Print Email Facebook Twitter The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps Title The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps Author Neumann, A. Berends, E.T.M. Nerlich, A. Molhoek, E.M. Gallo, R.L. Meerloo, T. Nizet, V. Naim, H.Y. von Köckritz-Blickwede, M. Publication year 2014 Abstract NETs (neutrophil extracellular traps) have been described as a fundamental innate immune defence mechanism. Duringformation of NETs, the nuclear membrane is disrupted by an asyet unknown mechanism. In the present study we investigated the role of human cathelicidin LL-37 in nuclear membrane disruption and formation of NETs. Immunofluorescence microscopy revealed that 5 μMLL-37 significantly facilitated NET formation by primary human blood-derived neutrophils alone, in the presence of the classical chemical NET inducer PMA or in the presence of Staphylococcus aureus. Parallel assays with a random LL-37 fragment library indicated that the NET induction is mediated by the hydrophobic character of the peptide. The translocalization of LL-37 towards the nucleus and the disruption of the nuclear membrane were visualized using confocal fluorescence microscopy. In conclusion, the present study demonstrates a novel role for LL-37 in the formation of NETs. Subject LifeCBRN - CBRN ProtectionEELS - Earth, Environmental and Life SciencesBiomedical InnovationHealthy LivingCathelicidinCell deathHydrophobicityNETosisNeutrophil extracellular trapNuclear membraneBeta defensin 1Cathelicidin antimicrobial peptide LL 37Lamin BPolymyxin BAnimal cellBacterial membraneCell nucleus membraneControlled studyElectron microscopyExtracellular matrixFluorescence microscopy cellHydrophobicityImmunofluorescence microscopyMaleMouseNeutrophilNeutrophil extracellular trapNonhumanNormal humanPhenotypeStaphylococcus aureusPolymyxin B, 1404-26-8, 1405-20-5 To reference this document use: http://resolver.tudelft.nl/uuid:079f5324-ee9a-495d-95fe-f01fb471ab15 DOI https://doi.org/10.1042/bj20140778 TNO identifier 519653 ISSN 0264-6021 Source Biochemical Journal, 464, 3-11 Bibliographical note Funding Details: KO 3552/4-1, DFG, Deutsche Forschungsgemeinschaft Document type article Files To receive the publication files, please send an e-mail request to TNO Library.