2014
DOI: 10.3389/fchem.2014.00073
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Methods of measuring protein disulfide isomerase activity: a critical overview

Abstract: Protein disulfide isomerase is an essential redox chaperone from the endoplasmic reticulum (ER) and is responsible for correct disulfide bond formation in nascent proteins. PDI is also found in other cellular locations in the cell, particularly the cell surface. Overall, PDI contributes to ER and global cell redox homeostasis and signaling. The knowledge about PDI structure and function progressed substantially based on in vitro studies using recombinant PDI and chimeric proteins. In these experimental scenari… Show more

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Cited by 31 publications
(26 citation statements)
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“…Two broad categories of PDI assays have been employed [9,12,32,43,47,48]. The first involves the ability of PDI to catalyze the isomerization of mispaired disulfides in peptides and proteins.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Two broad categories of PDI assays have been employed [9,12,32,43,47,48]. The first involves the ability of PDI to catalyze the isomerization of mispaired disulfides in peptides and proteins.…”
Section: Resultsmentioning
confidence: 99%
“…~10 μM glutathione and cysteine [28,30,31]). Here, the susceptibility of PDI to inhibition by thiol directed reagents is expected to be strongly influenced by the presence of additional exofacial reductive pathways and thiol-containing proteins [32,33]. …”
Section: Introductionmentioning
confidence: 99%
“…The thermodynamic and kinetic contours of the isomerization process are still very scarce (30,56). It is known that the actual isomerization rate of PDI is lower than the rate of thiol-disulfide exchange reactions and that the relative efficiency of each catalytic site in PDI is dependent of the substrate and the synergistic effects in its environment (16,25,57).…”
Section: Gsh/gssg Buffer In Catalysis By Hpdimentioning
confidence: 99%
“…With sGLuc 100 n M rPDI leads to a 1600‐fold enhancement in the bioluminescent activity over a 2 h incubation. This unscrambling assay sGLuc should provide a convenient bioluminescent screening assay for the isomerase activity of rPDI to complement the more widely employed reductase‐based assays …”
Section: Resultsmentioning
confidence: 99%
“…sGLuc now provides a sensitive alternative protein substrate for the unscrambling activity of rPDI. This new method may provide a convenient complement to the widely employed assays based on the ability of the isomerase to promote reduction of disulfide‐containing terminal oxidants …”
Section: Discussionmentioning
confidence: 99%