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Blood, Vol. 92 No. 12 (December 15), 1998:
pp. 4819-4827
Adhesion-Dependent Release of Elastase From Human Neutrophils in a
Novel, Flow-Based Model: Specificity of Different Chemotactic Agents
G. Ed Rainger,
Andrew F. Rowley, and
Gerard B. Nash
From the Department of Physiology, The Medical School, The University
of Birmingham, Birmingham, UK; and the School of Biological Sciences,
University of Wales Swansea, Swansea, Wales.
Neutrophils must adhere to the vessel wall, migrate, and degranulate
in an ordered manner to perform their protective function. Disruption
of these processes may be pathogenic. Current knowledge of the
degranulation process is derived almost exclusively from studies on
neutrophils in suspension, in which priming with the nonphysiological
agent cytochalasin B is necessary to obtain elastase release in
response to activating agents. To avoid this, we have adopted a
different approach. Using a novel flow-based adhesion system, we have
been able to quantify the release of elastase from the primary granules
of activated neutrophils adherent to immobilized platelets or purified
receptors without priming. Comparing stimuli, formyl tripeptide (fMLP),
interleukin-8 (IL-8), activated complement fragment C5a, and
platelet-activating factor (PAF) all induced rapid conversion to
CD11b/CD18 (MAC-1) -mediated stationary adhesion when perfused over
neutrophils already rolling on platelet monolayers or purified
P-selectin. However, fMLP, C5a, and IL-8, but not PAF, induced release
of elastase from the adherent cells in minutes. Neutrophils stimulated
in suspension showed little degranulation. Treatment of neutrophils
with an inhibitor of 5-lipoxygenase-activating protein (MK886) and
thus synthesis of leukotrienes (LTs) or with an antagonist of the
LTB4 receptor (LY223982) blocked the release of elastase.
This indicated that endogenous synthesis of 5-lipoxygenase products
such as LTs and autocrine activation of neutrophils was required for
fMLP-driven elastase release. We hypothesize that the differential
ability of PAF and fMLP to induce elastase release from
surface-adherent neutrophils could arise from differential ability to
generate leukotrienes, such as LTB4, and would be an appropriate mechanism for the control of elastase release during inflammation in vivo, where it is important that cytotoxic agents are
not released until activated neutrophils have migrated into the
extravascular tissues.
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