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A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom

This work reports the purification and functional characterization of BmooPAi, a platelet-aggregation-inhibiting factor from Bothrops moojeni snake venom. The toxin was purified by a combination of three chromatographic steps (ion-exchange on DEAE-Sephacel, molecular exclusion on Sephadex G-75, and...

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Autores principales: de Sousa, Bruna Barbosa, Mamede, Carla Cristine Neves, Matias, Mariana Santos, Pereira, Déborah Fernanda da Cunha, de Queiroz, Mayara Ribeiro, Dias, Edigar Henrique Vaz, Silva, Anielle Christine Almeida, Dantas, Noelio Oliveira, Costa, Júnia de Oliveira, de Oliveira, Fábio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5687129/
https://www.ncbi.nlm.nih.gov/pubmed/29226136
http://dx.doi.org/10.1155/2017/4315832
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author de Sousa, Bruna Barbosa
Mamede, Carla Cristine Neves
Matias, Mariana Santos
Pereira, Déborah Fernanda da Cunha
de Queiroz, Mayara Ribeiro
Dias, Edigar Henrique Vaz
Silva, Anielle Christine Almeida
Dantas, Noelio Oliveira
Costa, Júnia de Oliveira
de Oliveira, Fábio
author_facet de Sousa, Bruna Barbosa
Mamede, Carla Cristine Neves
Matias, Mariana Santos
Pereira, Déborah Fernanda da Cunha
de Queiroz, Mayara Ribeiro
Dias, Edigar Henrique Vaz
Silva, Anielle Christine Almeida
Dantas, Noelio Oliveira
Costa, Júnia de Oliveira
de Oliveira, Fábio
author_sort de Sousa, Bruna Barbosa
collection PubMed
description This work reports the purification and functional characterization of BmooPAi, a platelet-aggregation-inhibiting factor from Bothrops moojeni snake venom. The toxin was purified by a combination of three chromatographic steps (ion-exchange on DEAE-Sephacel, molecular exclusion on Sephadex G-75, and affinity chromatography on HiTrap™ Heparin HP). BmooPAi was found to be a single-chain protein with an apparent molecular mass of 32 kDa on 14% SDS-PAGE, under reducing conditions. Sequencing of BmooPAi by Edman degradation revealed the amino acid sequence LGPDIVPPNELLEVM. The toxin was devoid of proteolytic, haemorrhagic, defibrinating, or coagulant activities and induced no significant oedema or hyperalgesia. BmooPAi showed a rather specific inhibitory effect on ristocetin-induced platelet aggregation in human platelet-rich plasma, whereas it had little or no effect on platelet aggregation induced by collagen and adenosine diphosphate. The results presented in this work suggest that BmooPAi is a toxin comprised of disintegrin-like and cysteine-rich domains, originating from autolysis/proteolysis of PIII SVMPs from B. moojeni snake venom. This toxin may be of medical interest because it is a platelet aggregation inhibitor, which could potentially be developed as a novel therapeutic agent to prevent and/or treat patients with thrombotic disorders.
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spelling pubmed-56871292017-12-10 A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom de Sousa, Bruna Barbosa Mamede, Carla Cristine Neves Matias, Mariana Santos Pereira, Déborah Fernanda da Cunha de Queiroz, Mayara Ribeiro Dias, Edigar Henrique Vaz Silva, Anielle Christine Almeida Dantas, Noelio Oliveira Costa, Júnia de Oliveira de Oliveira, Fábio Biomed Res Int Research Article This work reports the purification and functional characterization of BmooPAi, a platelet-aggregation-inhibiting factor from Bothrops moojeni snake venom. The toxin was purified by a combination of three chromatographic steps (ion-exchange on DEAE-Sephacel, molecular exclusion on Sephadex G-75, and affinity chromatography on HiTrap™ Heparin HP). BmooPAi was found to be a single-chain protein with an apparent molecular mass of 32 kDa on 14% SDS-PAGE, under reducing conditions. Sequencing of BmooPAi by Edman degradation revealed the amino acid sequence LGPDIVPPNELLEVM. The toxin was devoid of proteolytic, haemorrhagic, defibrinating, or coagulant activities and induced no significant oedema or hyperalgesia. BmooPAi showed a rather specific inhibitory effect on ristocetin-induced platelet aggregation in human platelet-rich plasma, whereas it had little or no effect on platelet aggregation induced by collagen and adenosine diphosphate. The results presented in this work suggest that BmooPAi is a toxin comprised of disintegrin-like and cysteine-rich domains, originating from autolysis/proteolysis of PIII SVMPs from B. moojeni snake venom. This toxin may be of medical interest because it is a platelet aggregation inhibitor, which could potentially be developed as a novel therapeutic agent to prevent and/or treat patients with thrombotic disorders. Hindawi 2017 2017-11-01 /pmc/articles/PMC5687129/ /pubmed/29226136 http://dx.doi.org/10.1155/2017/4315832 Text en Copyright © 2017 Bruna Barbosa de Sousa et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
de Sousa, Bruna Barbosa
Mamede, Carla Cristine Neves
Matias, Mariana Santos
Pereira, Déborah Fernanda da Cunha
de Queiroz, Mayara Ribeiro
Dias, Edigar Henrique Vaz
Silva, Anielle Christine Almeida
Dantas, Noelio Oliveira
Costa, Júnia de Oliveira
de Oliveira, Fábio
A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom
title A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom
title_full A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom
title_fullStr A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom
title_full_unstemmed A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom
title_short A New Platelet-Aggregation-Inhibiting Factor Isolated from Bothrops moojeni Snake Venom
title_sort new platelet-aggregation-inhibiting factor isolated from bothrops moojeni snake venom
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5687129/
https://www.ncbi.nlm.nih.gov/pubmed/29226136
http://dx.doi.org/10.1155/2017/4315832
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