2020
DOI: 10.3390/antiox9040315
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Immunological Techniques to Assess Protein Thiol Redox State: Opportunities, Challenges and Solutions

Abstract: To understand oxidative stress, antioxidant defense, and redox signaling in health and disease it is essential to assess protein thiol redox state. Protein thiol redox state is seldom assessed immunologically because of the inability to distinguish reduced and reversibly oxidized thiols by Western blotting. An underappreciated opportunity exists to use Click PEGylation to realize the transformative power of simple, time and cost-efficient immunological techniques. Click PEGylation harnesses selective, bio-orth… Show more

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Cited by 22 publications
(23 citation statements)
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“…A modern, underappreciated opportunity exists to use Click PEGylation to realize the transformative power of simple, time and cost-efficient immunological techniques. Click PEGylation harnesses selective, bio-orthogonal Click chemistry to separate reduced and reversibly oxidized thiols by selectively ligating a low molecular weight polyethylene glycol moiety to the redox state of interest [55].…”
Section: Discussionmentioning
confidence: 99%
“…A modern, underappreciated opportunity exists to use Click PEGylation to realize the transformative power of simple, time and cost-efficient immunological techniques. Click PEGylation harnesses selective, bio-orthogonal Click chemistry to separate reduced and reversibly oxidized thiols by selectively ligating a low molecular weight polyethylene glycol moiety to the redox state of interest [55].…”
Section: Discussionmentioning
confidence: 99%
“…Protein thiol oxidation : Redox proteomics approaches are useful to measure protein thiol oxidation in a systematic high-throughput manner [ 175 , 176 , 177 , 178 , 179 ]. Immunological techniques (e.g., Click PEGylation) can also be used to assess the redox state of a protein of interest by Western blotting [ 180 , 181 , 182 , 183 ].…”
Section: How Mitochondria Produce Superoxide In Art: the Unknownmentioning
confidence: 99%
“…While fertilization is well known to increase H 2 O 2 production in sea urchins [ 271 , 272 , 273 ], Amaya’s group [ 274 ] recently tied fertilization triggered Ca 2+ -induced mitochondrial ROS release to the regulation of the embryonic cell cycle via reversible cdc25c oxidation in Xenopus laevis . By tying mitochondrial ROS to the early cell cycle via thiol oxidation, their work provides a precedent to reimagine the 2-cell block as increased thiol oxidation of regulatory cell cycle proteins [ 183 ] (see Figure 7 ). Consistent with this, reversing protein thiol oxidation may explain the ability of recombinant thioredoxin to release the 2-cell block [ 22 , 261 , 275 , 276 ].…”
Section: A Framework For Interpreting the Role Of Mitochondrial Romentioning
confidence: 99%
See 1 more Smart Citation
“…ROS include chemically heterogeneous free radicals (e.g., superoxide) and non-radicals (e.g., hydrogen peroxide) vital for cell development, survival and signaling [6] . Redox signaling occurs through posttranslational oxidation of proteins (e.g., cysteine residues) [7,8] . Moreover, there is also a known cross-talk between ROS and neutrophil inflammation clearance and pro-inflammatory markers [5,9] .…”
Section: Introductionmentioning
confidence: 99%