Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus

Detalhes bibliográficos
Autor(a) principal: Sousa, Ivancia D.L.
Data de Publicação: 2019
Outros Autores: Barbosa, Ayrton R., Salvador, Guilherme H.M. [UNESP], Frihling, Breno E.F., Santa-Rita, Paula H., Soares, Andreimar M., Pessôa, Hilzeth L.F., Marchi-Salvador, Daniela P.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.ijbiomac.2019.03.059
http://hdl.handle.net/11449/187449
Resumo: Among the activities triggered by Crotalus durissus terrificus snake venom, coagulation is intriguing and contradictory since the venom contains both coagulant and anticoagulant precursor proteins. This work describes the in vitro effects of crude venom and purified proteins from snake Crotalus durissus terrificus as they affect coagulation factors of clotting pathways. Coagulant and/or anticoagulant activities of crude venom, and purified proteins were all analyzed directly in human plasma. Clots formed by crude venom and Gyroxin presented as flexible hyaline masses in punctiform distribution. Clot formation time evaluation of isolated proteins with PT and APTT assays made it possible to infer that these proteins interfere in all coagulation pathways. However, regarding ophidism by C. d. terrificus, Gyroxin acts directly, breaking down fibrinogen to fibrin and increasing the amount plasminogen activator, which results in the formation of thrombi. Crotoxin complex, Crotoxin A and Crotoxin B proteins can act in prothrombinase complex formation; Crotoxin B can inhibit prothrombinase complex formation by direct interaction with Factor Xa. Crotamine interacts with negatively charged regions of differing coagulation factors in all coagulation pathways, and possesses a whole set of activities causing dysfunction, activation and/or inhibition of natural anticoagulants and disturbing hemostasis.
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spelling Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificusActivated Partial Thromboplastin TimeAnticoagulant proteinsBrazilian rattlesnakeOphidismProthrombin TimeAmong the activities triggered by Crotalus durissus terrificus snake venom, coagulation is intriguing and contradictory since the venom contains both coagulant and anticoagulant precursor proteins. This work describes the in vitro effects of crude venom and purified proteins from snake Crotalus durissus terrificus as they affect coagulation factors of clotting pathways. Coagulant and/or anticoagulant activities of crude venom, and purified proteins were all analyzed directly in human plasma. Clots formed by crude venom and Gyroxin presented as flexible hyaline masses in punctiform distribution. Clot formation time evaluation of isolated proteins with PT and APTT assays made it possible to infer that these proteins interfere in all coagulation pathways. However, regarding ophidism by C. d. terrificus, Gyroxin acts directly, breaking down fibrinogen to fibrin and increasing the amount plasminogen activator, which results in the formation of thrombi. Crotoxin complex, Crotoxin A and Crotoxin B proteins can act in prothrombinase complex formation; Crotoxin B can inhibit prothrombinase complex formation by direct interaction with Factor Xa. Crotamine interacts with negatively charged regions of differing coagulation factors in all coagulation pathways, and possesses a whole set of activities causing dysfunction, activation and/or inhibition of natural anticoagulants and disturbing hemostasis.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Departamento de Biologia Molecular CCEN UFPBDepartamento de Física e Biofísica Instituto de Biociências UNESPBiotério da Universidade Católica Dom Bosco PRPG UCDBFundação Oswaldo Cruz Unidade de Rondônia FiocruzDepartamento de Física e Biofísica Instituto de Biociências UNESPUniversidade Federal da Paraíba (UFPB)Universidade Estadual Paulista (Unesp)UCDBFiocruzSousa, Ivancia D.L.Barbosa, Ayrton R.Salvador, Guilherme H.M. [UNESP]Frihling, Breno E.F.Santa-Rita, Paula H.Soares, Andreimar M.Pessôa, Hilzeth L.F.Marchi-Salvador, Daniela P.2019-10-06T15:36:26Z2019-10-06T15:36:26Z2019-06-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article127-133http://dx.doi.org/10.1016/j.ijbiomac.2019.03.059International Journal of Biological Macromolecules, v. 131, p. 127-133.1879-00030141-8130http://hdl.handle.net/11449/18744910.1016/j.ijbiomac.2019.03.0592-s2.0-85062802674Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInternational Journal of Biological Macromoleculesinfo:eu-repo/semantics/openAccess2021-10-23T19:23:31Zoai:repositorio.unesp.br:11449/187449Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T14:54:38.255893Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
title Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
spellingShingle Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
Sousa, Ivancia D.L.
Activated Partial Thromboplastin Time
Anticoagulant proteins
Brazilian rattlesnake
Ophidism
Prothrombin Time
title_short Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
title_full Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
title_fullStr Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
title_full_unstemmed Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
title_sort Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
author Sousa, Ivancia D.L.
author_facet Sousa, Ivancia D.L.
Barbosa, Ayrton R.
Salvador, Guilherme H.M. [UNESP]
Frihling, Breno E.F.
Santa-Rita, Paula H.
Soares, Andreimar M.
Pessôa, Hilzeth L.F.
Marchi-Salvador, Daniela P.
author_role author
author2 Barbosa, Ayrton R.
Salvador, Guilherme H.M. [UNESP]
Frihling, Breno E.F.
Santa-Rita, Paula H.
Soares, Andreimar M.
Pessôa, Hilzeth L.F.
Marchi-Salvador, Daniela P.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal da Paraíba (UFPB)
Universidade Estadual Paulista (Unesp)
UCDB
Fiocruz
dc.contributor.author.fl_str_mv Sousa, Ivancia D.L.
Barbosa, Ayrton R.
Salvador, Guilherme H.M. [UNESP]
Frihling, Breno E.F.
Santa-Rita, Paula H.
Soares, Andreimar M.
Pessôa, Hilzeth L.F.
Marchi-Salvador, Daniela P.
dc.subject.por.fl_str_mv Activated Partial Thromboplastin Time
Anticoagulant proteins
Brazilian rattlesnake
Ophidism
Prothrombin Time
topic Activated Partial Thromboplastin Time
Anticoagulant proteins
Brazilian rattlesnake
Ophidism
Prothrombin Time
description Among the activities triggered by Crotalus durissus terrificus snake venom, coagulation is intriguing and contradictory since the venom contains both coagulant and anticoagulant precursor proteins. This work describes the in vitro effects of crude venom and purified proteins from snake Crotalus durissus terrificus as they affect coagulation factors of clotting pathways. Coagulant and/or anticoagulant activities of crude venom, and purified proteins were all analyzed directly in human plasma. Clots formed by crude venom and Gyroxin presented as flexible hyaline masses in punctiform distribution. Clot formation time evaluation of isolated proteins with PT and APTT assays made it possible to infer that these proteins interfere in all coagulation pathways. However, regarding ophidism by C. d. terrificus, Gyroxin acts directly, breaking down fibrinogen to fibrin and increasing the amount plasminogen activator, which results in the formation of thrombi. Crotoxin complex, Crotoxin A and Crotoxin B proteins can act in prothrombinase complex formation; Crotoxin B can inhibit prothrombinase complex formation by direct interaction with Factor Xa. Crotamine interacts with negatively charged regions of differing coagulation factors in all coagulation pathways, and possesses a whole set of activities causing dysfunction, activation and/or inhibition of natural anticoagulants and disturbing hemostasis.
publishDate 2019
dc.date.none.fl_str_mv 2019-10-06T15:36:26Z
2019-10-06T15:36:26Z
2019-06-15
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.ijbiomac.2019.03.059
International Journal of Biological Macromolecules, v. 131, p. 127-133.
1879-0003
0141-8130
http://hdl.handle.net/11449/187449
10.1016/j.ijbiomac.2019.03.059
2-s2.0-85062802674
url http://dx.doi.org/10.1016/j.ijbiomac.2019.03.059
http://hdl.handle.net/11449/187449
identifier_str_mv International Journal of Biological Macromolecules, v. 131, p. 127-133.
1879-0003
0141-8130
10.1016/j.ijbiomac.2019.03.059
2-s2.0-85062802674
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv International Journal of Biological Macromolecules
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 127-133
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
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