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Cited by 311Immune Response and InflammationNF-κB Signaling PathwaysProtein Kinase Regulation and GTPase Signaling

Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages.

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Weinstein, S L, Gold, M R, DeFranco, A L·1991·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.88.10.4148PMC PMC51615
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Abstract

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.

    “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]

    The Abstract (p. 4148) reports that LPS rapidly increases protein tyrosine phosphorylation in macrophages. It also reports that a tyrosine kinase inhibitor blocked both phosphorylation and release of arachidonic acid metabolites, but concludes only that phosphorylation *may* mediate that response; it does not establish as fact that phosphorylation aids cellular activation generally. (LLM, conf=0.83)

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Authors
Weinstein, S. L., Gold, M. R., & DeFranco, A. L.
Affiliations
Department of Microbiology and Immunology, George Williams Hooper Foundation, San Francisco, CA.
ORCID
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
DOI
10.1073/pnas.88.10.4148
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
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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