The C-Terminal Sequence of Several Human Serine Proteases Encodes Host Defense Functions.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

Serine proteases of the S1 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.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Immunologi inom det medicinska området

Nyckelord

Originalspråkengelska
Sidor (från-till)471-482
TidskriftJournal of Innate Immunity
Volym3
Utgivningsnummer5
StatusPublished - 2011
PublikationskategoriForskning
Peer review utfördJa

Relaterad forskningsoutput

Kasetty, G., 2014, Department of Dermatology and Venereology, Lund University. 54 s.

Forskningsoutput: AvhandlingDoktorsavhandling (sammanläggning)

Visa alla (1)