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*
Departments of Microbiology and Immunology and
Medicine, University of Western Ontario, London, Ontario, Canada; and
Laboratory of Molecular Immunology and Inflammation, John P. Robarts Research Institute, London, Ontario, Canada
The expression of the seven-transmembrane domain chemokine
receptors CXCR1 and CXCR2 modulates neutrophil responsiveness to the
chemoattractant IL-8 and a number of closely related CXC chemokines. In
the present study, we investigated the mechanism by which bacterial LPS
induces the down-modulation of IL-8 responsiveness and CXCR1 and CXCR2
expression on human neutrophils. Treating neutrophils with LPS reduced
IL-8R expression to 55 ± 5% of the control within 30 min and to
23 ± 2% within 1 h of stimulation. Furthermore, this
down-modulation could not be attributed to increased concentrations of
IL-8, TNF-
, or IL-1ß, since ELISA studies indicated that
LPS-stimulated neutrophils did not release detectable amounts of these
proteins before 2 h poststimulation. The tyrosine kinase (TK)
inhibitors genistein and herbimycin A attenuated the LPS-mediated
down-modulation of CXCR1 and CXCR2, indicating that the activation of a
TK is required for LPS to mediate its effect. The effect of LPS on
receptor expression paralleled the hyperphosphorylation of the protein
TK p72syk. Although IL-8 induced a comparable
down-modulation of CXCR1 and CXCR2, TK inhibitors did not attenuate
this effect. These studies provide the first evidence of an
agonist-independent, TK-dependent pathway of chemokine receptor
regulation by endotoxin.
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