The macrophage-specific transcription factor can be modified posttranslationally by ubiquitination in the lipopolysaccharide-treated macrophages
Open accessAbstract
Background: Macrophages are one of the most important inflammatory cells in innate immunity.PU.1 is a macrophage-specific transcription factor.Ubiquitins are the ultimate regulator of eukaryotic transcription.The ubiquitination process for PU.1 is unknown.This study investigated the lipopolysaccharide (LPS)-induced activation of PU.1 and its relation to ubiquitins in the macrophages.Methods: Raw264.7 cells, the primary cultured alveolar, pulmonary, and bone marrow derived macrophages were used.The Raw264.7 cells were treated with MG-132, NH 4 Cl, lactacytin and LPS.Nitric oxide and prostaglandin D2 and E2 were measured.Immunoprecipitation and Western blots were used to check ubiquitination of PU.1.Results: The PU.1 ubiquitination increased after LPS (1μg/mL) treatment for 4 hours on Raw264.7 cells.The ubiquitination of PU.1 by LPS was increased by MG-132 or NH 4 Cl pretreatment.Two hours of LPS treatment on macrophages, PU.1 activation was not induced nor increased with the inhibition of proteasomes and/or lysosomes.The ubiquitination of PU.1 was increased in LPS-treated Raw264.7 cells at 12-and at 24 hours.LPS-treated cells increased nitric oxide production, which was diminished by MG-132 or NH 4 Cl.LPS increased the production of PGE2 in the alveolar and peritoneal macrophages of wild type mice; however, PGE2 was blocked or diminished in Rac2 null mice.Pretreatment of lactacystin increased PGE 2 , however it decreased the PGD 2 level in the macrophages derived from the bone marrow of B57/BL6 mice.Conclusion: LPS treatment in the macrophages ubiquitinates PU.1.Ubiquitination of PU.1 may be involved in synthesis of nitric oxide and prostaglandins.
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Lipopolysaccharide regulates PU.1 at protein levels in macrophages.
“In another study, it was shown that lipopolysaccharide also regulated PU.1 at protein levels in macrophages (50).”
From FBW7 Inhibits Myeloid Differentiation in Acute Myeloid Leukemia via GSK3-Dependent Ubiquitination of PU.1 (2021) · cites this paper as [50]
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- Authors
- Jung, J. W., Choi, J. C., Kim, J. Y., Park, I. W., Choi, B. W., Shin, J. W., & Christman, J. W.
- Affiliations
- Chung-Ang University Healthcare System (KR)
- University of Illinois Chicago (US)
- Venue
- Tuberculosis and Respiratory Diseases
- Published
- 2011
- Volume
- 70
- Issue
- 2
- Pages
- 113
- ISSN
- 0378-0066 (ISSN-L)
- 1738-3536
- OpenAlex
- W2153046081
- Cited by
- 2
- References
- 30
- Citations by year
- 2020: 1 · 2013: 1
- FWCI
- 0.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Tuberculosis & respiratory diseases (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- PU.1, ubiquitination, macrophages, lipopolysaccharide, transcription factor regulation, nitric oxide, prostaglandin E2, prostaglandin D2, Rac2, proteasome inhibition, innate immunity, alveolar macrophages, bone marrow-derived macrophages
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