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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2016: 3.273

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1437-4315
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Volume 386, Issue 6

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

Jeanne Claíne de Albuquerque Modesto
  • Laboratório de Bioquímica e Biofísica, Instituto Butantan, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil
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/ Inácio Loióla Meireles Junqueira-de-Azevedo
  • Centro de Biotecnologia, Instituto Butantan, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil
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/ Ana Gisele C. Neves-Ferreira
  • Departamento de Fisiologia e Farmacodinâmica, Instituto Osvaldo Cruz-Fiocruz, Rio de Janeiro 21045-900, RJ, Brazil
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/ Márcio Fritzen
  • Laboratório de Bioquímica e Biofísica, Instituto Butantan, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil
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/ Maria Luíza Vilela Oliva
  • Departamento de Bioquímica, Universidade Federal de São Paulo, São Paulo 0550801, SP, Brazil
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/ Paulo Lee Ho
  • Centro de Biotecnologia, Instituto Butantan, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil and Instituto de Biociências e Instituto de Química da Universidade de São Paulo, São Paulo 0550801, SP, Brazil
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/ Jonas Perales
  • Departamento de Fisiologia e Farmacodinâmica, Instituto Osvaldo Cruz-Fiocruz, Rio de Janeiro 21045-900, RJ, Brazil
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/ Ana Marisa Chudzinski-Tavassi
  • Laboratório de Bioquímica e Biofísica, Instituto Butantan, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil
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Published Online: 2005-07-07 | DOI: https://doi.org/10.1515/BC.2005.069

Abstract

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, SDS-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.

Keywords: Bothrops insularis; coagulation; endothelial cell; metalloprotease; prothrombin activator; snake venom

About the article

Corresponding author


Received: November 10, 2004

Accepted: April 7, 2005

Published Online: 2005-07-07

Published in Print: 2005-06-01


Citation Information: Biological Chemistry, Volume 386, Issue 6, Pages 589–600, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.069.

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