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Lipopolysaccharide-induced cytokine production in human monocytes: role of tyrosine phosphorylation in transmembrane signal transduction.
Eur J Immunol. 1994 Jun; 24(6):1278-84.EJ

Abstract

The signal transduction events that follow the binding of lipopolysaccharide (LPS) to the macrophage cell surface are not well defined. In the current studies LPS was found to induce alterations in phosphorylation of monocyte proteins on tyrosine. Herbimycin A and genistein, inhibitors of tyrosine kinases, markedly attenuated LPS-induced tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) protein and mRNA production. Reciprocally, the tyrosine phosphatase inhibitor sodium orthovanadate enhanced LPS-induced production of TNF-alpha. LPS induced a concentration-dependent increase in tyrosine phosphorylation of several proteins, which paralleled and preceded the onset of LPS-induced TNF-alpha production. LPS stimulation had different but reproducible effects on three members of the src family of tyrosine kinases. Both Hck and Lyn kinase activity increased before the onset of TNF-alpha production, consistent with their participation in the observed LPS-induced tyrosine phosphoprotein accumulation. In contrast, Yes kinase activity was not affected. These observations were made at concentrations of LPS that required serum rich in LPS-binding protein and the monocyte surface antigen CD14 for TNF-alpha production. These data indicate that tyrosine kinases and phosphatases are involved in the signal transduction cascade by which LPS induces production of TNF-alpha and IL-6 by human monocytes, and suggest that Lyn and Hck are candidate participants in this process.

Authors+Show Affiliations

Department of Medicine, University of Washington School of Medicine, Seattle.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7515809

Citation

Beaty, C D., et al. "Lipopolysaccharide-induced Cytokine Production in Human Monocytes: Role of Tyrosine Phosphorylation in Transmembrane Signal Transduction." European Journal of Immunology, vol. 24, no. 6, 1994, pp. 1278-84.
Beaty CD, Franklin TL, Uehara Y, et al. Lipopolysaccharide-induced cytokine production in human monocytes: role of tyrosine phosphorylation in transmembrane signal transduction. Eur J Immunol. 1994;24(6):1278-84.
Beaty, C. D., Franklin, T. L., Uehara, Y., & Wilson, C. B. (1994). Lipopolysaccharide-induced cytokine production in human monocytes: role of tyrosine phosphorylation in transmembrane signal transduction. European Journal of Immunology, 24(6), 1278-84.
Beaty CD, et al. Lipopolysaccharide-induced Cytokine Production in Human Monocytes: Role of Tyrosine Phosphorylation in Transmembrane Signal Transduction. Eur J Immunol. 1994;24(6):1278-84. PubMed PMID: 7515809.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Lipopolysaccharide-induced cytokine production in human monocytes: role of tyrosine phosphorylation in transmembrane signal transduction. AU - Beaty,C D, AU - Franklin,T L, AU - Uehara,Y, AU - Wilson,C B, PY - 1994/6/1/pubmed PY - 1994/6/1/medline PY - 1994/6/1/entrez SP - 1278 EP - 84 JF - European journal of immunology JO - Eur J Immunol VL - 24 IS - 6 N2 - The signal transduction events that follow the binding of lipopolysaccharide (LPS) to the macrophage cell surface are not well defined. In the current studies LPS was found to induce alterations in phosphorylation of monocyte proteins on tyrosine. Herbimycin A and genistein, inhibitors of tyrosine kinases, markedly attenuated LPS-induced tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) protein and mRNA production. Reciprocally, the tyrosine phosphatase inhibitor sodium orthovanadate enhanced LPS-induced production of TNF-alpha. LPS induced a concentration-dependent increase in tyrosine phosphorylation of several proteins, which paralleled and preceded the onset of LPS-induced TNF-alpha production. LPS stimulation had different but reproducible effects on three members of the src family of tyrosine kinases. Both Hck and Lyn kinase activity increased before the onset of TNF-alpha production, consistent with their participation in the observed LPS-induced tyrosine phosphoprotein accumulation. In contrast, Yes kinase activity was not affected. These observations were made at concentrations of LPS that required serum rich in LPS-binding protein and the monocyte surface antigen CD14 for TNF-alpha production. These data indicate that tyrosine kinases and phosphatases are involved in the signal transduction cascade by which LPS induces production of TNF-alpha and IL-6 by human monocytes, and suggest that Lyn and Hck are candidate participants in this process. SN - 0014-2980 UR - https://www.unboundmedicine.com/medline/citation/7515809/Lipopolysaccharide_induced_cytokine_production_in_human_monocytes:_role_of_tyrosine_phosphorylation_in_transmembrane_signal_transduction_ L2 - https://doi.org/10.1002/eji.1830240606 DB - PRIME DP - Unbound Medicine ER -