Advanced search
Start date
Betweenand
Related content

ANTITHROMBOTIC AND TROMBOLYTIC ACTIVITIES OF BATROXASE, A METALLOPROTEINASE PURIFIED FROM THE VENOM OF Bothrops atrox SNAKE, IN EXPERIMENTAL ANIMAL MODELS.

Grant number: 12/21569-9
Support Opportunities:Scholarships in Brazil - Post-Doctoral
Effective date (Start): March 01, 2013
Effective date (End): February 28, 2017
Field of knowledge:Health Sciences - Pharmacy
Principal Investigator:Suely Vilela
Grantee:Anna Laura Bechara Jacob Ferreira
Host Institution: Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Associated research grant:11/23236-4 - Native and recombinant animal toxins: functional, structural and molecular analysis, AP.TEM

Abstract

Animal venoms are constituted by a variety of substances with toxic effects, which may act either isolated or in synergy, causing different types of damage to the victim or pray. To study chemical and functional characteristics of the isolated toxins is interesting not only due to its relevance in the poisoning, but also due to its potential as a source of bioactive molecules that can be used as a model of new drugs for the treatment of different pathological processes. Due to the importance of blood coagulation and platelet aggregation in cardiovascular and cerebrovascular diseases, snake venom proteins, which interfere in these processes, have received considerable attention in recent years. Batroxase, which is a metalloproteinase isolated from Bothrops atrox (Pará) snake venom, was recently purified and biochemically characterized in our laboratory. Batroxase showed antithrombotic and thrombolytic activity in vitro, as it is capable to proteolyse components of the coagulation cascade, as fibrinogen and fibrin. In this project we aim at investigate batroxase's activity to the hemostasis of rats, analysing its thrombolytic and antithrombotic activity, in comparison with clinically relevant drugs like tPA and heparin, respectively, in two thrombosis models: arterial and venous. Nevertheless, we will observe the influence of batroxase over the blood pressure, heart rate, and coagulation measurements of the studied animals. With the beginning of the functional characterization of batroxase, we will be able to initiate exploring the therapeutic potential of this animal toxin for the development and production of new drugs in the future.

News published in Agência FAPESP Newsletter about the scholarship:
Articles published in other media outlets (0 total):
More itemsLess items
VEICULO: TITULO (DATA)
VEICULO: TITULO (DATA)

Scientific publications (4)
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
MENALDO, DANILO L.; JACOB-FERREIRA, ANNA L.; BERNARDES, CAROLINA P.; CINTRA, ADELIA C. O.; SAMPAIO, SUELY V.. Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A(2) from Bothrops atrox snake venom. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 21, . (12/21569-9, 11/23236-4, 12/11963-1)
JACOB-FERREIRA, ANNA L.; MENALDO, DANILO L.; SARTIM, MARCO A.; RIUL, THALITA B.; DIAS-BARUFFI, MARCELO; SAMPAIO, SUELY V.. Antithrombotic activity of Batroxase, a metalloprotease from Bothrops atrox venom, in a model of venous thrombosis. International Journal of Biological Macromolecules, v. 95, p. 263-267, . (11/23236-4, 12/21569-9)
DANILO L. MENALDO; ANNA L. JACOB-FERREIRA; CAROLINA P. BERNARDES; ADÉLIA C. O. CINTRA; SUELY V. SAMPAIO. Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A 2 fromBothrops atrox snake venom. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 21, p. 0-0, . (12/21569-9, 12/11963-1, 11/23236-4)
JACOB-FERREIRA, ANNA L.; MENALDO, DANILO L.; BERNARDES, CAROLINA P.; SARTIM, MARCO A.; DE ANGELIS, CELIO D.; TANUS-SANTOS, JOSE E.; SAMPAIO, SUELY V.. Evaluation of the in vivo thrombolytic activity of a metalloprotease from Bothrops atrox venom using a model of venous thrombosis. Toxicon, v. 109, p. 18-25, . (11/23236-4, 12/21569-9)

Please report errors in scientific publications list using this form.