Journal ArticleDOI
Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction.
José-Ramón Conejo García,Florian Jaumann,Sandra Schulz,Alexander Krause,Javier Rodríguez-Jiménez,Ulf Forssmann,Knut Adermann,Enno Klüver,Claus Vogelmeier,Dirk Becker,Rainer Hedrich,Wolf-Georg Forssmann,Robert Bals +12 more
TLDR
It is shown that screening of genomic sequences is a valuable tool with which to identify novel regulatory peptides in β-defensins, a family of antimicrobial peptides differentially expressed in most tissues, regulated by specific mechanisms, and exerting physiological functions not only related to direct host defense.Abstract:
Previous studies have shown the implication of β-defensins in host defense of the human body. The human β-defensins 1 and 2 (hBD-1, hBD-2) have been isolated by biochemical methods. Here we report the identification of a third human β-defensin, called human β-defensin 3 (hBD-3; cDNA sequence, Genbank accession no. AF295370), based on bioinformatics and functional genomic analysis. Expression of hBD-3 is detected throughout epithelia of many organs and in non-epithelial tissues. In contrast to hBD-2, which is upregulated by microorganisms or tumor necrosis factor-α (TNF-α), hBD-3 expression is increased particularly after stimulation by interferon-γ. Synthetic hBD-3 exhibits a strong antimicrobial activity against gram-negative and gram-positive bacteria and fungi, including Burkholderia cepacia. In addition, hBD-3 activates monocytes and elicits ion channel activity in biomembranes, specifically in oocytes of Xenopus laevis. This paper also shows that screening of genomic sequences is a valuable tool with which to identify novel regulatory peptides. Human β-defensins represent a family of antimicrobial peptides differentially expressed in most tissues, regulated by specific mechanisms, and exerting physiological functions not only related to direct host defense.read more
Citations
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Journal ArticleDOI
Mammalian defensins in the antimicrobial immune response
TL;DR: This review focuses on the biological functions of three structural subgroups of mammalian defensins and the evidence for their involvement as effectors of antimicrobial innate immunity.
Journal ArticleDOI
An angiogenic role for the human peptide antibiotic LL-37/hCAP-18
Rembert Koczulla,Georges von Degenfeld,Christian Kupatt,Florian Krötz,Stefan Zahler,Torsten Gloe,Katja Issbrücker,Pia Unterberger,Mohamed Zaiou,Mohamed Zaiou,Corinna Lebherz,Alexander Karl,Philip Raake,Achim Pfosser,Peter Boekstegers,Ulrich Welsch,Pieter S. Hiemstra,Claus Vogelmeier,Richard L. Gallo,Richard L. Gallo,Matthias Clauss,Robert Bals,Robert Bals +22 more
TL;DR: It is demonstrated that LL-37/hCAP-18 is a multifunctional antimicrobial peptide with a central role in innate immunity by linking host defense and inflammation with angiogenesis and arteriogenesis.
Journal ArticleDOI
Alarmins: chemotactic activators of immune responses.
Joost J. Oppenheim,De Yang +1 more
TL;DR: This work proposes to highlight a group of structurally diverse multifunctional host proteins that are rapidly released following pathogen challenge and/or cell death and are able to both recruit and activate antigen-presenting cells by grouping them under the novel term 'alarmins', in recognition of their role in mobilizing the immune system.
Journal ArticleDOI
Mammalian defensins in immunity: more than just microbicidal.
TL;DR: Although showing similarity in activity and overall tertiary structure, the evolutionary relationship between defensins and chemokines remains to be determined.
Journal ArticleDOI
Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo
TL;DR: The diversity, history and the various mechanisms of action of AMPs are discussed, and some of the recent strategies developed to improve the activity and biocompatibility of AMP are reviewed.
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