Redox-control of the alarmin, Interleukin-1α
Open accessAbstract
The pro-inflammatory cytokine Interleukin-1α (IL-1α) has recently emerged as a susceptibility marker for a wide array of inflammatory diseases associated with oxidative stress including Alzheimer's, arthritis, atherosclerosis, diabetes and cancer. In the present study, we establish that expression and nuclear localization of IL-1α are redox-dependent. Shifts in steady-state H2O2 concentrations (SS-[H2O2]) resulting from enforced expression of manganese superoxide dismutase (SOD2) drive IL-1α mRNA and protein expression. The redox-dependent expression of IL-1α is accompanied by its increased nuclear localization. Both IL-1α expression and its nuclear residency are abrogated by catalase co-expression. Sub-lethal doses of H2O2 also cause IL-1α nuclear localization. Mutagenesis revealed IL-1α nuclear localization does not involve oxidation of cysteines within its N terminal domain. Inhibition of the processing enzyme calpain prevents IL-1α nuclear localization even in the presence of H2O2. H2O2 treatment caused extracellular Ca(2+) influx suggesting oxidants may influence calpain activity indirectly through extracellular Ca(2+) mobilization. Functionally, as a result of its nuclear activity, IL-1α overexpression promotes NF-kB activity, but also interacts with the histone acetyl transferase (HAT) p300. Together, these findings demonstrate a mechanism by which oxidants impact inflammation through IL-1α and suggest that antioxidant-based therapies may prove useful in limiting inflammatory disease progression.
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The cellular redox state mediates IL-1α expression and processing through the Ca2+-dependent protease calpain and alterations in Ca2+ homeostasis.
“redox-engineered fibrosarcoma cells were used to demonstrate that the cellular redox state mediates IL-1α expression and processing through the Ca2+ dependent protease calpain and alterations in calcium (Ca2+) homeostasis”
From Redox control of senescence and age-related disease. (2017) · cites this paper as [129]
Steady state levels of intracellular H2O2 promote IL-1α expression and nuclear translocation, where it serves as a pro-inflammatory mediator by increasing NF-κB activity.
“Steady state levels of intracellular hydrogen peroxide (H2O2) significantly promoted IL-1α expression and nuclear translocation, where it serves as a pro-inflammatory mediator by increasing NF-κB activity”
From Redox control of senescence and age-related disease. (2017) · cites this paper as [129]
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- Authors
- McCarthy, D. A., Ranganathan, A., Subbaram, S., Flaherty, N. L., Patel, N., Trebak, M., Hempel, N., & Melendez, J. A.
- Affiliations
- University at Albany, State University of New York (US)
- University of Arizona College of Medicine- Phoenix (US)
- Albany Medical College (US)
- Venue
- Redox Biology
- Publisher
- Elsevier BV
- Published
- 2013
- Volume
- 1
- Issue
- 1
- Pages
- 218-225
- ISSN
- 2213-2317 (ISSN-L)
- PMC
- PMC3757693
- OpenAlex
- W2063169852
- Cited by
- 35
- References
- 43
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 5 · 2015: 2 · 2014: 3 · 2013: 2
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Redox Biology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Public Health Service (AG031067)
- National Institute of Aging
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Keywords
- interleukin-1 alpha, redox regulation, hydrogen peroxide, manganese superoxide dismutase, catalase, nuclear localization, calpain, extracellular calcium influx, NF-kB, P300, histone acetyltransferase, oxidative stress, inflammation, antioxidant therapy, cysteine oxidation
- MeSH terms
- Superoxide Dismutase 2, Calcium, Calpain, Cell Nucleus, Cysteine, Fibrosarcoma, Humans, Hydrogen Peroxide, Oxidation-Reduction, Superoxide Dismutase, NF-kappa B, Cell Line, Tumor, E1A-Associated p300 Protein, Interleukin-1alpha, HEK293 Cells
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