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Lipopolysaccharide enhances CD11b/CD18 function but inhibits neutrophil
aggregation
EB Lynam, SI Simon, YP Rochon and LA Sklar
Department of Cytometry, University of New Mexico School of Medicine,
Albuquerque 87131.
Human neutrophils are primed in the presence of complexes of
lipopolysaccharide (LPS) with its serum binding protein (LBP) in a manner
dependent on CD14. Cellular consequences of priming include increased
responsiveness, the upregulation of surface proteins including the adhesive
integrin CD11b/CD18 (Mac-1), the increased binding of certain ligands to
CD11b/CD18, and the concurrent shedding of the L-selectin homing receptor.
Because expression of both CD11b/CD18 and L-selectin is obligatory for
formyl peptide-stimulated neutrophil aggregation in vitro (Simon et al,
Blood 82:1097, 1993), we have examined the consequences of bacterial
endotoxin on the expression of neutrophil adhesive molecules. We observed
that the exposure of neutrophils to LPS/LBP, while enhancing the surface
numbers and adhesive function of CD11b/CD18 for latex particles, did not
induce aggregation. In contrast, as the LPS/LBP concentration increased
(ED50 = 30 ng/mL LPS/LBP), the ability of neutrophils to aggregate
decreased in parallel with the shedding of L-selectin. Moreover, when
L-selectin adhesive activity was blocked by treatment with Fab fragments of
Dreg- 200, aggregation was inhibited to an extent roughly proportional to
the available L-selection. Blocking of LPS/LBP with CD14-specific
monoclonal antibodies suppressed L-selectin shedding and preserved formyl
peptide-stimulated aggregation. Taken together, the data suggest that
inhibition of neutrophil aggregation by LPS/LBP is related to the
expression of L-selectin via CD14 rather than LPS inhibition of CD11b/CD18
function during cellular stimulation.
Volume 83,
Issue 11,
pp. 3303-3311,
06/01/1994
Copyright © 1994 by The American Society of Hematology
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