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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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]
Total Authors: 6
Affiliation:
[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
Total Affiliations: 2
Document type: Journal article
Source: Biochimie; v. 95, n. 8, p. 1655-1659, AUG 2013.
Web of Science Citations: 6
Abstract

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)

FAPESP's process: 98/14307-9 - Center for Applied Toxinology
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 11/11308-0 - Proteomic analysis of leaves of sugarcane cultivars and genotypes
Grantee:Eduardo Shigueo Kitano
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 11/08514-8 - Study of the degradome of HF3, a PIII-class snake venom metalloproteinase from Bothrops jararaca venom, on cultured fibroblasts
Grantee:André Zelanis Palitot Pereira
Support type: Scholarships in Brazil - Post-Doctorate