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Blood, Vol. 92 No. 10 (November 15), 1998:
pp. 3898-3903
Inhibition of Activation of the Classical Pathway of Complement by
Human Neutrophil Defensins
Rocco H. van den Berg,
Maria C. Faber-Krol,
Sandra van Wetering,
Pieter S. Hiemstra, and
Mohamed R. Daha
From the Departments of Nephrology and Pulmonology, Leiden University
Medical Center, Leiden, The Netherlands.
Defensins are small, cationic antimicrobial peptides that are
present in the azurophilic granules of neutrophils. Earlier studies
have shown that defensins may influence complement activation by
specific interaction with activated C1, C1q, and C1-inhibitor. In the
present study, we show that the defensin human neutrophil peptide-1
(HNP-1) is able to inhibit activation of the classical complement
pathway by inhibition of C1q hemolytic activity. The binding site for
HNP-1 on C1q is most likely located on the collagen-like stalks, as a
clear, dose-dependent binding of HNP-1 to either intact C1q or to the
collagen-like stalks of C1q was demonstrated using enzyme-linked
immunosorbent assay (ELISA). Besides binding of HNP-1 to C1q, also a
limited binding to C1 and to a mixture of C1r and C1s was observed,
whereas no binding to C1-inhibitor was found. Because binding of HNP-1
to C1-inhibitor has been suggested in earlier studies, we also assessed
the binding of HNP-1 to mixtures of C1-inhibitor with either C1r/ C1s
or C1. No binding was found. Using a competition ELISA, it was found
that HNP-1, but not protamine, inhibited binding of biotin-labeled
HNP-1 to C1q in a dose-dependent fashion. In the fluid phase,
preincubation of HNP-1 with C1q resulted in complex formation of HNP-1
and C1q and generation of stable complexes. In conclusion, HNP-1 is
able to bind to C1q in the fluid phase and inhibits the classical
complement pathway. This mechanism may be involved in the control of an
inflammatory response in vivo.
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