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J. Biol. Chem., Vol. 268, Issue 28, 20725-20728, 10, 1993
I Stefanova, ML Corcoran, EM Horak, LM Wahl, JB Bolen and ID Horak
Bacterial lipopolysaccharide (LPS) induces a pleiotropic activation of the
immune system which might subsequently result in septic shock. One of the
cell surface receptors for LPS is the glycophosphatidylinositol- anchored
protein CD14. Binding of LPS to CD14 induces production of lymphokines such
as tumor necrosis factor-alpha (TNF-alpha), interleukin-1 (IL-1), IL-6, and
IL-8, and CD14 is subsequently released from the cell surface. However, the
mechanism of signaling via CD14 is still not known. We report here that
protein tyrosine kinase (PTK) p56lyn is coupled to the LPS receptor CD14 in
human monocytes. LPS rapidly activates CD14-associated p56lyn
simultaneously with PTKs p58hck and p59c-fgr. Inhibition of PTKs by
herbimycin A completely blocks LPS-induced down-modulation of CD14 and
production of TNF-alpha and IL-1. These data suggest a critical role of
PTKs in the LPS/CD14- mediated signal transduction pathway in human
monocytes.
Lipopolysaccharide induces activation of CD14-associated protein tyrosine kinase p53/56lyn
Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
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