Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2

Detalhes bibliográficos
Autor(a) principal: Rodrigues, Caroline Fabri Bittencourt [UNESP]
Data de Publicação: 2019
Outros Autores: Ferreira, Marcelo José Pena, Belchor, Mariana Novo [UNESP], Costa, Caroline R.C. [UNESP], Novaes, Danielle P. [UNESP], dos Santos, Adeilso Bispo [UNESP], Tamayose, Cinthia I., Pinho, Marcus Vinícius Terashima [UNESP], de Oliveira, Marcos Antonio [UNESP], Toyama, Marcos Hikari [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.3390/md17070403
http://hdl.handle.net/11449/189380
Resumo: Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential.
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spelling Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2Anti-inflammatoryCasuarictinCrotalus durissus terrificusEdemaEnzymatic inhibitionLaguncularia racemosaMyonecrosisSecretory phospholipase A2Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential.National Council for Scientific ResearchUniversidade de São PauloLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteLaboratório de Herpetologia Instituto Butantan São PauloDepartamento de Botânica Instituto de Biociências Universidade de São PauloLaboratório de Biologia Molecular Estrutural (LABIMES) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteLaboratório de Biologia Molecular Estrutural (LABIMES) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteNational Council for Scientific Research: 001Universidade de São Paulo: 2013/10938-6Universidade de São Paulo: 2014/20932-8Universidade de São Paulo: 2014/21593-2Universidade de São Paulo: 2017/20291-0Universidade Estadual Paulista (Unesp)São PauloUniversidade de São Paulo (USP)Rodrigues, Caroline Fabri Bittencourt [UNESP]Ferreira, Marcelo José PenaBelchor, Mariana Novo [UNESP]Costa, Caroline R.C. [UNESP]Novaes, Danielle P. [UNESP]dos Santos, Adeilso Bispo [UNESP]Tamayose, Cinthia I.Pinho, Marcus Vinícius Terashima [UNESP]de Oliveira, Marcos Antonio [UNESP]Toyama, Marcos Hikari [UNESP]2019-10-06T16:38:46Z2019-10-06T16:38:46Z2019-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.3390/md17070403Marine Drugs, v. 17, n. 7, 2019.1660-3397http://hdl.handle.net/11449/18938010.3390/md170704032-s2.0-850685958338573195327542061Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengMarine Drugsinfo:eu-repo/semantics/openAccess2021-10-23T17:30:11Zoai:repositorio.unesp.br:11449/189380Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:50:31.995687Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
title Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
spellingShingle Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
Rodrigues, Caroline Fabri Bittencourt [UNESP]
Anti-inflammatory
Casuarictin
Crotalus durissus terrificus
Edema
Enzymatic inhibition
Laguncularia racemosa
Myonecrosis
Secretory phospholipase A2
title_short Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
title_full Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
title_fullStr Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
title_full_unstemmed Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
title_sort Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
author Rodrigues, Caroline Fabri Bittencourt [UNESP]
author_facet Rodrigues, Caroline Fabri Bittencourt [UNESP]
Ferreira, Marcelo José Pena
Belchor, Mariana Novo [UNESP]
Costa, Caroline R.C. [UNESP]
Novaes, Danielle P. [UNESP]
dos Santos, Adeilso Bispo [UNESP]
Tamayose, Cinthia I.
Pinho, Marcus Vinícius Terashima [UNESP]
de Oliveira, Marcos Antonio [UNESP]
Toyama, Marcos Hikari [UNESP]
author_role author
author2 Ferreira, Marcelo José Pena
Belchor, Mariana Novo [UNESP]
Costa, Caroline R.C. [UNESP]
Novaes, Danielle P. [UNESP]
dos Santos, Adeilso Bispo [UNESP]
Tamayose, Cinthia I.
Pinho, Marcus Vinícius Terashima [UNESP]
de Oliveira, Marcos Antonio [UNESP]
Toyama, Marcos Hikari [UNESP]
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
São Paulo
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Rodrigues, Caroline Fabri Bittencourt [UNESP]
Ferreira, Marcelo José Pena
Belchor, Mariana Novo [UNESP]
Costa, Caroline R.C. [UNESP]
Novaes, Danielle P. [UNESP]
dos Santos, Adeilso Bispo [UNESP]
Tamayose, Cinthia I.
Pinho, Marcus Vinícius Terashima [UNESP]
de Oliveira, Marcos Antonio [UNESP]
Toyama, Marcos Hikari [UNESP]
dc.subject.por.fl_str_mv Anti-inflammatory
Casuarictin
Crotalus durissus terrificus
Edema
Enzymatic inhibition
Laguncularia racemosa
Myonecrosis
Secretory phospholipase A2
topic Anti-inflammatory
Casuarictin
Crotalus durissus terrificus
Edema
Enzymatic inhibition
Laguncularia racemosa
Myonecrosis
Secretory phospholipase A2
description Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential.
publishDate 2019
dc.date.none.fl_str_mv 2019-10-06T16:38:46Z
2019-10-06T16:38:46Z
2019-01-01
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/10.3390/md17070403
Marine Drugs, v. 17, n. 7, 2019.
1660-3397
http://hdl.handle.net/11449/189380
10.3390/md17070403
2-s2.0-85068595833
8573195327542061
url http://dx.doi.org/10.3390/md17070403
http://hdl.handle.net/11449/189380
identifier_str_mv Marine Drugs, v. 17, n. 7, 2019.
1660-3397
10.3390/md17070403
2-s2.0-85068595833
8573195327542061
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Marine Drugs
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)
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