Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.jchromb.2021.122695 http://hdl.handle.net/11449/207721 |
Resumo: | C-type lectin-like proteins found in snake venom, known as snaclecs, have important effects on hemostasis through targeting membrane receptors, coagulation factors and other hemostatic proteins. Here, we present the isolation and functional characterization of a snaclec isolated from Bothrops alternatus venom, designated as Baltetin. We purified the protein in three chromatographic steps (anion-exchange, affinity and reversed-phase chromatography). Baltetin is a dimeric snaclec that is approximately 15 and 25 kDa under reducing and non-reducing conditions, respectively, as estimated by SDS-PAGE. Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry and Edman degradation sequencing revealed that Baltetin is a heterodimer. The first 40 amino acid residues of the N-terminal region of Baltetin subunits share a high degree of sequence identity with other snaclecs. Baltetin had a specific, dose-dependent inhibitory effect on epinephrine-induced platelet aggregation in human platelet-rich plasma, inhibiting up to 69% of platelet aggregation. Analysis of the infrared spectra suggested that the interaction between Baltetin and platelets can be attributed to the formation of hydrogen bonds between the PO32- groups in the protein and PO2- groups in the platelet membrane. This interaction may lead to membrane lipid peroxidation, which prevents epinephrine from binding to its receptor. The present work suggests that Baltetin, a new C-type lectin-like protein isolated from B. alternatus venom, is the first snaclec to inhibit epinephrine-induced platelet aggregation. This could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders. |
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Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibitingBothrops alternatusPlatelet aggregationSnaclecsSnake venomC-type lectin-like proteins found in snake venom, known as snaclecs, have important effects on hemostasis through targeting membrane receptors, coagulation factors and other hemostatic proteins. Here, we present the isolation and functional characterization of a snaclec isolated from Bothrops alternatus venom, designated as Baltetin. We purified the protein in three chromatographic steps (anion-exchange, affinity and reversed-phase chromatography). Baltetin is a dimeric snaclec that is approximately 15 and 25 kDa under reducing and non-reducing conditions, respectively, as estimated by SDS-PAGE. Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry and Edman degradation sequencing revealed that Baltetin is a heterodimer. The first 40 amino acid residues of the N-terminal region of Baltetin subunits share a high degree of sequence identity with other snaclecs. Baltetin had a specific, dose-dependent inhibitory effect on epinephrine-induced platelet aggregation in human platelet-rich plasma, inhibiting up to 69% of platelet aggregation. Analysis of the infrared spectra suggested that the interaction between Baltetin and platelets can be attributed to the formation of hydrogen bonds between the PO32- groups in the protein and PO2- groups in the platelet membrane. This interaction may lead to membrane lipid peroxidation, which prevents epinephrine from binding to its receptor. The present work suggests that Baltetin, a new C-type lectin-like protein isolated from B. alternatus venom, is the first snaclec to inhibit epinephrine-induced platelet aggregation. This could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders.Instituto de Biotecnologia Universidade Federal de Uberlândia, Campus UberlândiaInstituto de Ciências Biomédicas Universidade Federal de Uberlândia, Campus UberlândiaUniversidade do Estado de Minas Gerais Unidade ItuiutabaInstituto Federal de Educação Ciência e Tecnologia do Triângulo Mineiro, Campus ItuiutabaUNESP - Universidade Estadual Paulista, Campus Experimental de RegistroFaculdade de Ciências Farmacêuticas de Ribeirão Preto Universidade de São PauloInstituto de Física Universidade Federal de AlagoasUNESP - Universidade Estadual Paulista, Campus Experimental de RegistroUniversidade Federal de Uberlândia (UFU)Unidade ItuiutabaCiência e Tecnologia do Triângulo MineiroUniversidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Universidade Federal de AlagoasPereira, Déborah Fernanda da CunhaMatias Ribeiro, Mariana Santosde Sousa Simamoto, Bruna BarbosaDias, Edigar Henrique VazCosta, Júnia de OliveiraSantos-Filho, Norival Alves [UNESP]Bordon, Karla de Castro FigueiredoArantes, Eliane CandianiDantas, Noelio OliveiraSilva, Anielle Christine Almeidade Oliveira, FábioMamede, Carla Cristine Neves2021-06-25T10:59:52Z2021-06-25T10:59:52Z2021-05-30info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.jchromb.2021.122695Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, v. 1173.1873-376X1570-0232http://hdl.handle.net/11449/20772110.1016/j.jchromb.2021.1226952-s2.0-85105691170Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciencesinfo:eu-repo/semantics/openAccess2024-05-03T13:20:09Zoai:repositorio.unesp.br:11449/207721Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-05-03T13:20:09Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
title |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
spellingShingle |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting Pereira, Déborah Fernanda da Cunha Bothrops alternatus Platelet aggregation Snaclecs Snake venom |
title_short |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
title_full |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
title_fullStr |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
title_full_unstemmed |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
title_sort |
Baltetin: a new C-type lectin-like isolated from Bothrops alternatus snake venom which act as a platelet aggregation inhibiting |
author |
Pereira, Déborah Fernanda da Cunha |
author_facet |
Pereira, Déborah Fernanda da Cunha Matias Ribeiro, Mariana Santos de Sousa Simamoto, Bruna Barbosa Dias, Edigar Henrique Vaz Costa, Júnia de Oliveira Santos-Filho, Norival Alves [UNESP] Bordon, Karla de Castro Figueiredo Arantes, Eliane Candiani Dantas, Noelio Oliveira Silva, Anielle Christine Almeida de Oliveira, Fábio Mamede, Carla Cristine Neves |
author_role |
author |
author2 |
Matias Ribeiro, Mariana Santos de Sousa Simamoto, Bruna Barbosa Dias, Edigar Henrique Vaz Costa, Júnia de Oliveira Santos-Filho, Norival Alves [UNESP] Bordon, Karla de Castro Figueiredo Arantes, Eliane Candiani Dantas, Noelio Oliveira Silva, Anielle Christine Almeida de Oliveira, Fábio Mamede, Carla Cristine Neves |
author2_role |
author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de Uberlândia (UFU) Unidade Ituiutaba Ciência e Tecnologia do Triângulo Mineiro Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) Universidade Federal de Alagoas |
dc.contributor.author.fl_str_mv |
Pereira, Déborah Fernanda da Cunha Matias Ribeiro, Mariana Santos de Sousa Simamoto, Bruna Barbosa Dias, Edigar Henrique Vaz Costa, Júnia de Oliveira Santos-Filho, Norival Alves [UNESP] Bordon, Karla de Castro Figueiredo Arantes, Eliane Candiani Dantas, Noelio Oliveira Silva, Anielle Christine Almeida de Oliveira, Fábio Mamede, Carla Cristine Neves |
dc.subject.por.fl_str_mv |
Bothrops alternatus Platelet aggregation Snaclecs Snake venom |
topic |
Bothrops alternatus Platelet aggregation Snaclecs Snake venom |
description |
C-type lectin-like proteins found in snake venom, known as snaclecs, have important effects on hemostasis through targeting membrane receptors, coagulation factors and other hemostatic proteins. Here, we present the isolation and functional characterization of a snaclec isolated from Bothrops alternatus venom, designated as Baltetin. We purified the protein in three chromatographic steps (anion-exchange, affinity and reversed-phase chromatography). Baltetin is a dimeric snaclec that is approximately 15 and 25 kDa under reducing and non-reducing conditions, respectively, as estimated by SDS-PAGE. Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry and Edman degradation sequencing revealed that Baltetin is a heterodimer. The first 40 amino acid residues of the N-terminal region of Baltetin subunits share a high degree of sequence identity with other snaclecs. Baltetin had a specific, dose-dependent inhibitory effect on epinephrine-induced platelet aggregation in human platelet-rich plasma, inhibiting up to 69% of platelet aggregation. Analysis of the infrared spectra suggested that the interaction between Baltetin and platelets can be attributed to the formation of hydrogen bonds between the PO32- groups in the protein and PO2- groups in the platelet membrane. This interaction may lead to membrane lipid peroxidation, which prevents epinephrine from binding to its receptor. The present work suggests that Baltetin, a new C-type lectin-like protein isolated from B. alternatus venom, is the first snaclec to inhibit epinephrine-induced platelet aggregation. This could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-25T10:59:52Z 2021-06-25T10:59:52Z 2021-05-30 |
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/10.1016/j.jchromb.2021.122695 Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, v. 1173. 1873-376X 1570-0232 http://hdl.handle.net/11449/207721 10.1016/j.jchromb.2021.122695 2-s2.0-85105691170 |
url |
http://dx.doi.org/10.1016/j.jchromb.2021.122695 http://hdl.handle.net/11449/207721 |
identifier_str_mv |
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, v. 1173. 1873-376X 1570-0232 10.1016/j.jchromb.2021.122695 2-s2.0-85105691170 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life 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_ |
1799965009412882432 |