Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/16857

TitleWound healing activity of the human antimicrobial peptide LL37
Author(s)Ramos, Reinaldo Rodrigues
Silva, João P.
Rodrigues, Ana Cristina Costa
Costa, Raquel
Schmitt, Fernando C.
Soares, Raquel
Guardão, Luísa
Vilanova, Manuel
Domingues, Lucília
Gama, F. M.
KeywordsWound healing
Antimicrobial peptide
LL37
Angiogenesis
Issue date2011
PublisherElsevier
JournalPeptides
Abstract(s)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.
TypeArticle
URIhttp://hdl.handle.net/1822/16857
DOI10.1016/j.peptides.2011.06.005
ISSN0196-9781
Publisher versionhttp://www.sciencedirect.com/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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