Source:http://linkedlifedata.com/resource/pubmed/id/21693141
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2011-7-15
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pubmed:abstractText |
Antimicrobial peptides (AMPs) are part of the innate immune system and are generally defined as cationic, amphipathic peptides, with less than 50 amino acids, including multiple arginine and lysine residues. The human cathelicidin antimicrobial peptide LL37 can be found at different concentrations in many different cells, tissues and body fluids and has a broad spectrum of antimicrobial and immunomodulatory activities. The healing of wound is a complex process that involves different steps: hemostasis, inflammation, remodeling/granulation tissue formation and re-epithelialization. Inflammation and angiogenesis are two fundamental physiological conditions implicated in this process. We have recently developed a new method for the expression and purification of recombinant LL37. In this work, we show that the recombinant peptide P-LL37 with a N-terminus proline preserves its immunophysiological properties in vitro and in vivo. P-LL37 neutralized the activation of macrophages by lipopolysaccharide (LPS). Besides, the peptide induced proliferation, migration and tubule-like structures formation by endothelial cells. Wound healing experiments were performed in dexamethasone-treated mice to study the effect of LL37 on angiogenesis and wound regeneration. The topical application of synthetic and recombinant LL37 increased vascularization and re-epithelialization. Taken together, these results clearly demonstrate that LL37 may have a key role in wound regeneration through vascularization.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cathelicidins,
http://linkedlifedata.com/resource/pubmed/chemical/Dexamethasone,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cathelicidin antimicrobial peptide
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1873-5169
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pubmed:author |
pubmed-author:CostaRaquelR,
pubmed-author:DominguesLucíliaL,
pubmed-author:GamaMiguelM,
pubmed-author:GuardãoLuísaL,
pubmed-author:RamosReinaldoR,
pubmed-author:RodriguesAna CristinaAC,
pubmed-author:SchmittFernandoF,
pubmed-author:SilvaJoão PedroJP,
pubmed-author:SoaresRaquelR,
pubmed-author:VilanovaManuelM
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1469-76
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pubmed:meshHeading |
pubmed-meshheading:21693141-Animals,
pubmed-meshheading:21693141-Anti-Bacterial Agents,
pubmed-meshheading:21693141-Cathelicidins,
pubmed-meshheading:21693141-Cell Movement,
pubmed-meshheading:21693141-Cell Survival,
pubmed-meshheading:21693141-Dexamethasone,
pubmed-meshheading:21693141-Endothelial Cells,
pubmed-meshheading:21693141-Endothelium, Vascular,
pubmed-meshheading:21693141-Granulation Tissue,
pubmed-meshheading:21693141-Humans,
pubmed-meshheading:21693141-Lipopolysaccharides,
pubmed-meshheading:21693141-Macrophages,
pubmed-meshheading:21693141-Mice,
pubmed-meshheading:21693141-Mice, Inbred C57BL,
pubmed-meshheading:21693141-Microscopy,
pubmed-meshheading:21693141-Neovascularization, Physiologic,
pubmed-meshheading:21693141-Recombinant Proteins,
pubmed-meshheading:21693141-Soft Tissue Injuries,
pubmed-meshheading:21693141-Wound Healing
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pubmed:year |
2011
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pubmed:articleTitle |
Wound healing activity of the human antimicrobial peptide LL37.
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pubmed:affiliation |
IBB, Institute of Biotechnology and Bioengineering, Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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