Cotiarinase is a novel prothrombin activator from the venom of Bothrops cotiara

Autor(es)

Kitano, Eduardo S. ^[1] ; Garcia, Thalita C. ^[1] ; Menezes, Milene C. ^[1] ; Tashima, Alexandre K. ^{[2, 1]} ; Zelanis, Andre ^[1] ; Serrano, Solange M. T. ^[1]

Afiliação do(s) autor(es)

^[1] Inst Butantan, CAT Cepid, Lab Especial Toxinol Aplicada, BR-05503000 Sao Paulo - Brazil

^[2] Univ Fed Sao Paulo, Dept Ciencias Exatas & Terra, Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Biochimie; v. 95, n. 8, p. 1655-1659, AUG 2013.
• Citações Web of Science: 6

Resumo

Snake venom serine proteinases (SVSPs) may affect hemostatic pathways by specifically activating components involved in coagulation, fibrinolysis and platelet aggregation or by unspecific proteolytic degradation. In this study, we purified and characterized an SVSP from Bothrops cotiara venom, named cotiarinase, which generated thrombin upon incubation with prothrombin. Cotiarinase was isolated by a two-step procedure including gel-filtration and cation-exchange chromatographies and showed a single protein band with a molecular mass of 29 kDa by SDS-polyacrylamide gel electrophoresis under reducing conditions. Identification of cotiarinase by mass spectrometric analysis revealed peptides that matched sequences of viperid SVSPs. Cotiarinase did not show fibrinogen-clotting, platelet-aggregating, fibrino-genolytic and factor X activating activities. Upon incubation with prothrombin the generation of thrombin was detected using the peptide substrate D-Phe-Pip-Arg-pNA. Moreover, mass spectrometric identification of prothrombin fragments generated by cotiarinase in the absence of co-factors (phospholipids, factor Va, factor Xa and Ca2+ ions), indicated the limited proteolysis of this protein to release prothrombin 1, fragment 1 and thrombin. Cotiarinase is a novel SVSP that acts on prothrombin to release active thrombin that does not match any group of the current classification of snake venom prothrombin activators. (C) 2013 Elsevier Masson SAS. All rights reserved. (AU)

• Processo FAPESP: 98/14307-9 - Center for Applied Toxinology
• Beneficiário: Hugo Aguirre Armelin
• Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
• Processo FAPESP: 11/11308-0 - Estudo do proteoma de folhas de cultivares e genótipos de cana-de-açúcar
• Beneficiário: Eduardo Shigueo Kitano
• Linha de fomento: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 11/08514-8 - Estudo do degradoma do HF3, uma metaloproteinase hemorrágica da classe P-III do veneno da serpente Bothrops jararaca, sobre fibroblastos em cultura
• Beneficiário: André Zelanis Palitot Pereira
• Linha de fomento: Bolsas no Brasil - Pós-Doutorado