Secondary hemostasis studies of crude venom and isolated proteins from the snake Crotalus durissus terrificus
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , |
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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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 |
|
_version_ |
1808128434706055168 |