Wound healing activity of the human antimicrobial peptide LL37
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , , , , |
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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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 instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
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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1817545062103384064 |