Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains

Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains

Autor Modesto, JCD Google Scholar
Junqueira-de-Azevedo, ILM Google Scholar
Neves-Ferreira, AGC Google Scholar
Fritzen, M. Google Scholar
Oliva, MLV Google Scholar
Ho, P. L. Google Scholar
Perales, J. Google Scholar
Chudzinski-Tavassi, A. M. Google Scholar
Instituição Inst Butantan
Inst Burantan
Fiocruz MS
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Resumo The first low-molecular-mass metalloprotease presenting prothrombin activating activity was purified from Bothrops insularis venom and named insularinase A. It is a single-chain protease with a molecular mass of 22 639 Da. cDNA sequence analysis revealed that the disintegrin domain of the precursor protein is post-translationally processed, producing the mature insularinase A. Analysis of its deduced amino acid sequence showed a high similarity with several fibrin(ogen)olytic metalloproteases and only a moderate similarity with prothrombin activators. However, SIDS-PAGE of prothrombin after activation by insularinase A showed fragment patterns similar to those generated by group A prothrombin activators, which convert prothrombin into meizothrombin independently of the prothrombinase complex. in addition, insularinase A activates factor X and hydrolyses fibrinogen and fibrin. Chelating agents fully inhibit all insularinase A activities. Insularinase A induced neither detachment nor apoptosis of human endothelial cells and was also not able to trigger an endothelial proinflammatory cell response. Nitric oxide and prostacyclin levels released by endothelial cells were significantly increased after treatment with insularinase A. Our results show that, although its primary structure is related to class P-I fibrin(ogen)olytic metalloproteases, insularinase A is functionally similar to group A prothrombin activators.
Assunto Bothrops insularis
coagulation
endothelial cell
metalloprotease
prothrombin activator
snake venom
Idioma Inglês
Data 2005-06-01
Publicado em Biological Chemistry. Berlin: Walter de Gruyter Gmbh, v. 386, n. 6, p. 589-600, 2005.
ISSN 1431-6730 (Sherpa/Romeo, fator de impacto)
Editor Walter de Gruyter Gmbh
Extensão 589-600
Fonte http://dx.doi.org/10.1515/BC.2005.069
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000230256800010
URI http://repositorio.unifesp.br/handle/11600/28341

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