Structure-function study of Lachesis muta rhombeata venom toxin active in thrombus formation in vivo

• Grant number: 09/02299-8
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• Start date: August 01, 2009
• End date: January 31, 2012
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Sergio Marangoni
• Grantee: Daniela Carla da Silva Damico
• Host Institution: Instituto de Biologia (IB). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil

Abstract

The snake venom of the family Viperidae is characterized by its rich protein/peptides content, able to interfere in specific stages of the haemostatic system. In general, these components stimulate or they inhibit stages key in the cascade of the clotting, fibrinolises, vascular permeability and platelets function. Venom proteins affecting blood coagulation have been classified in several families, as the serine proteinases, metalloproteinases, C-type lectin, desintegrins and phospholipases. During years, toxins that affect the blood circulation they come being isolated and characterized of several snake venoms. Studies of these factors have been contributing vastly to the discovery of several molecular mechanisms involved in these physiologic processes. Besides, these studies have been helping in the several new therapeutic agents development for the treatment of cardiovascular and haemostatic disorders. Results preliminaries show us that this venom presents PLA2 activity and anticoagulant activity. A larger number of researches are necessary to delineate the relationship between structure-function and mechanism of new anticoagulant proteins. Such studies contribute to a better understanding of "vulnerable" sites in the coagulation cascade. Thus, this study can help us to designate new strategies to develop anticoagulant therapeutic agents. (AU)

Scientific publications

(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)

TORRES-HUACO, FRANK DENIS; WERNECK, CLAUDIO C.; VICENTE, CRISTINA PONTES; VASSEQUI-SILVA, TALITA; COELHO NERY-DIEZ, ANA CLAUDIA; MENDES, CAMILA B.; ANTUNES, EDSON; MARANGONI, SERGIO; DAMICO, DANIELA C. S.. Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis muta rhombeata Snake Venom. BIOMED RESEARCH INTERNATIONAL, 2013. (09/02299-8)

DAMICO, DANIELA C. S.; VASSEQUI-SILVA, T.; TORRES-HUACO, F. D.; NERY-DIEZ, A. C. C.; DE SOUZA, R. C. G.; DA SILVA, S. L.; VICENTE, C. P.; MENDES, C. B.; ANTUNES, E.; WERNECK, C. C.; et al. LmrTX, a basic PLA(2) (D49) purified from Lachesis muta rhombeata snake venom with enzymatic-related antithrombotic and anticoagulant activity. Toxicon, v. 60, n. 5, p. 773-781, OCT 2012. (10/19916-7, 09/02299-8)

TORRES-HUACO, FRANK DENIS; WERNECK, CLAUDIO C.; VICENTE, CRISTINA PONTES; VASSEQUI-SILVA, TALITA; COELHO NERY-DIEZ, ANA CLAUDIA; MENDES, CAMILA B.; ANTUNES, EDSON; MARANGONI, SERGIO; DAMICO, DANIELA C. S.. Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis muta rhombeata Snake Venom. BIOMED RESEARCH INTERNATIONAL, v. 2013, p. 12-pg., 2013-01-01. (09/02299-8)