Protein disulfide isomerase (PDI) has two distinct CGHC redox-active sites; however, the contribution of these sites during different physiologic reactions, including thrombosis, is unknown. Here, we evaluated the role of PDI and redox-active sites of PDI in thrombosis by generating mice with blood cells and vessel wall cells lacking PDI (Mx1-Cre Pdifl/fl mice) and transgenic mice harboring PDI...

background: biofilm infections are a major challenge in medical practice. bacteria that live in a biofilm phenotype are more resistant to both antimicrobial therapy and host immune responses compared to their planktonic counterparts. so, there is need for new therapeutic strategies to combat these infections. a promising approach [known as photodynamic inactivation (pdi)] to kill bacteria growi...

1. When pDj < pDi, the demand allocation is xDj = min{max{QD(pDj )− θj , QD(pDj )− yS , 0}, yDj}, (A1a) xDi = min{max{QD(pDi)− yDj − θi, QD(pDi)− yDj − yS , 0}, yDi}, (A1b) xS = min{max{QD(pDi)− yDi − yDj , θi},max{QD(pDj )− yDj , θj}, yS}. (A1c) 2. When pD2 = pD1, the demand allocation is xDi = min { max { QD(pDi)− θi 2 , QD(pDi)− yS 2 , QD(pDi)− θi − yDj , QD(pDi)− yS − yDj , 0 } , yDi} , (A2...

In eukaryotic cells, protein disulfide isomerase (PDI) found in the endoplasmic reticulum (ER) catalyzes disulfide bond exchange and assists in protein folding of newly synthesized proteins. PDI also functions as a molecular chaperone and has been found associated with proteins in the ER. In addition, PDI functions as a subunit of two more complex enzyme systems: the prolyl-4-hydroxylase and th...

Coexpression of the enzyme, protein disulfide isomerase (PDI), has been shown to increase soluble and secreted IgG levels from baculovirus-infected insect cells (Hsu, T.-A., Watson, S., Eiden, J. J., and Betenbaugh, M. J. (1996) Protein Expression Purif. 7, 281-288). PDI is known to include catalytic active sites in two separate thioredoxin-like domains, one near the amino terminus and another ...

Analysis of previously reported [((Ph2PPr)PDI)MoI][I] by cyclic voltammetry revealed a reversible wave at -1.20 V vs. Fc(+/0), corresponding to the Mo(ii)/Mo(i) redox couple. Reduction of [((Ph2PPr)PDI)MoI][I] using stoichiometric K/naphthalene resulted in ligand deprotonation rather than reduction to yield a Mo(ii) monoiodide complex featuring a Mo-C bond to the α-position of one imine substit...

Protein disulfide isomerase (PDI) derived from intravascular cells is required for thrombus formation. However, it remains unclear whether platelet PDI contributes to the process. Using platelet-specific PDI-deficient mice, we demonstrate that PDI-null platelets have defects in aggregation and ATP secretion induced by thrombin, collagen, and ADP. Such defects were rescued by exogenously-added w...

Protein disulfide isomerase (PDI) is an abundant protein primarily found in the endoplasmic reticulum and also secreted into the blood by a variety of vascular cells. The evidence obtained here, suggests that PDI could directly participate in the efflux of NO(+) from red blood cells (RBC). PDI was detected both in RBC membranes and in the cytosol. PDI was S-nitrosylated when RBCs were exposed t...

BACKGROUND Protein disulfide isomerase (PDI), is sorted to be enzymatic chaperone for reconstructing misfolded protein in endoplasmic reticulum lumen. Recently, PDI has been identified as a link between misfolded protein and neuron apoptosis. However, the potential for PDI to be involved in the pathogenesis of prion disease remains unknown. In this study, we propose that PDI may function as a p...