A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells

Detalhes bibliográficos
Autor(a) principal: Fagundes, Fabio H. R. [UNESP]
Data de Publicação: 2011
Outros Autores: Aparício, Ricardo, Dos Santos, Marcelo L., Filho, Eduardo B. S. Diz [UNESP], Oliveira, Simone C. B. [UNESP], Toyama, Daniela O., Toyama, Marcos H. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
DOI: 10.2174/092986611797200940
Texto Completo: http://dx.doi.org/10.2174/092986611797200940
http://hdl.handle.net/11449/226531
Resumo: A new secretory phospholipase A2 (sPLA2) isoform from Bothrops jararacussu venom (BjVIII) has been characterized by causing platelet aggregation, an absent activity in BthTx-I, Prtx-I and PrTx-II sPLA2s. According to our results, BjVIII also enhances insulin release by the pancreatic beta cells. The complete amino acid sequence of the new isoform was determined by Edman degradation and de novo peptide sequencing. These analyses showed a G35K amino acid modification for BjVIII in comparison with BthTx-I, PrTx-I and Prtx-II, a structural difference that has been related to the conflicting biological activities among BjVIII and other Lys49 sPLA2s. The whole set of evidences collected in this work indicates that, besides the C-terminal region and B-wing of PLA2, the calcium binding loop in BjVIII should be considered as an important region, involved in the pharmacological effects of Lys49-sPLA2 isoforms from the Bothrops genus. © 2011 Bentham Science Publishers.
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spelling A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cellsBothrops jararacussuEdman degradationInsulin secretionMass spectraPancreatic beta cellsPLA2Platelet aggregationA new secretory phospholipase A2 (sPLA2) isoform from Bothrops jararacussu venom (BjVIII) has been characterized by causing platelet aggregation, an absent activity in BthTx-I, Prtx-I and PrTx-II sPLA2s. According to our results, BjVIII also enhances insulin release by the pancreatic beta cells. The complete amino acid sequence of the new isoform was determined by Edman degradation and de novo peptide sequencing. These analyses showed a G35K amino acid modification for BjVIII in comparison with BthTx-I, PrTx-I and Prtx-II, a structural difference that has been related to the conflicting biological activities among BjVIII and other Lys49 sPLA2s. The whole set of evidences collected in this work indicates that, besides the C-terminal region and B-wing of PLA2, the calcium binding loop in BjVIII should be considered as an important region, involved in the pharmacological effects of Lys49-sPLA2 isoforms from the Bothrops genus. © 2011 Bentham Science Publishers.Departamento de Bioquímica IB UNICAMP, SP, CampinasInstituto de Química UNICAMP, SP, CampinasCentro de Ciências Biológicas e da Saúde Universidade Mackenzie - SP, São PauloUNESP Campus do Litoral Paulista - SP Unidade de São Vicente, São VicenteUNESP Campus do Litoral Paulista - SP Unidade de São Vicente, São VicenteUniversidade Estadual de Campinas (UNICAMP)Universidade Mackenzie - SPUniversidade Estadual Paulista (UNESP)Fagundes, Fabio H. R. [UNESP]Aparício, RicardoDos Santos, Marcelo L.Filho, Eduardo B. S. Diz [UNESP]Oliveira, Simone C. B. [UNESP]Toyama, Daniela O.Toyama, Marcos H. [UNESP]2022-04-29T00:50:31Z2022-04-29T00:50:31Z2011-11-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1133-1139http://dx.doi.org/10.2174/092986611797200940Protein and Peptide Letters, v. 18, n. 11, p. 1133-1139, 2011.0929-8665http://hdl.handle.net/11449/22653110.2174/0929866117972009402-s2.0-80053016977Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengProtein and Peptide Lettersinfo:eu-repo/semantics/openAccess2022-04-29T00:50:31Zoai:repositorio.unesp.br:11449/226531Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:46:38.853532Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
title A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
spellingShingle A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
Fagundes, Fabio H. R. [UNESP]
Bothrops jararacussu
Edman degradation
Insulin secretion
Mass spectra
Pancreatic beta cells
PLA2
Platelet aggregation
Fagundes, Fabio H. R. [UNESP]
Bothrops jararacussu
Edman degradation
Insulin secretion
Mass spectra
Pancreatic beta cells
PLA2
Platelet aggregation
title_short A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
title_full A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
title_fullStr A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
title_full_unstemmed A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
title_sort A catalytically inactive Lys49 PLA2 isoform from Bothrops jararacussu venom that stimulates insulin secretion in pancreatic beta cells
author Fagundes, Fabio H. R. [UNESP]
author_facet Fagundes, Fabio H. R. [UNESP]
Fagundes, Fabio H. R. [UNESP]
Aparício, Ricardo
Dos Santos, Marcelo L.
Filho, Eduardo B. S. Diz [UNESP]
Oliveira, Simone C. B. [UNESP]
Toyama, Daniela O.
Toyama, Marcos H. [UNESP]
Aparício, Ricardo
Dos Santos, Marcelo L.
Filho, Eduardo B. S. Diz [UNESP]
Oliveira, Simone C. B. [UNESP]
Toyama, Daniela O.
Toyama, Marcos H. [UNESP]
author_role author
author2 Aparício, Ricardo
Dos Santos, Marcelo L.
Filho, Eduardo B. S. Diz [UNESP]
Oliveira, Simone C. B. [UNESP]
Toyama, Daniela O.
Toyama, Marcos H. [UNESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual de Campinas (UNICAMP)
Universidade Mackenzie - SP
Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Fagundes, Fabio H. R. [UNESP]
Aparício, Ricardo
Dos Santos, Marcelo L.
Filho, Eduardo B. S. Diz [UNESP]
Oliveira, Simone C. B. [UNESP]
Toyama, Daniela O.
Toyama, Marcos H. [UNESP]
dc.subject.por.fl_str_mv Bothrops jararacussu
Edman degradation
Insulin secretion
Mass spectra
Pancreatic beta cells
PLA2
Platelet aggregation
topic Bothrops jararacussu
Edman degradation
Insulin secretion
Mass spectra
Pancreatic beta cells
PLA2
Platelet aggregation
description A new secretory phospholipase A2 (sPLA2) isoform from Bothrops jararacussu venom (BjVIII) has been characterized by causing platelet aggregation, an absent activity in BthTx-I, Prtx-I and PrTx-II sPLA2s. According to our results, BjVIII also enhances insulin release by the pancreatic beta cells. The complete amino acid sequence of the new isoform was determined by Edman degradation and de novo peptide sequencing. These analyses showed a G35K amino acid modification for BjVIII in comparison with BthTx-I, PrTx-I and Prtx-II, a structural difference that has been related to the conflicting biological activities among BjVIII and other Lys49 sPLA2s. The whole set of evidences collected in this work indicates that, besides the C-terminal region and B-wing of PLA2, the calcium binding loop in BjVIII should be considered as an important region, involved in the pharmacological effects of Lys49-sPLA2 isoforms from the Bothrops genus. © 2011 Bentham Science Publishers.
publishDate 2011
dc.date.none.fl_str_mv 2011-11-01
2022-04-29T00:50:31Z
2022-04-29T00:50:31Z
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/10.2174/092986611797200940
Protein and Peptide Letters, v. 18, n. 11, p. 1133-1139, 2011.
0929-8665
http://hdl.handle.net/11449/226531
10.2174/092986611797200940
2-s2.0-80053016977
url http://dx.doi.org/10.2174/092986611797200940
http://hdl.handle.net/11449/226531
identifier_str_mv Protein and Peptide Letters, v. 18, n. 11, p. 1133-1139, 2011.
0929-8665
10.2174/092986611797200940
2-s2.0-80053016977
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Protein and Peptide Letters
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1133-1139
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_ 1822182335095767040
dc.identifier.doi.none.fl_str_mv 10.2174/092986611797200940

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