUNY Downstate Medical Center, Brooklyn, New York, USA
Front. Biosci. (Landmark Ed) 2018, 23(9), 1612–1627;
Published: 1 March 2018

Protein disulfide isomerase (PDI) is an abundant reticulum endoplasmic protein but also acts as an important functional regulator of some extracellular surface proteins. Recent studies suggest that PDI plays a role in integrin activation and thrombus formation. The aim of this study was to examine whether activation of integrin is the first stage leading to release of PDI from the subcellular compartments of endothelial cells to extracellular space. Our results show that endothelial cells which adhere to fibronectin or fibrinogen release significantly more PDI than those which adhere to poly-L-lysine. Cells treated with RGD peptide, Src and FAK kinase inhibitors and anti alphaVbeta3 antibody display lower PDI secretion. The destruction of the actin cytoskeleton of endothelial cells by cytochalasin D inhibits PDI release. When the endothelial cells adhere to fibrinogen or fibronectin, PDI and alphaVbeta3 gain free thiol groups. Our data suggest that upon activation of integrins, PDI is released from endothelial cells and forms a disulfide bond complex with alphaVbeta3 integrin.

Thiol Groups
Endothelial Cells
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