2016
DOI: 10.17554/j.issn.2313-7177.2016.02.29
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Protein Disulfide Isomerase: Structure, Mechanism of Oxidative Protein Folding and Multiple Functional Roles

Abstract: Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily of redox proteins. Originally, PDI was identified in the lumen of the endoplasmic reticulum and subsequently detected abundantly in many other tissues and account for 0.8% of total cellular protein. PDI consists of four tandem thioredoxinlike domains a, b, b′, and a′ plus a C-terminal extension which are arranged into a U-shape structure. PDI has three catalytic activities including, thiol-disulfide oxidoreductase, disulfide isomerase… Show more

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Cited by 7 publications
(4 citation statements)
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References 69 publications
(106 reference statements)
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“…Several studies have shown that PDI has physiological roles in the diseases such as diabetes, cardiovascular diseases, cancer, neurodegenerative conditions as well as in the entry of pathogen in infectious diseases like HIV‐1 103 . The exact role remains unclear but it has been shown that PDI is upregulated into infected cells; overexpression of PDI has been shown to increase the fusion of viral membrane into the host cell in the case of HIV‐1 103 . PDI relies on many signals for activation, with vitamin D being one of these signaling molecules.…”
Section: Vitamin D's Impact On the Function And Regulation Of Thioredoxin And Protein Disulfide Isomerasementioning
confidence: 99%
“…Several studies have shown that PDI has physiological roles in the diseases such as diabetes, cardiovascular diseases, cancer, neurodegenerative conditions as well as in the entry of pathogen in infectious diseases like HIV‐1 103 . The exact role remains unclear but it has been shown that PDI is upregulated into infected cells; overexpression of PDI has been shown to increase the fusion of viral membrane into the host cell in the case of HIV‐1 103 . PDI relies on many signals for activation, with vitamin D being one of these signaling molecules.…”
Section: Vitamin D's Impact On the Function And Regulation Of Thioredoxin And Protein Disulfide Isomerasementioning
confidence: 99%
“…This observation was in accordance with in vitro studies (Figures a,b and S22a,b). Cancer cells necessitate overexpressed PDI to encounter ER stress and surge in protein synthesis to endure rapid proliferation. ,, Considering the overexpression of PDI in melanoma cells, the quenching effect was more prominent in B16F10 than that in NIH3T3 (noncancerous) cells, which was evident from the corresponding flow cytometry data (Figure S34c,f). The mean fluorescence intensity of NINSS FONPs after 24 h incubation was very low, 189 and 47 for NIH3T3 and B16F10 cells, respectively (Figure S34c,f).…”
Section: Resultsmentioning
confidence: 83%
“…Being a member of the thioredoxin superfamily, protein disulfide isomerase (PDI) is a 57 kDa dithiol–disulfide oxidoreductase with molecular chaperone functions that maintain cellular homeostasis. , PDI, overexpressed in the endoplasmic reticulum (ER), serves as the primary catalyst for protein folding by mediating the formation, cleavage, and rearrangement of disulfide. , In ER, PDI acts as an oxidase that forms disulfide bonds in nascent secretory proteins. , Alternatively, PDI reduces disulfide bonds of target proteins on cell surfaces and in the cytoplasm or endosomes. The oxidized state has more open conformation that allows the entry of chaperone substrates, while the reduced state has closed conformation that inhibits their entry during protein folding. , PDI is actively involved in the proliferation, survival, and metastasis of several cancers through participation in cellular processes including unfolded protein response (UPR) signaling and apoptosis. ,, Considering its pivotal role in physiological behavior, the selective diagnosis of PDI at its varying redox state would be very crucial. To date, a variety of assays have been developed to monitor PDI activity .…”
Section: Introductionmentioning
confidence: 99%
“…The canonical PDI gene (mammalian PDIA1) encodes a protein consisting of four sequential domains (a-b-b'-a'). The a and a' domains possess the catalytic (redox-active) motif sharing homology to thioredoxin, whereas the b and b' domains are redox-inactive thioredoxin-fold domains (Yuen et al, 2013;Khan et al, 2016).…”
Section: Introductionmentioning
confidence: 99%