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The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps

Neumann, Ariane LU ; Berends, Evelien T. M.; Nerlich, Andreas; Molhoek, E. Margo; Gallo, Richard L.; Meerloo, Timo; Nizet, Victor; Naim, Hassan Y. and von Köckritz-Blickwede, Maren (2014) In The Biochemical journal 464(1). p.3-11
Abstract

NETs (neutrophil extracellular traps) have been described as a fundamental innate immune defence mechanism. During formation of NETs, the nuclear membrane is disrupted by an as-yet 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 μM LL-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 trans-localization of... (More)

NETs (neutrophil extracellular traps) have been described as a fundamental innate immune defence mechanism. During formation of NETs, the nuclear membrane is disrupted by an as-yet 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 μM LL-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 trans-localization 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.

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publishing date
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publication status
published
keywords
Amino Acid Sequence, Animals, Cathelicidins, Extracellular Traps, Humans, Male, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Neutrophils, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
in
The Biochemical journal
volume
464
issue
1
pages
9 pages
publisher
Portland Press Limited
external identifiers
  • scopus:84908453654
ISSN
0264-6021
DOI
10.1042/BJ20140778
language
English
LU publication?
no
id
cbd66a6f-2967-4537-a20c-aeac98c2631d
date added to LUP
2017-09-19 12:16:07
date last changed
2017-11-14 09:54:16
@article{cbd66a6f-2967-4537-a20c-aeac98c2631d,
  abstract     = {<p>NETs (neutrophil extracellular traps) have been described as a fundamental innate immune defence mechanism. During formation of NETs, the nuclear membrane is disrupted by an as-yet 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 μM LL-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 trans-localization 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.</p>},
  author       = {Neumann, Ariane and Berends, Evelien T. M. and Nerlich, Andreas and Molhoek, E. Margo and Gallo, Richard L. and Meerloo, Timo and Nizet, Victor and Naim, Hassan Y. and von Köckritz-Blickwede, Maren},
  issn         = {0264-6021},
  keyword      = {Amino Acid Sequence,Animals,Cathelicidins,Extracellular Traps,Humans,Male,Mice,Mice, Inbred C57BL,Molecular Sequence Data,Neutrophils,Journal Article,Research Support, N.I.H., Extramural,Research Support, Non-U.S. Gov't},
  language     = {eng},
  month        = {11},
  number       = {1},
  pages        = {3--11},
  publisher    = {Portland Press Limited},
  series       = {The Biochemical journal},
  title        = {The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps},
  url          = {http://dx.doi.org/10.1042/BJ20140778},
  volume       = {464},
  year         = {2014},
}