Lonomia obliqua venom action on fibrinolytic system
- Autores
- Fritzen, Márcio; Schattner, Mirta Ana; Quintana Ribeiro, Ana Laura; Correia Batista, Isabel De Fátima; Ventura, Janaina; Carlos Prezoto, Benedito; Chudzinski-Tavassi, Ana Marisa
- Año de publicación
- 2003
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Accidental skin contact with the Lonomia caterpillar bristles causes a severe hemorrhagic syndrome. While fibrinolytic activation is considered to be the main cause of hemorrhage in Lonomia achelous envenomation, a consumptive coagulopathy was found to be a major component involved in the bleeding complications observed in patients envenomed by contact with Lonomia obliqua. Although we have previously observed that in L. obliqua envenomations, fibrinolysis activation appeared to be secondary to coagulation system activation, there are no reports regarding the ability of L. obliqua venom to activate directly fibrinolytic pathways. We examined the action of L. obliqua crude bristles extract (LOCBE) on several fibrinolytic system components. We demonstrated that LOCBE degraded the A-alpha fibrinogen chain only at high concentrations and after long incubation times. Under these conditions, LOCBE also induced prolongation of the fibrinogen clotting time, but no clot lysis was observed before 24 h. LOCBE did not contain t-PA- or u-PA-like activities. Gel filtration and SDS-PAGE showed that LOCBE did not induce FXIII digestion. In addition, no FXIII activity inhibition was detected by dansylcadaverin method. FXIII levels remained unchanged when FXIII was measured in fibrinogen-depleted LOCBE-treated rat plasma, suggesting that the observed 50% FXIII reduction in rats was related to consumption. In conclusion, our results clearly demonstrated that LOCBE did not display either FXIII inhibition or degradation nor fibrinolytic activity. Furthermore, although proteolytic activity on Aα fibrinogen chain was observed, cross-linked fibrin was not affected by LOCBE. © 2003 Elsevier Ltd. All rights reserved.
Fil: Fritzen, Márcio. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: Schattner, Mirta Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Medicina Experimental. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental; Argentina
Fil: Quintana Ribeiro, Ana Laura. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: Correia Batista, Isabel De Fátima. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: Ventura, Janaina. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: Carlos Prezoto, Benedito. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: Chudzinski-Tavassi, Ana Marisa. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil - Materia
-
Caterpillar
Envenomation
Factor Xiii
Fibrinogen
Fibrinolysis - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/66450
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Lonomia obliqua venom action on fibrinolytic systemFritzen, MárcioSchattner, Mirta AnaQuintana Ribeiro, Ana LauraCorreia Batista, Isabel De FátimaVentura, JanainaCarlos Prezoto, BeneditoChudzinski-Tavassi, Ana MarisaCaterpillarEnvenomationFactor XiiiFibrinogenFibrinolysishttps://purl.org/becyt/ford/3.2https://purl.org/becyt/ford/3Accidental skin contact with the Lonomia caterpillar bristles causes a severe hemorrhagic syndrome. While fibrinolytic activation is considered to be the main cause of hemorrhage in Lonomia achelous envenomation, a consumptive coagulopathy was found to be a major component involved in the bleeding complications observed in patients envenomed by contact with Lonomia obliqua. Although we have previously observed that in L. obliqua envenomations, fibrinolysis activation appeared to be secondary to coagulation system activation, there are no reports regarding the ability of L. obliqua venom to activate directly fibrinolytic pathways. We examined the action of L. obliqua crude bristles extract (LOCBE) on several fibrinolytic system components. We demonstrated that LOCBE degraded the A-alpha fibrinogen chain only at high concentrations and after long incubation times. Under these conditions, LOCBE also induced prolongation of the fibrinogen clotting time, but no clot lysis was observed before 24 h. LOCBE did not contain t-PA- or u-PA-like activities. Gel filtration and SDS-PAGE showed that LOCBE did not induce FXIII digestion. In addition, no FXIII activity inhibition was detected by dansylcadaverin method. FXIII levels remained unchanged when FXIII was measured in fibrinogen-depleted LOCBE-treated rat plasma, suggesting that the observed 50% FXIII reduction in rats was related to consumption. In conclusion, our results clearly demonstrated that LOCBE did not display either FXIII inhibition or degradation nor fibrinolytic activity. Furthermore, although proteolytic activity on Aα fibrinogen chain was observed, cross-linked fibrin was not affected by LOCBE. © 2003 Elsevier Ltd. All rights reserved.Fil: Fritzen, Márcio. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: Schattner, Mirta Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Medicina Experimental. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental; ArgentinaFil: Quintana Ribeiro, Ana Laura. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: Correia Batista, Isabel De Fátima. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: Ventura, Janaina. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: Carlos Prezoto, Benedito. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: Chudzinski-Tavassi, Ana Marisa. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilPergamon-Elsevier Science Ltd2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/66450Fritzen, Márcio; Schattner, Mirta Ana; Quintana Ribeiro, Ana Laura; Correia Batista, Isabel De Fátima; Ventura, Janaina; et al.; Lonomia obliqua venom action on fibrinolytic system; Pergamon-Elsevier Science Ltd; Thrombosis Research; 112; 1-2; 12-2003; 105-1100049-3848CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0049384803005863info:eu-repo/semantics/altIdentifier/doi/10.1016/j.thromres.2003.11.005info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:44:43Zoai:ri.conicet.gov.ar:11336/66450instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:44:44.145CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Lonomia obliqua venom action on fibrinolytic system |
title |
Lonomia obliqua venom action on fibrinolytic system |
spellingShingle |
Lonomia obliqua venom action on fibrinolytic system Fritzen, Márcio Caterpillar Envenomation Factor Xiii Fibrinogen Fibrinolysis |
title_short |
Lonomia obliqua venom action on fibrinolytic system |
title_full |
Lonomia obliqua venom action on fibrinolytic system |
title_fullStr |
Lonomia obliqua venom action on fibrinolytic system |
title_full_unstemmed |
Lonomia obliqua venom action on fibrinolytic system |
title_sort |
Lonomia obliqua venom action on fibrinolytic system |
dc.creator.none.fl_str_mv |
Fritzen, Márcio Schattner, Mirta Ana Quintana Ribeiro, Ana Laura Correia Batista, Isabel De Fátima Ventura, Janaina Carlos Prezoto, Benedito Chudzinski-Tavassi, Ana Marisa |
author |
Fritzen, Márcio |
author_facet |
Fritzen, Márcio Schattner, Mirta Ana Quintana Ribeiro, Ana Laura Correia Batista, Isabel De Fátima Ventura, Janaina Carlos Prezoto, Benedito Chudzinski-Tavassi, Ana Marisa |
author_role |
author |
author2 |
Schattner, Mirta Ana Quintana Ribeiro, Ana Laura Correia Batista, Isabel De Fátima Ventura, Janaina Carlos Prezoto, Benedito Chudzinski-Tavassi, Ana Marisa |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
Caterpillar Envenomation Factor Xiii Fibrinogen Fibrinolysis |
topic |
Caterpillar Envenomation Factor Xiii Fibrinogen Fibrinolysis |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.2 https://purl.org/becyt/ford/3 |
dc.description.none.fl_txt_mv |
Accidental skin contact with the Lonomia caterpillar bristles causes a severe hemorrhagic syndrome. While fibrinolytic activation is considered to be the main cause of hemorrhage in Lonomia achelous envenomation, a consumptive coagulopathy was found to be a major component involved in the bleeding complications observed in patients envenomed by contact with Lonomia obliqua. Although we have previously observed that in L. obliqua envenomations, fibrinolysis activation appeared to be secondary to coagulation system activation, there are no reports regarding the ability of L. obliqua venom to activate directly fibrinolytic pathways. We examined the action of L. obliqua crude bristles extract (LOCBE) on several fibrinolytic system components. We demonstrated that LOCBE degraded the A-alpha fibrinogen chain only at high concentrations and after long incubation times. Under these conditions, LOCBE also induced prolongation of the fibrinogen clotting time, but no clot lysis was observed before 24 h. LOCBE did not contain t-PA- or u-PA-like activities. Gel filtration and SDS-PAGE showed that LOCBE did not induce FXIII digestion. In addition, no FXIII activity inhibition was detected by dansylcadaverin method. FXIII levels remained unchanged when FXIII was measured in fibrinogen-depleted LOCBE-treated rat plasma, suggesting that the observed 50% FXIII reduction in rats was related to consumption. In conclusion, our results clearly demonstrated that LOCBE did not display either FXIII inhibition or degradation nor fibrinolytic activity. Furthermore, although proteolytic activity on Aα fibrinogen chain was observed, cross-linked fibrin was not affected by LOCBE. © 2003 Elsevier Ltd. All rights reserved. Fil: Fritzen, Márcio. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: Schattner, Mirta Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Medicina Experimental. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental; Argentina Fil: Quintana Ribeiro, Ana Laura. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: Correia Batista, Isabel De Fátima. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: Ventura, Janaina. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: Carlos Prezoto, Benedito. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: Chudzinski-Tavassi, Ana Marisa. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil |
description |
Accidental skin contact with the Lonomia caterpillar bristles causes a severe hemorrhagic syndrome. While fibrinolytic activation is considered to be the main cause of hemorrhage in Lonomia achelous envenomation, a consumptive coagulopathy was found to be a major component involved in the bleeding complications observed in patients envenomed by contact with Lonomia obliqua. Although we have previously observed that in L. obliqua envenomations, fibrinolysis activation appeared to be secondary to coagulation system activation, there are no reports regarding the ability of L. obliqua venom to activate directly fibrinolytic pathways. We examined the action of L. obliqua crude bristles extract (LOCBE) on several fibrinolytic system components. We demonstrated that LOCBE degraded the A-alpha fibrinogen chain only at high concentrations and after long incubation times. Under these conditions, LOCBE also induced prolongation of the fibrinogen clotting time, but no clot lysis was observed before 24 h. LOCBE did not contain t-PA- or u-PA-like activities. Gel filtration and SDS-PAGE showed that LOCBE did not induce FXIII digestion. In addition, no FXIII activity inhibition was detected by dansylcadaverin method. FXIII levels remained unchanged when FXIII was measured in fibrinogen-depleted LOCBE-treated rat plasma, suggesting that the observed 50% FXIII reduction in rats was related to consumption. In conclusion, our results clearly demonstrated that LOCBE did not display either FXIII inhibition or degradation nor fibrinolytic activity. Furthermore, although proteolytic activity on Aα fibrinogen chain was observed, cross-linked fibrin was not affected by LOCBE. © 2003 Elsevier Ltd. All rights reserved. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-12 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/66450 Fritzen, Márcio; Schattner, Mirta Ana; Quintana Ribeiro, Ana Laura; Correia Batista, Isabel De Fátima; Ventura, Janaina; et al.; Lonomia obliqua venom action on fibrinolytic system; Pergamon-Elsevier Science Ltd; Thrombosis Research; 112; 1-2; 12-2003; 105-110 0049-3848 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/66450 |
identifier_str_mv |
Fritzen, Márcio; Schattner, Mirta Ana; Quintana Ribeiro, Ana Laura; Correia Batista, Isabel De Fátima; Ventura, Janaina; et al.; Lonomia obliqua venom action on fibrinolytic system; Pergamon-Elsevier Science Ltd; Thrombosis Research; 112; 1-2; 12-2003; 105-110 0049-3848 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0049384803005863 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.thromres.2003.11.005 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Pergamon-Elsevier Science Ltd |
publisher.none.fl_str_mv |
Pergamon-Elsevier Science Ltd |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844613407895977984 |
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13.070432 |