Interleukin-10 Inhibits Lipopolysaccharide-induced Tumor Necrosis Factor-α Translation through a SHIP1-dependent Pathway
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Production of the proinflammatory cytokine TNFα by activated macrophages is an important component of host defense. However, TNFα production must be tightly controlled to avoid pathological consequences. The anti-inflammatory cytokine IL-10 inhibits TNFα mRNA expression through activation of the STAT3 transcription factor pathway and subsequent expression of STAT3-dependent gene products. We hypothesized that IL-10 must also have more rapid mechanisms of action and show that IL-10 rapidly shifts existing TNFα mRNA from polyribosome-associated polysomes to monosomes. This translation suppression requires the presence of SHIP1 (SH2 domain-containing inositol 5'-phosphatase 1) and involves inhibition of Mnk1 (MAPK signal-integrating kinase 1). Furthermore, activating SHIP1 using a small-molecule agonist mimics the inhibitory effect of IL-10 on Mnk1 phosphorylation and TNFα translation. Our data support the existence of an alternative STAT3-independent pathway through SHIP1 for IL-10 to regulate TNFα translation during the anti-inflammatory response.
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In macrophages, IL-10 suppresses TNF-α secretion, which is promoted by both phosphatase-dependent and -independent activities of SHIP1.
“In macrophages, the anti-inflammatory cytokine IL-10 can suppress TNF-α secretion, which is promoted by both phosphatase-dependent and -independent activities of SHIP1 [131–133].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [132]
The Results (Fig. 1C; page unavailable) report reduced TNF-α protein in macrophage culture supernatants after IL-10 treatment, and the SHIP1 results show that IL-10’s suppression of TNF-α translation requires SHIP1. The paper describes a SHIP1 agonist that stimulates phosphatase activity, but it does not establish a phosphatase-independent contribution to the suppression. (LLM, conf=0.88)
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etabolisme mitochondrial et peroxysomal des acides gras et sur l'inammation
Kebbaj, R. E. (2014)
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Self-citation
- Authors
- Chan, C. S., Ming-Lum, A., Golds, G. B., Lee, S. J., Anderson, R. J., & Mui, A. L.-F.
- Affiliations
- University of British Columbia (CA)
- Corresponding author
- Mui, Alice L.-F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-11
- Volume
- 287
- Issue
- 45
- Pages
- 38020-38027
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3488072
- OpenAlex
- W1974952444
- Cited by
- 52
- References
- 46
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 4 · 2022: 2 · 2021: 6 · 2020: 5 · 2019: 1 · 2018: 5 · 2017: 1 · 2016: 10 · 2015: 4 · 2014: 2 · 2013: 3 · 2012: 1
- FWCI
- 1.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Michael Smith Health Research BC
- Canadian Institutes of Health Research (84539_1)
- Canadian Cancer Society Research Institute (017289)
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- IL-10, TNF-α, SHIP1, MNK1, translational regulation, lipopolysaccharide, macrophages, anti-inflammatory cytokines
- MeSH terms
- Inositol Polyphosphate 5-Phosphatases, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Animals, Cell Line, Cells, Cultured, Female, Lipopolysaccharides, Macrophages, Mice, Inbred BALB C, Phosphoric Monoester Hydrolases, Phosphorylation, Polyribosomes, RNA, Messenger, Protein Biosynthesis, Tumor Necrosis Factor-alpha, Immunoblotting, Signal Transduction, Interleukin-10, Protein Serine-Threonine Kinases, Mice, Knockout, RNA Interference, Mice
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