The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages.
Open accessAbstract
Lipopolysaccharide (LPS), a membrane component of Gram-negative bacteria, stimulates immune responses by activating macrophages, B lymphocytes, and other cells of the immune system. The mechanisms by which LPS activates these cells are poorly characterized. Since protein tyrosine phosphorylation appears to be a major intracellular signaling event that mediates cellular responses, we examined whether LPS alters tyrosine phosphorylation in macrophages. We found that Escherichia coli K235 LPS increased tyrosine phosphorylation of several proteins in the RAW 264.7 murine macrophage cell line and in resident peritoneal macrophages from C3H/HeSNJ mice. Changes in tyrosine phosphorylation were detectable by 4-5 min, reached a maximum by 15 min, and declined after 30-60 min. Protein tyrosine phosphorylation increased following stimulation with LPS at 100 pg/ml and was maximal with 10 ng/ml. Similar changes in tyrosine phosphorylation were induced by Salmonella minnesota R595 LPS and by the biologically active domain of LPS, lipid A, but not by the inactive lipid A derivative N2-monoacylglucosamine 1-phosphate. Phorbol 12-myristate 13-acetate also stimulated protein tyrosine phosphorylation, but some of the modulated proteins were different than those phosphorylated by LPS. Treatment of RAW 264.7 cells with a tyrosine kinase inhibitor, herbimycin A, inhibited both LPS-stimulated tyrosine phosphorylation and LPS-stimulated release of arachidonic acid metabolites. Thus, increased protein tyrosine phosphorylation is a rapid LPS-activated signaling event that may mediate release of arachidonic acid metabolites in RAW 264.7 cells.
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“Tyrosine phosphorylation has been characterized as a main event following LPS stimulation in macrophages which aids in cellular activation [47]”
From Alzheimer’s disease-associated protective variant Plcg2-P522R modulates peripheral macrophage function in a sex-dimorphic manner (2024) · cites this paper as [47]
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Cites
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Guaiume, E. A. (2005) · MOspace Institutional Repository (University of Missouri)
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Metadata
- Authors
- Weinstein, S. L., Gold, M. R., & DeFranco, A. L.
- Affiliations
- Department of Microbiology and Immunology, George Williams Hooper Foundation, San Francisco, CA.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1991-05-15
- Volume
- 88
- Issue
- 10
- Pages
- 4148-4152
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC51615
- OpenAlex
- W2027152576
- Cited by
- 311
- References
- 33
- Citations by year
- 2026: 1 · 2024: 2 · 2023: 1 · 2021: 2 · 2020: 1 · 2019: 3 · 2017: 2 · 2016: 1 · 2014: 2 · 2013: 3 · 2012: 2
- FWCI
- 10.80
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ai023864-02)
- National Institute of Allergy and Infectious Diseases (AI20038, AI23864)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- lipopolysaccharide, tyrosine phosphorylation, macrophages, intracellular signaling, lipid A, Salmonella minnesota, herbimycin A, tyrosine kinase, arachidonic acid metabolites, RAW 264.7 macrophages, peritoneal macrophages, phorbol myristate acetate
- MeSH terms
- Animals, Cell Line, Transformed, Escherichia coli, Female, Kinetics, Lipid A, Lipopolysaccharides, Macrophage Activation, Macrophages, Mice, Inbred C3H, Peritoneal Cavity, Phosphoproteins, Phosphorylation, Protein-Tyrosine Kinases, Quinones, Salmonella, Tetradecanoylphorbol Acetate, Tyrosine, Benzoquinones, Rifabutin, Phosphotyrosine, Lactams, Macrocyclic, Mice
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