LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis

Innate immunity responds to infections and inflammatory stimuli through a carefully choreographed set of interactions between cells, stimuli and their specific receptors. Of particular importance are endogenous peptides, which assume roles as defensins or alarmins, growth factors or wound repair ind...

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Main Authors: Marko Radic, Sylviane Muller
Format: Article
Language:English
Published: MDPI AG 2022-08-01
Series:Cells
Subjects:
Online Access:https://www.mdpi.com/2073-4409/11/15/2463
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author Marko Radic
Sylviane Muller
author_facet Marko Radic
Sylviane Muller
author_sort Marko Radic
collection DOAJ
description Innate immunity responds to infections and inflammatory stimuli through a carefully choreographed set of interactions between cells, stimuli and their specific receptors. Of particular importance are endogenous peptides, which assume roles as defensins or alarmins, growth factors or wound repair inducers. LL-37, a proteolytic fragment of cathelicidin, fulfills the roles of a defensin by inserting into the membranes of bacterial pathogens, functions as alarmin in stimulating chemotaxis of innate immune cells, and alters the structure and efficacy of various cytokines. Here, we draw attention to the direct effect of LL-37 on neutrophils and the release of extracellular traps (NETs), as NETs have been established as mediators of immune defense against pathogens but also as important contributors to chronic disease and tissue pathogenesis. We propose a specific structural basis for LL-37 function, in part by highlighting the structural flexibility of LL-37 and its ability to adapt to distinct microenvironments and interacting counterparts.
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spelling doaj.art-07e3485ead8b43e18a7059d734ee8f882023-12-01T22:53:26ZengMDPI AGCells2073-44092022-08-011115246310.3390/cells11152463LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosisMarko Radic0Sylviane Muller1Department of Microbiology, Immunology and Biochemistry, College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163, USACNRS-Strasbourg University Biotechnology and Cell Signaling UMR7242/Strasbourg Drug Discovery and Development Institute (IMS), 67000 Strasbourg, FranceInnate immunity responds to infections and inflammatory stimuli through a carefully choreographed set of interactions between cells, stimuli and their specific receptors. Of particular importance are endogenous peptides, which assume roles as defensins or alarmins, growth factors or wound repair inducers. LL-37, a proteolytic fragment of cathelicidin, fulfills the roles of a defensin by inserting into the membranes of bacterial pathogens, functions as alarmin in stimulating chemotaxis of innate immune cells, and alters the structure and efficacy of various cytokines. Here, we draw attention to the direct effect of LL-37 on neutrophils and the release of extracellular traps (NETs), as NETs have been established as mediators of immune defense against pathogens but also as important contributors to chronic disease and tissue pathogenesis. We propose a specific structural basis for LL-37 function, in part by highlighting the structural flexibility of LL-37 and its ability to adapt to distinct microenvironments and interacting counterparts.https://www.mdpi.com/2073-4409/11/15/2463cathelicidincationic antimicrobial proteinNETosislupusneutrophilsstructural flexibility
spellingShingle Marko Radic
Sylviane Muller
LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
Cells
cathelicidin
cationic antimicrobial protein
NETosis
lupus
neutrophils
structural flexibility
title LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
title_full LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
title_fullStr LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
title_full_unstemmed LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
title_short LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis
title_sort ll 37 a multi faceted amphipathic peptide involved in netosis
topic cathelicidin
cationic antimicrobial protein
NETosis
lupus
neutrophils
structural flexibility
url https://www.mdpi.com/2073-4409/11/15/2463
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