The peptide secreted at the water to land transition in a model amphibian has antioxidant effects

Detalhes bibliográficos
Autor(a) principal: Barbosa, Eder Alves
Data de Publicação: 2021
Outros Autores: Plácido, Alexandra, Moreira, Daniel C., Albuquerque, Lucas, Dematei, Anderson, Silva-Carvalho, Amandda É., Cabral, Wanessa F., Báo, Sonia N., Saldanha-Araújo, Felipe, Kuckelhaus, Selma A. S., Borges, Tatiana K., Portugal, Camila C., Socodato, Renato, Teixeira, Cátia, Lima, Filipe Camargo D. A., Batagin-Neto, Augusto [UNESP], Sebben, Antônio, Eaton, Peter, Gomes, Paula, Brand, Guilherme D., Relvas, Joao B., Kato, Massuo J., Leite, Jose Roberto S. A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1098/rspb.2021.1531
http://hdl.handle.net/11449/229957
Resumo: In addition to the morphophysiological changes experienced by amphibians during metamorphosis, they must also deal with a different set of environmental constraints when they shift from the water to the land. We found that Pithecopus azureus secretes a single peptide ([M + H]+ = 658.38 Da) at the developmental stage that precedes the onset of terrestrial behaviour. De novo peptide and cDNA sequencing revealed that the peptide, named PaT-2, is expressed in tandem and is a member of the tryptophyllins family. In silico studies allowed us to identify the position of reactive sites and infer possible antioxidant mechanisms of the compounds. Cell-based assays confirmed the predicted antioxidant activity in mammalian microglia and neuroblast cells. The potential neuroprotective effect of PaT-2 was further corroborated in FRET-based live cell imaging assays, where the peptide prevented lipopolysaccharide-induced ROS production and glutamate release in human microglia. In summary, PaT-2 is the first peptide expressed during the ontogeny of P. azureus, right before the metamorphosing froglet leaves the aquatic environment to occupy terrestrial habitats. The antioxidant activity of PaT-2, predicted by in silico analyses and confirmed by cell-based assays, might be relevant for the protection of the skin of P. azureus adults against increased O 2 levels and UV exposure on land compared with aquatic environments.
id UNSP_6bbcf878970124e9f60234af4fc0b4be
oai_identifier_str oai:repositorio.unesp.br:11449/229957
network_acronym_str UNSP
network_name_str Repositório Institucional da UNESP
repository_id_str 2946
spelling The peptide secreted at the water to land transition in a model amphibian has antioxidant effectsAmphibiaantioxidant peptideMALDI mass spectrometry imagingoxidative stressPithecopus azureustryptophyllinIn addition to the morphophysiological changes experienced by amphibians during metamorphosis, they must also deal with a different set of environmental constraints when they shift from the water to the land. We found that Pithecopus azureus secretes a single peptide ([M + H]+ = 658.38 Da) at the developmental stage that precedes the onset of terrestrial behaviour. De novo peptide and cDNA sequencing revealed that the peptide, named PaT-2, is expressed in tandem and is a member of the tryptophyllins family. In silico studies allowed us to identify the position of reactive sites and infer possible antioxidant mechanisms of the compounds. Cell-based assays confirmed the predicted antioxidant activity in mammalian microglia and neuroblast cells. The potential neuroprotective effect of PaT-2 was further corroborated in FRET-based live cell imaging assays, where the peptide prevented lipopolysaccharide-induced ROS production and glutamate release in human microglia. In summary, PaT-2 is the first peptide expressed during the ontogeny of P. azureus, right before the metamorphosing froglet leaves the aquatic environment to occupy terrestrial habitats. The antioxidant activity of PaT-2, predicted by in silico analyses and confirmed by cell-based assays, might be relevant for the protection of the skin of P. azureus adults against increased O 2 levels and UV exposure on land compared with aquatic environments.Laboratório de Síntese e Análise de Biomoléculas Instituto de Química Universidade de BrasíliaNúcleo de Pesquisa em Morfologia e Imunologia Aplicada (NuPMIA) Faculdade de Medicina Universidade de BrasíliaLaboratório de Imunologia Celular NuPMIA Faculdade de Medicina Universidade de BrasíliaPrograma de Pós-graduação em Medicina Tropical Núcleo de Medicina Tropical Faculdade de Medicina Universidade de BrasíliaLaboratório de Hematologia e Celulas-tronco Faculdade de Ciências da Saúde Universidade de BrasíliaLaboratório de Microscopia e Microanálise Instituto de Ciências Biológicas Universidade de BrasíliaInstituto de Ciências Biológicas Universidade de BrasíliaLaboratório de Espectrometria de Massa Embrapa Recursos Genéticos e BiotecnologiaBioprospectum Lda UPTECLAQV/REQUIMTE Departamento de Química e Bioquímica Faculdade de Ciências Universidade Do PortoGlial Cell Biology Lab Instituto de Investigacao e Inovacao em Saude and Instituto de Biologia Molecular e Celular Universidade Do PortoInstituto Federal de Educação Ciência e Tecnologia de São PauloSão Paulo State University (Unesp) Campus of ItapevaThe Bridge School of Chemistry Joseph Banks Laboratories University of LincolnDepartamento de Química Fundamental Instituto de Química Universidade de São Paulo, SPSão Paulo State University (Unesp) Campus of ItapevaUniversidade de Brasília (UnB)Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)UPTECUniversidade Do PortoCiência e Tecnologia de São PauloUniversidade Estadual Paulista (UNESP)University of LincolnUniversidade de São Paulo (USP)Barbosa, Eder AlvesPlácido, AlexandraMoreira, Daniel C.Albuquerque, LucasDematei, AndersonSilva-Carvalho, Amandda É.Cabral, Wanessa F.Báo, Sonia N.Saldanha-Araújo, FelipeKuckelhaus, Selma A. S.Borges, Tatiana K.Portugal, Camila C.Socodato, RenatoTeixeira, CátiaLima, Filipe Camargo D. A.Batagin-Neto, Augusto [UNESP]Sebben, AntônioEaton, PeterGomes, PaulaBrand, Guilherme D.Relvas, Joao B.Kato, Massuo J.Leite, Jose Roberto S. A.2022-04-29T08:36:48Z2022-04-29T08:36:48Z2021-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1098/rspb.2021.1531Proceedings of the Royal Society B: Biological Sciences, v. 288, n. 1962, 2021.1471-29540962-8452http://hdl.handle.net/11449/22995710.1098/rspb.2021.15312-s2.0-85119997100Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengProceedings of the Royal Society B: Biological Sciencesinfo:eu-repo/semantics/openAccess2022-04-29T08:36:49Zoai:repositorio.unesp.br:11449/229957Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:48:26.317884Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
title The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
spellingShingle The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
Barbosa, Eder Alves
Amphibia
antioxidant peptide
MALDI mass spectrometry imaging
oxidative stress
Pithecopus azureus
tryptophyllin
title_short The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
title_full The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
title_fullStr The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
title_full_unstemmed The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
title_sort The peptide secreted at the water to land transition in a model amphibian has antioxidant effects
author Barbosa, Eder Alves
author_facet Barbosa, Eder Alves
Plácido, Alexandra
Moreira, Daniel C.
Albuquerque, Lucas
Dematei, Anderson
Silva-Carvalho, Amandda É.
Cabral, Wanessa F.
Báo, Sonia N.
Saldanha-Araújo, Felipe
Kuckelhaus, Selma A. S.
Borges, Tatiana K.
Portugal, Camila C.
Socodato, Renato
Teixeira, Cátia
Lima, Filipe Camargo D. A.
Batagin-Neto, Augusto [UNESP]
Sebben, Antônio
Eaton, Peter
Gomes, Paula
Brand, Guilherme D.
Relvas, Joao B.
Kato, Massuo J.
Leite, Jose Roberto S. A.
author_role author
author2 Plácido, Alexandra
Moreira, Daniel C.
Albuquerque, Lucas
Dematei, Anderson
Silva-Carvalho, Amandda É.
Cabral, Wanessa F.
Báo, Sonia N.
Saldanha-Araújo, Felipe
Kuckelhaus, Selma A. S.
Borges, Tatiana K.
Portugal, Camila C.
Socodato, Renato
Teixeira, Cátia
Lima, Filipe Camargo D. A.
Batagin-Neto, Augusto [UNESP]
Sebben, Antônio
Eaton, Peter
Gomes, Paula
Brand, Guilherme D.
Relvas, Joao B.
Kato, Massuo J.
Leite, Jose Roberto S. A.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de Brasília (UnB)
Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
UPTEC
Universidade Do Porto
Ciência e Tecnologia de São Paulo
Universidade Estadual Paulista (UNESP)
University of Lincoln
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Barbosa, Eder Alves
Plácido, Alexandra
Moreira, Daniel C.
Albuquerque, Lucas
Dematei, Anderson
Silva-Carvalho, Amandda É.
Cabral, Wanessa F.
Báo, Sonia N.
Saldanha-Araújo, Felipe
Kuckelhaus, Selma A. S.
Borges, Tatiana K.
Portugal, Camila C.
Socodato, Renato
Teixeira, Cátia
Lima, Filipe Camargo D. A.
Batagin-Neto, Augusto [UNESP]
Sebben, Antônio
Eaton, Peter
Gomes, Paula
Brand, Guilherme D.
Relvas, Joao B.
Kato, Massuo J.
Leite, Jose Roberto S. A.
dc.subject.por.fl_str_mv Amphibia
antioxidant peptide
MALDI mass spectrometry imaging
oxidative stress
Pithecopus azureus
tryptophyllin
topic Amphibia
antioxidant peptide
MALDI mass spectrometry imaging
oxidative stress
Pithecopus azureus
tryptophyllin
description In addition to the morphophysiological changes experienced by amphibians during metamorphosis, they must also deal with a different set of environmental constraints when they shift from the water to the land. We found that Pithecopus azureus secretes a single peptide ([M + H]+ = 658.38 Da) at the developmental stage that precedes the onset of terrestrial behaviour. De novo peptide and cDNA sequencing revealed that the peptide, named PaT-2, is expressed in tandem and is a member of the tryptophyllins family. In silico studies allowed us to identify the position of reactive sites and infer possible antioxidant mechanisms of the compounds. Cell-based assays confirmed the predicted antioxidant activity in mammalian microglia and neuroblast cells. The potential neuroprotective effect of PaT-2 was further corroborated in FRET-based live cell imaging assays, where the peptide prevented lipopolysaccharide-induced ROS production and glutamate release in human microglia. In summary, PaT-2 is the first peptide expressed during the ontogeny of P. azureus, right before the metamorphosing froglet leaves the aquatic environment to occupy terrestrial habitats. The antioxidant activity of PaT-2, predicted by in silico analyses and confirmed by cell-based assays, might be relevant for the protection of the skin of P. azureus adults against increased O 2 levels and UV exposure on land compared with aquatic environments.
publishDate 2021
dc.date.none.fl_str_mv 2021-01-01
2022-04-29T08:36:48Z
2022-04-29T08:36:48Z
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://dx.doi.org/10.1098/rspb.2021.1531
Proceedings of the Royal Society B: Biological Sciences, v. 288, n. 1962, 2021.
1471-2954
0962-8452
http://hdl.handle.net/11449/229957
10.1098/rspb.2021.1531
2-s2.0-85119997100
url http://dx.doi.org/10.1098/rspb.2021.1531
http://hdl.handle.net/11449/229957
identifier_str_mv Proceedings of the Royal Society B: Biological Sciences, v. 288, n. 1962, 2021.
1471-2954
0962-8452
10.1098/rspb.2021.1531
2-s2.0-85119997100
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Proceedings of the Royal Society B: Biological Sciences
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808128704195330048