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Tytuł pozycji:

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

Tytuł :
Contribution of activated beta3 integrin in the PDI release from endothelial cells.
Autorzy :
Ponamarczuk H; Department of Cytobiology and Proteomics, Medical University of Lodz, Poland.
Popielarski M; Department of Cytobiology and Proteomics, Medical University of Lodz, Poland.
Stasiak M; Department of Cytobiology and Proteomics, Medical University of Lodz, Poland.
Bednarek R; Department of Cytobiology and Proteomics, Medical University of Lodz, Poland.
Studzian M; Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland.
Pulaski L; Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland.
Babinska A; Department of Medicine, SUNY Downstate Medical Center, Brooklyn, New York, United States of America.
Swiatkowska M; Department of Cytobiology and Proteomics, Medical University of Lodz, Poland, .
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Źródło :
Frontiers in bioscience (Landmark edition) [Front Biosci (Landmark Ed)] 2018 Mar 01; Vol. 23, pp. 1612-1627. Date of Electronic Publication: 2018 Mar 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
Język :
English
Imprint Name(s) :
Publication: Irvine, CA : Frontiers in Bioscience
Original Publication: Searington, NY : Frontiers in Bioscience
MeSH Terms :
Endothelial Cells/*metabolism
Extracellular Space/*metabolism
Integrin beta3/*metabolism
Protein Disulfide-Isomerases/*metabolism
Actin Cytoskeleton/metabolism ; Cell Adhesion ; Cell Line ; Disulfides/metabolism ; Fibronectins/metabolism ; Humans ; Hybridomas ; Immunoblotting ; Microscopy, Confocal ; Polylysine/metabolism
Substance Nomenclature :
0 (Disulfides)
0 (Fibronectins)
0 (Integrin beta3)
25104-18-1 (Polylysine)
EC 5.3.4.1 (Protein Disulfide-Isomerases)
Entry Date(s) :
Date Created: 20180103 Date Completed: 20190128 Latest Revision: 20190923
Update Code :
20210210
DOI :
10.2741/4663
PMID :
29293453
Czasopismo naukowe
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.

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