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Am J Physiol Lung Cell Mol Physiol 284: L607-L613, 2003. First published December 20, 2002; doi:10.1152/ajplung.00116.2002
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Vol. 284, Issue 4, L607-L613, April 2003

Involvement of protein tyrosine kinase in Toll-like receptor 4-mediated NF-kappa B activation in human peripheral blood monocytes

Ling-Yu Chen1, Bruce L. Zuraw1, Ming Zhao1, Fu-Tong Liu2, Shuang Huang3, and Zhixing K. Pan1

Departments of 1 Molecular and Experimental Medicine and 3 Immunology, The Scripps Research Institute, La Jolla 92037; and 2 La Jolla Institute for Allergy and Immunology, San Diego, California 92121

Bacterial lipopolysaccharide (LPS) is a powerful activator of the innate immune system. Exposure to LPS induces an inflammatory reaction in the lung mediated primarily by human blood monocytes and alveolar macrophages, which release an array of inflammatory chemokines and cytokines including IL-8, TNF-alpha , IL-1beta , and IL-6. The signaling mechanisms utilized by LPS to stimulate the release of cytokines and chemokines are still incompletely understood. Pretreatment with the protein tyrosine kinase-specific inhibitors genistein and herbimycin A effectively blocked LPS-induced NF-kappa B activation as well as IL-8 gene expression in human peripheral blood monocytes. However, when genistein was added 2 min after the addition of LPS, no inhibition was observed. Utilizing a coimmunoprecipitation assay, we further showed that LPS-stimulated tyrosine phosphorylation of Toll-like receptor 4 (TLR4) may be involved in downstream signaling events induced by LPS. These findings provide evidence that LPS-induced NF-kappa B activation and IL-8 gene expression use a signaling pathway requiring protein tyrosine kinase and that such regulation may occur through tyrosine phosphorylation of TLR4.

inflammation; chemokine; lipopolysaccharide; signal transduction; monocytes


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