Redox_proteomics_of_the_inflammatory_secretome_identifies_a_common_set_of_redoxins_and_other_glutathionylated_proteins_released_in_inflammation,_influenza_virus_infection_and_oxidative_stress.pdf (4.91 MB)
Redox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress
journal contribution
posted on 2023-06-08, 20:55 authored by Paola Checconi, Sonia Salzano, Lucas Bowler, Lisa MullenLisa Mullen, Manuela MengozziManuela Mengozzi, Eva-Maria Hanschmann, Christopher Horst Lillig, Rossella Sgarbanti, Simona Panella, Lucia Nencioni, Anna Teresa Palamara, Pietro GhezziProtein cysteines can form transient disulfides with glutathione (GSH), resulting in the production of glutathionylated proteins, and this process is regarded as a mechanism by which the redox state of the cell can regulate protein function. Most studies on redox regulation of immunity have focused on intracellular proteins. In this study we have used redox proteomics to identify those proteins released in glutathionylated form by macrophages stimulated with lipopolysaccharide (LPS) after pre-loading the cells with biotinylated GSH. Of the several proteins identified in the redox secretome, we have selected a number for validation. Proteomic analysis indicated that LPS stimulated the release of peroxiredoxin (PRDX) 1, PRDX2, vimentin (VIM), profilin1 (PFN1) and thioredoxin 1 (TXN1). For PRDX1 and TXN1, we were able to confirm that the released protein is glutathionylated. PRDX1, PRDX2 and TXN1 were also released by the human pulmonary epithelial cell line, A549, infected with influenza virus. The release of the proteins identified was inhibited by the anti-inflammatory glucocorticoid, dexamethasone (DEX), which also inhibited tumor necrosis factor (TNF)-a release, and by thiol antioxidants (N-butanoyl GSH derivative, GSH-C4, and N-acetylcysteine (NAC), which did not affect TNF-a production. The proteins identified could be useful as biomarkers of oxidative stress associated with inflammation, and further studies will be required to investigate if the extracellular forms of these proteins has immunoregulatory functions.
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- Published
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- Published version
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PLoS ONEISSN
1932-6203Publisher
Public Library of ScienceExternal DOI
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5Volume
10Article number
e0127086Department affiliated with
- Clinical and Experimental Medicine Publications
Full text available
- Yes
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- Yes
Legacy Posted Date
2015-06-01First Open Access (FOA) Date
2015-06-01First Compliant Deposit (FCD) Date
2015-06-01Usage metrics
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