Endothelial cell surface expression of protein disulfide isomerase activates β1 and β3 integrins and facilitates dengue virus infection

2011 ◽  
pp. n/a-n/a ◽  
Author(s):  
Shu-Wen Wan ◽  
Chiou-Feng Lin ◽  
Yi-Tien Lu ◽  
Huan-Yao Lei ◽  
Robert Anderson ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Virus Infection ◽  
Cell Surface ◽  
Protein Disulfide Isomerase ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Dengue Virus Infection ◽  
Disulfide Isomerase ◽  
Endothelial Cell Surface ◽  
Protein Disulfide

scholarly journals Urate hydroperoxide oxidizes endothelial cell surface protein disulfide isomerase-A1 and impairs adherence

2020 ◽  
Vol 1864 (3) ◽  
pp. 129481
Author(s):  
Marcela Franco Mineiro ◽  
Eliziane de Souza Patricio ◽  
Álbert Souza Peixoto ◽  
Thaís Larissa Silva Araujo ◽  
Railmara Pereira da Silva ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Surface ◽  
Protein Disulfide Isomerase ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Disulfide Isomerase ◽  
Endothelial Cell Surface ◽  
Protein Disulfide

Characterization of porcine UL16-binding protein 1 endothelial cell surface expression

2008 ◽  
Vol 15 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Benjamin G. Lilienfeld ◽  
Anita Schildknecht ◽  
Lukas L. Imbach ◽  
Nicolas J. Mueller ◽  
Mårten K. J. Schneider ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Surface ◽  
Binding Protein ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Endothelial Cell Surface

Time course of recovery of endothelial cell surface thrombin receptor (PAR-1) expression

1999 ◽  
Vol 276 (1) ◽  
pp. C38-C45 ◽  
Author(s):  
Chad A. Ellis ◽  
Chinnaswamy Tiruppathi ◽  
Raudel Sandoval ◽  
Walter D. Niles ◽  
Asrar B. Malik
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Cell Surface ◽  
Electrical Resistance ◽  
Time Course ◽  
De Novo ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Thrombin Receptor ◽  
Endothelial Cell Surface

We studied dynamics of cell surface expression of proteolytically activated thrombin receptor (PAR-1) in human pulmonary artery endothelial cells (HPAEC). PAR-1 activation was measured by changes in cytosolic calcium concentration ([Ca2+]i) and HPAEC retraction response (determined by real-time transendothelial monolayer electrical resistance). [Ca2+]iincrease in response to thrombin was abolished by preexposure to 25 nM thrombin for >60 min, indicating PAR-1 desensitization, but preexposure to 25 nM thrombin for only 30 min or to 10 nM thrombin for up to 2 h did not desensitize PAR-1. Exposure to 10 or 25 nM thrombin decreased monolayer electrical resistance 40–60%. Cells preexposed to 10 nM thrombin, but not those preexposed to 25 nM thrombin, remained responsive to thrombin 3 h later. Loss of cell retractility was coupled to decreased cell surface PAR-1 expression as determined by immunofluorescence. Cell surface PAR-1 disappeared upon short-term (30 min) thrombin exposure but reappeared within 90 min after incubation in thrombin-free medium. Exposure to 25 nM thrombin for >60 min prevented rapid cycloheximide-insensitive PAR-1 reappearance. Cycloheximide-sensitive recovery of cell surface PAR-1 expression required 18 h. Therefore, both duration and concentration of thrombin exposure regulate the time course of recovery of HPAEC surface PAR-1 expression. The results support the hypothesis that initial recovery of PAR-1 surface expression in endothelial cells results from a rapidly mobilizable PAR-1 pool, whereas delayed recovery results from de novo PAR-1 synthesis. We conclude that thrombin itself regulates endothelial cell surface PAR-1 expression and that decreased surface expression interferes with thrombin-induced endothelial cell activation responses.

Protein disulfide isomerase induces endothelial cell dysfunction

2007 ◽  
Vol 205 (3) ◽  
pp. S32-S33
Author(s):  
Danielle B. Peterson ◽  
Deron Jones ◽  
Jing-Song Ou ◽  
John Densmore ◽  
Sushma Kaul ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Protein Disulfide Isomerase ◽  
Endothelial Cell Dysfunction ◽  
Disulfide Isomerase ◽  
Cell Dysfunction ◽  
Protein Disulfide

scholarly journals Thiol/Disulfide Exchange Is Required for Membrane Fusion Directed by the Newcastle Disease Virus Fusion Protein

2006 ◽  
Vol 81 (5) ◽  
pp. 2328-2339 ◽  
Author(s):  
Surbhi Jain ◽  
Lori W. McGinnes ◽  
Trudy G. Morrison
Keyword(s):  
Cell Surface ◽  
Newcastle Disease Virus ◽  
Newcastle Disease ◽  
Fusion Proteins ◽  
Protein Disulfide Isomerase ◽  
Viral Fusion ◽  
Disulfide Isomerase ◽  
F Protein ◽  
Viral Fusion Proteins ◽  
Protein Disulfide

ABSTRACT Newcastle disease virus (NDV), an avian paramyxovirus, initiates infection with attachment of the viral hemagglutinin-neuraminidase (HN) protein to sialic acid-containing receptors, followed by fusion of viral and cell membranes, which is mediated by the fusion (F) protein. Like all class 1 viral fusion proteins, the paramyxovirus F protein is thought to undergo dramatic conformational changes upon activation. How the F protein accomplishes extensive conformational rearrangements is unclear. Since several viral fusion proteins undergo disulfide bond rearrangement during entry, we asked if similar rearrangements occur in NDV proteins during entry. We found that inhibitors of cell surface thiol/disulfide isomerase activity—5′5-dithio-bis(2-nitrobenzoic acid) (DTNB), bacitracin, and anti-protein disulfide isomerase antibody—inhibited cell-cell fusion and virus entry but had no effect on cell viability, glycoprotein surface expression, or HN protein attachment or neuraminidase activities. These inhibitors altered the conformation of surface-expressed F protein, as detected by conformation-sensitive antibodies. Using biotin maleimide (MPB), a reagent that binds to free thiols, free thiols were detected on surface-expressed F protein, but not HN protein. The inhibitors DTNB and bacitracin blocked the detection of these free thiols. Furthermore, MPB binding inhibited cell-cell fusion. Taken together, our results suggest that one or several disulfide bonds in cell surface F protein are reduced by the protein disulfide isomerase family of isomerases and that F protein exists as a mixture of oxidized and reduced forms. In the presence of HN protein, only the reduced form may proceed to refold into additional intermediates, leading to the fusion of membranes.

Cell Surface Protein Disulfide-Isomerase Is Involved in the Shedding of Human Thyrotropin Receptor Ectodomain†

Biochemistry ◽  
1996 ◽  
Vol 35 (47) ◽  
pp. 14800-14805 ◽  
Author(s):  
Jacques Couët ◽  
Simon de Bernard ◽  
Hugues Loosfelt ◽  
Bertrand Saunier ◽  
Edwin Milgrom ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protein Disulfide Isomerase ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Thyrotropin Receptor ◽  
Disulfide Isomerase ◽  
Protein Disulfide
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