Protein disulphide-isomerase from human placenta and rat liver. Purification and immunological characterization with monoclonal antibodies

Kaetzel, Charlotte S.; Rao, Chetana; Lamm, Michael E.

doi:10.1042/bj2410039

Cited by 64 publications

(36 citation statements)

References 34 publications

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“…I). This value is similar to that of mammalian POI, 7,8) and obviously different from that of yeast thioredoxin. 6 ) Our results clearly show that POI is present in yeast.…”

supporting

confidence: 60%

The Presence of Protein Disulfide Isomerase in the YeastSaccharomyces cerevisiae

Katakura

Mizunaga

Miura

et al. 1990

Agricultural and Biological Chemistry

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“…I). This value is similar to that of mammalian POI, 7,8) and obviously different from that of yeast thioredoxin. 6 ) Our results clearly show that POI is present in yeast.…”

supporting

confidence: 60%

The Presence of Protein Disulfide Isomerase in the YeastSaccharomyces cerevisiae

Katakura

Mizunaga

Miura

et al. 1990

Agricultural and Biological Chemistry

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“…mAb HP13 directed against human PDI (12) inhibited HIV infection of H9 cells by 83 ± 3.4% (Table 1). This inhibition was greater than expected, since the effect of HP13 on PDI activity was found to level off at 50o inhibition even at a 10-to 15-fold molar excess of mAb over antigen (12). This upper limit suggests, among other possibilities (12), that the mAb might bind to only one ofthe two active sites of soluble PDI (16).…”

Section: Inhibitorymentioning

confidence: 79%

“…HIViMiB and the H9 and C8166 cell lines were obtained from Martin Hirsch (Massachusetts General Hospital, Boston) and the U937 cell line was from Tun-Hou Lee (Harvard School of Public Health, Boston). The hybridomas producing mAbs against human PDI (HP13) and rat PDI (RL90) were a gift from Charlotte S. Kaetzel (University of Kentucky College of Medicine, Lexington) (12). The mAbs were purified from ascites fluid or conditioned medium and tested for anti-PDI activity as described (3).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction.

Ryser

Levy

Mandel

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

262

259

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The cell surface ofmammalian cells is capable of reductively cleaving disulfide bonds of exogenous membrane-bound macromolecules (for instance, the interchain disulfde of diphtheria toxin), and inhibiting this process with membrane-impermeant sulfhydryl reagents prevents diphtheria toxin cytotoxicity. More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thioldisulide interchange between its thiols and the disulfides of membrane-bound macromolecules. We provide evidence that the same reductive process plays a role in the penetration of membrane-bound human immunodeficiency virus (IHV) and show that HIV infection of human lymphoid cells is markedly inhibited by the membrane-impermeant sulfhydryl blocker 5,5'-dithiobis(2-nitrobenzoic acid), by bacitracin, and by anti-PDI antibodies. The results imply that HIV and its target cell engage in a thio-disulfide interchange mediated by PDI and that the reduction of critical disulfides in viral envelope glycoproteins may be the initial event that triggers conformational changes required for HIV entry and cell infection. These findings suggest additional approaches to impede cell infection by HIV.The surface of CHO cells has a reductive function capable of cleaving disulfide bonds of various membrane-bound macromolecules, and that cleavage is inhibited by the membraneimpermeant sulfhydryl reagents 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) and pCMBS (p-chloromercuriphenylsulfonic acid) (1,2). In one instance, cleavage was associated with the reductive activation of diphtheria toxin (DT), a disulfidecontaining protein that binds to a specific surface receptor and must undergo a reductive chain separation to exert its cytotoxicity. Both DTNB and pCMBS prevented DT cytotoxicity (2). More recent work showed (3) that monoclonal antibodies (mAbs) to protein disulfide-isomerase (PDI) and bacitracin, an inhibitor of PDI, cause similar inhibitions. PDI is an oxidoreductase capable of mediating thio-disulfide interchange reactions. It is present mostly in the endoplastic reticulum (4) but has also been detected at the surface of mammalian cells (5,6). Experiments based on the knowledge that DTNB inhibits DT cytotoxicity (2) and on the observation that the structure of the Sindbis virus envelope is maintained by disulfide bonds (7) showed that DTNB causes a significant inhibition of Sindbis infection of BHK cells (8,9). The viral glycoprotein gpl20 by which human immunodeficiency virus (HIV) attaches to its receptor CD4 also contains disulfide bonds (10). The events that follow HIV attachment and lead to viral infection are not yet fully understood (11). We postulated that the plasma membrane of human lymphoid cells would have a reductive function similar to that of CHO cells (3), and we reasoned that the reductive mechanism might cleave disulfides in membranebound gp120 and facilitate viral entry into cells. To dete...

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“…As shown in Figure 2A, the 2 mAbs used at 10 g/mL significantly enhanced the Xa generation on TF-EC, whereas the 2 polyclonal antibodies did not. In addition to RL-90 mAb, a reported inhibitor of PDI enzymatic activity in vitro 40,41 and in vivo, 14,29 we found that BD34 mAb was the most potent inhibitor in our screening. We used an insulin reduction assay to test the functional properties of BD34 mAb against purified bovine PDI ( Figure 2B).…”

mentioning

confidence: 83%

Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure

Popescu

Lupu

2010

Blood

111

115

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Tissue factor (TF) is the cellular receptor for plasma protease factor VIIa (FVIIa), and the TF-FVIIa complex initiates coagulation in both hemostasis and thrombosis. Cell surface-exposed TF is mainly cryptic and requires activation to fully exhibit the procoagulant potential. Recently, the protein disulfide isomerase (PDI) has been hypothesized to regulate TF decryption through the redox switch of an exposed disulfide in TF extracellular domain. In this study, we analyzed PDI contribution to coagulation using an in vitro endothelial cell model. In this model, extracellular PDI is detected by imaging and flow cytometry. Inhibition of cell surface PDI induces a marked increase in TF procoagulant function, whereas exogenous addition of PDI inhibits TF decryption. The coagulant effects of PDI inhibition were sensitive to annexin V treatment, suggesting exposure of phosphatidylserine (PS), which was confirmed by prothrombinase assays and direct labeling.In contrast, exogenous PDI addition enhanced PS internalization. Analysis of fluorescent PS revealed that PDI affects both the apparent flippase and floppase activities on endothelial cells. In conclusion, we identified a new mechanism for PDI contribution to coagulation on endothelial cells, namely, the regulation of PS exposure, where PDI acts as a negative regulator of coagulation. (Blood. 2010; 116(6):993-1001) IntroductionTissue factor (TF) is a transmembrane glycoprotein that binds with high affinity to the plasma protease factor VII in either zymogen (FVII) or activated form (FVIIa). The formation of the TF-FVIIa complex is crucial for initiation of coagulation, leading to thrombin generation and fibrin formation. Although the primary role of TF-FVIIa is to maintain hemostasis after vascular injury, aberrant activation of coagulation underlies thrombosis, the major cause of mortality in most industrialized countries. 1 In physiologic conditions, initiation of coagulation is maintained silent by restricting the exposure of TF to the plasma factors. 2,3 In pathologic conditions, however, TF may become exposed on the endothelium 4,5 and on circulating monocytes. 6 At these sites, TF can initiate thrombotic events associated with sepsis, 4,7 cancer, 8,9 or atherosclerosis. 10,11 Multiple in vitro studies have indicated that most of the cell-exposed TF is "cryptic," thus not fully active toward coagulation, 12,13 and TF "decryption" has been proposed as the initial step in the activation of coagulation. 14 Although the molecular mechanisms of TF decryption are not completely understood, many of the stimuli that decrypt TF also increase the exposure of phosphatidylserine (PS), [15][16][17][18] which is known to enhance coagulation. PS-independent mechanisms of TF decryption have also been postulated, such as TF self-association, 19 association with lipid rafts, [20][21][22] and the redox switch of an exposed disulfide in the membrane proximal domain of TF. 23 Protein disulfide isomerase (PDI) is an oxidoreductase 24 localized mainly in the endoplasmic reticulum (ER...

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Protein disulphide-isomerase from human placenta and rat liver. Purification and immunological characterization with monoclonal antibodies

Cited by 64 publications

References 34 publications

The Presence of Protein Disulfide Isomerase in the YeastSaccharomyces cerevisiae

The Presence of Protein Disulfide Isomerase in the YeastSaccharomyces cerevisiae

Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction.

Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure

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