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*
Immunology Research Center, Institut Armand-Frappier, Université du Québec, des-Prairies, Laval, Québec, Canada; and
Service de pneumologie, Département de médecine, Université de Sherbrooke, Sherbrooke, Québec, Canada
Human leukocyte elastase (HLE) participates in tissue
destruction in a number of inflammatory disorders, including rheumatoid
arthritis and cystic fibrosis. Since HLE has been shown to bind to
Mac-1, and ICAM-1 plays a key role during the recruitment and the
activation of leukocytes at inflamed sites, we investigated the
capacity of HLE to cleave ICAM-1. Flow-cytometric analyses showed a
dose-dependent cleavage of ICAM-1 by HLE on different human cell lines.
The cleavage was completely inhibited by 
1-antitrypsin, a natural
HLE protease inhibitor. The ability of HLE to degrade ICAM-1 was
further confirmed by electrophoretic analysis using a soluble form of
ICAM-1 (D1-D5). Enzymatic removal of N-linked
glycosylation did not significantly modulate ICAM-1 cleavage by HLE,
while removal of sialic acid residues partially reduced the sensitivity
of ICAM-1 to HLE. We further showed that sputum of cystic fibrosis
patients contains high levels of HLE activity capable of cleavage of
cell surface ICAM-1. The cleavage induced by incubation of cells with
the sputum sample was totally inhibited by 1-antitrypsin and the
specific peptidic HLE inhibitor
N-methoxysuccinyl-Ala-Ala-Pro-Val-chloromethylketone.
Moreover, the cleavage of ICAM-1 was concomitant to that of CD4 at the
surface of the same cell, at the same amplitude, and at all HLE
concentrations. The capacity of HLE to modulate the expression of
ICAM-1 on the surface of leukocytes by proteolytic cleavage brings
support to the hypothesis that overproduction of HLE can cause severe
immunologic lung disorders by affecting intercellular
adhesion.
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