Journal
JOURNAL OF INNATE IMMUNITY
Volume 3, Issue 5, Pages 471-482Publisher
KARGER
DOI: 10.1159/000327016
Keywords
Antimicrobial peptide; Coagulation; Host defense; Endotoxin; Proteinase
Categories
Funding
- Swedish Research Council [521-2009-3378, 7480, 621-2003-4022]
- Royal Physiographic Society in Lund
- Welander-Finsen Foundation
- Crafoord Foundation
- Osterlund Foundation
- Kock Foundation
- Marianne and Marcus Wallenberg Foundation
- XImmune AB
- The Swedish Government
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Serine proteases of the Si family have maintained a common structure over an evolutionary span of more than one billion years, and evolved a variety of substrate specificities and diverse biological roles, involving digestion and degradation, blood clotting, fibrinolysis and epithelial homeostasis. We here show that a wide range of C-terminal peptide sequences of serine proteases, particularly from the coagulation and kallikrein systems, share characteristics common with classical antimicrobial peptides of innate immunity. Under physiological conditions, these peptides exert antimicrobial effects as well as immunomodulatory functions by inhibiting macrophage responses to bacterial lipopolysaccharide. In mice, selected peptides are protective against lipopolysaccharide-induced shock. Moreover, these S1-derived host defense peptides exhibit helical structures upon binding to lipopolysaccharide and also permeabilize liposomes. The results uncover new and fundamental aspects on host defense functions of serine proteases present particularly in blood and epithelia, and provide tools for the identification of host defense molecules of therapeutic interest. Copyright (C) 2011 S. Karger AG, Basel
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