Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-7-15
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1873-5169
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1469-76
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
pubmed:year
2011
pubmed:articleTitle
Wound healing activity of the human antimicrobial peptide LL37.
pubmed:affiliation
IBB, Institute of Biotechnology and Bioengineering, Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't