Ablation of the Thiol Transferase Glutaredoxin-1 Augments Protein <i>S</i>-Glutathionylation and Modulates Type 2 Inflammatory Responses and IL-17 in a House Dust Mite Model of Allergic Airway Disease in Mice

Hoffman, Sidra M.; Nolin, James D.; Jones, Jane T.; Lahue, Karolyn G.; Chapman, David G.; Aliyeva, Minara; Daphtary, Nirav; Lundblad, Lennart K. A.; Abdalla, Sarah; Ather, Jennifer L.; Ho, Ye-Shih; Irvin, Charles G.; Anathy, Vikas; Wouters, Emiel F.M.; Poynter, Matthew E.; Janssen–Heininger, Yvonne M. W.

doi:10.1513/annalsats.201510-656mg

Cited by 9 publications

(2 citation statements)

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“…Glutaredoxin-1 is a small cytosolic thioltransferase that controls a reversible protein thiol modification, S-glutationylation (protein-GSH adducts), thereby regulating redox signaling. Glutaredoxin-1 deletion enhances GSH adduct formation on key signaling proteins and decreases pro-inflammatory cytokine release in alveolar macrophages. , …”

Section: Resultsmentioning

confidence: 99%

“…Glutaredoxin-1 deletion enhances GSH adduct formation on key signaling proteins and decreases proinflammatory cytokine release in alveolar macrophages. 31,32 In addition, ELISA was conducted to validate the presence of allergenic proteins in the collected eluate by a third party (Oumarsi Biotechnology Co., Ltd., Shanghai, China) (https:// www.oumarsi.com/). Following the experimental procedures described in Materials and Methods, the potential allergens in crucian carp sarcoplasmic protein extracts were captured by using the serum of an allergic patient, S1, and eluted, and the obtained eluate was taken for fish parvalbumin ELISA test.…”

Section: Identification Of Potential Allergens In Crucian Carp Sarcop...mentioning

confidence: 99%

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Microfluidic Chip Coupled with MALDI-TOF MS for Multitarget Detection of Allergens in Crucian Carp (Carassius auratus)

Xu,

Qin,

2024

J. Agric. Food Chem.

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The goal of the present study was to establish a rapid, simple method for simultaneous allergy testing of sera from multiple fish-allergic patients. Sera from fish-allergic patients were pooled and used for capturing allergens in fish muscle of crucian carp (Carassius auratus), which was studied as a fish model. Sarcoplasmic proteins of crucian carp (Carassius auratus) were extracted for the analysis of allergens. Anti-human IgE antibody−functionalized magnetic beads were utilized to collect IgE antibodies from human pooled sera. The isolation of allergenic proteins was immunomagnetically performed in microfluidic channels, and the elution of the captured allergenic proteins was done with 5% (v/v) acetic acid aqueous solution. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and peptide mass fingerprinting were used for the analysis of tryptic digests of eluted proteins. Ten potential allergenic proteins were identified from crucian carp (Carassius auratus). The present protocol provides a rapid, efficient, and simple method for simultaneous detection of multiple allergens, based on multitargeted antibodies from pooled sera of allergic patients. The constructed multiple antibody-modified MBs can be applied for the deallergenicity of food matrices. The efficiency of allergen detection can be greatly improved, with promising application in allergen discovery and filtration for other muscle-based foods.

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Section: Resultsmentioning

confidence: 99%

Section: Identification Of Potential Allergens In Crucian Carp Sarcop...mentioning

confidence: 99%

Microfluidic Chip Coupled with MALDI-TOF MS for Multitarget Detection of Allergens in Crucian Carp (Carassius auratus)

Xu,

Qin,

2024

J. Agric. Food Chem.

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Protein S-glutathionylation and the regulation of cellular functions

2020

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An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation

Zhang

Singh

et al. 2018

Free Radical Biology and Medicine

128

103

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By nature of the reversibility of the addition of glutathione to low pKa cysteine residues, the post-translational modification of S-glutathionylation sanctions a cycle that can create a conduit for cell signaling events linked with cellular exposure to oxidative or nitrosative stress. The modification can also avert proteolysis by protection from over-oxidation of those clusters of target proteins that are substrates. Altered functions are associated with S-glutathionylation of proteins within the mitochondria and endoplasmic reticulum compartments, and these impact energy production and protein folding pathways. The existence of human polymorphisms of enzymes involved in the cycle (particularly glutathione S-transferase P) create a scenario for inter-individual variance in response to oxidative stress and a number of human diseases with associated aberrant S-glutathionylation have now been identified.

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Ablation of the Thiol Transferase Glutaredoxin-1 Augments Protein S-Glutathionylation and Modulates Type 2 Inflammatory Responses and IL-17 in a House Dust Mite Model of Allergic Airway Disease in Mice

Abstract: Author disclosures are available with the text of this article at www.atsjournals.org.

Cited by 9 publications

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Microfluidic Chip Coupled with MALDI-TOF MS for Multitarget Detection of Allergens in Crucian Carp (Carassius auratus)

Microfluidic Chip Coupled with MALDI-TOF MS for Multitarget Detection of Allergens in Crucian Carp (Carassius auratus)

Protein S-glutathionylation and the regulation of cellular functions

An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation

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