Faculty Opinions recommendation of Protein disulfide-isomerase mediates delivery of nitric oxide redox derivatives into platelets.

2007 ◽  
Author(s):  
Peter Taylor
Keyword(s):  
Nitric Oxide ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Protein disulfide isomerase regulation by nitric oxide maintains vascular quiescence and controls thrombus formation

2018 ◽  
Vol 16 (11) ◽  
pp. 2322-2335 ◽  
Author(s):  
R. H. Bekendam ◽  
D. Iyu ◽  
F. Passam ◽  
J. D. Stopa ◽  
K. De Ceunynck ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Disulfide Isomerase ◽  
Thrombus Formation ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Nitric Oxide Mediates Selective Degeneration of Hypothalamic Orexin Neurons through Dysfunction of Protein Disulfide Isomerase

2013 ◽  
Vol 33 (31) ◽  
pp. 12557-12568 ◽  
Author(s):  
K. Obukuro ◽  
M. Nobunaga ◽  
M. Takigawa ◽  
H. Morioka ◽  
A. Hisatsune ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Coagulation factor XIII serves as protein disulfide isomerase

2009 ◽  
Vol 101 (05) ◽  
pp. 840-844 ◽  
Author(s):  
Zsuzsa Bagoly ◽  
Vera Sheptovitsky ◽  
Rima Dardik ◽  
Judith Lahav ◽  
Eli Karniel ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Disulfide Isomerase ◽  
Factor Xiii ◽  
Tissue Transglutaminase ◽  
Coagulation Factor ◽  
Disulfide Isomerase ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Bond Rearrangement ◽  
Protein Disulfide

SummaryTissue transglutaminase was reported to act as protein disulfide isomerase (PDI). We studied whether plasma transglutaminase – coagulation factor XIII (FXIII) – has PDI activity as well. PDI activity was measured by determining the ability to renature reduced-denatured RNase (rdRNase). We found that FXIII can re-nature rdRNase, with efficiency comparable to commercial PDI. This PDI activity was inhibited by bacitracin. Like tissue transglu-taminase, FXIII-mediated PDI activity is independent of its transglutaminase activity and is located on the A subunit. Surface-associated PDI has been previously shown to catalyse two distinct functions: transnitrosation with subsequent release of intracellular nitric oxide and disulfide bond rearrangement during platelet integrin ligation. Our results imply that FXIII-PDI activity may have a role in platelet function.

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