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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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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 Modesto1 / Inácio Loióla Meireles Junqueira-de-Azevedo2 / Ana Gisele C. Neves-Ferreira3 / Márcio Fritzen4 / Maria Luíza Vilela Oliva5 / Paulo Lee Ho6 / Jonas Perales7 / Ana Marisa Chudzinski-Tavassi8

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Corresponding author

Citation Information: Biological Chemistry. Volume 386, Issue 6, Pages 589–600, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2005.069, July 2005

Publication History

Received:
November 10, 2004
Accepted:
April 7, 2005
Published Online:
2005-07-07

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

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