Wound healing activity of the human antimicrobial peptide LL37

Detalhes bibliográficos
Autor(a) principal: Ramos, Reinaldo Rodrigues
Data de Publicação: 2011
Outros Autores: Silva, João P., Rodrigues, Ana Cristina Costa, Costa, Raquel, Schmitt, Fernando C., Soares, Raquel, Guardão, Luísa, Vilanova, Manuel, Domingues, Lucília, Gama, F. M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/16857
Resumo: 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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spelling Wound healing activity of the human antimicrobial peptide LL37Wound healingAntimicrobial peptideLL37AngiogenesisScience & TechnologyAntimicrobial 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.This work was supported by the individual Grant SFRH/BD/27404/2006 from Fundacaopara a Ciencia e a Tecnologia (Portugal). We are grateful to Joana Almeida, at the Department of Biochemistry, University of Porto, for the help with the histological analyzes.ElsevierUniversidade do MinhoRamos, Reinaldo RodriguesSilva, João P.Rodrigues, Ana Cristina CostaCosta, RaquelSchmitt, Fernando C.Soares, RaquelGuardão, LuísaVilanova, ManuelDomingues, LucíliaGama, F. M.20112011-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/16857eng0196-978110.1016/j.peptides.2011.06.00521693141http://www.sciencedirect.com/info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-11T06:41:57Zoai:repositorium.sdum.uminho.pt:1822/16857Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-11T06:41:57Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Wound healing activity of the human antimicrobial peptide LL37
title Wound healing activity of the human antimicrobial peptide LL37
spellingShingle Wound healing activity of the human antimicrobial peptide LL37
Ramos, Reinaldo Rodrigues
Wound healing
Antimicrobial peptide
LL37
Angiogenesis
Science & Technology
title_short Wound healing activity of the human antimicrobial peptide LL37
title_full Wound healing activity of the human antimicrobial peptide LL37
title_fullStr Wound healing activity of the human antimicrobial peptide LL37
title_full_unstemmed Wound healing activity of the human antimicrobial peptide LL37
title_sort Wound healing activity of the human antimicrobial peptide LL37
author Ramos, Reinaldo Rodrigues
author_facet 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.
author_role author
author2 Silva, João P.
Rodrigues, Ana Cristina Costa
Costa, Raquel
Schmitt, Fernando C.
Soares, Raquel
Guardão, Luísa
Vilanova, Manuel
Domingues, Lucília
Gama, F. M.
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv 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.
dc.subject.por.fl_str_mv Wound healing
Antimicrobial peptide
LL37
Angiogenesis
Science & Technology
topic Wound healing
Antimicrobial peptide
LL37
Angiogenesis
Science & Technology
description 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.
publishDate 2011
dc.date.none.fl_str_mv 2011
2011-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/16857
url http://hdl.handle.net/1822/16857
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0196-9781
10.1016/j.peptides.2011.06.005
21693141
http://www.sciencedirect.com/
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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