Self-proteolysis regulation in the Bothrops jararaca venom: The metallopeptidases and their intrinsic peptidic inhibitor

2008 ◽  
Vol 147 (4) ◽  
pp. 424-433 ◽  
Author(s):  
Rafael Marques-Porto ◽  
Ivo Lebrun ◽  
Daniel C. Pimenta
Keyword(s):  
Bothrops Jararaca ◽  
Proteolysis Regulation

Properties of Fibrinogen Cleaved by Jararhagin, a Metalloproteinase from the Venom of Bothrops jararaca

1994 ◽  
Vol 72 (02) ◽  
pp. 244-249 ◽  
Author(s):  
Aura S Kamiguti ◽  
Joseph R Slupsky ◽  
Mirko Zuzel ◽  
Charles R M Hay
Keyword(s):  
Platelet Aggregation ◽  
Platelet Function ◽  
Fibrin Clot ◽  
Clot Formation ◽  
Human Fibrinogen ◽  
Activated Platelets ◽  
Bothrops Jararaca ◽  
Platelet Binding ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule

SummaryHaemorrhagic metalloproteinases from Bothrops jararaca and other venoms degrade vessel-wall and plasma proteins involved in platelet plug and fibrin clot formation. These enzymes also cause proteolytic digestion of fibrinogen which has been suggested to cause defective platelet function. Fibrinogen degradation by jararhagin, a metalloproteinase from B. jararaca, and the effect of jararhagin fibrinogenolysis on both platelet aggregation and fibrin clot formation were investigated. Jararhagin was found to cleave human fibrinogen in the C-terminal region of the Aα-chain giving rise to a 285-290 kDa fibrinogen molecule lacking the Aα-chain RGD 572-574 platelet-binding site. Platelet binding and aggregation of ADP-activated platelets is unaffected by this modification. This indicates that the lost site is not essential for platelet aggregation, and that the remaining platelet binding sites located in the N-terminal portion of Aα chains (RGD 95-97) and the C-terminal of γ chains (dodecapeptide 400-411) are unaffected by jararhagin-digestion of fibrinogen. Fibrin clot formation with thrombin of this remnant fibrinogen molecule was defective, with poor polymerization of fibrin monomers but normal release of FPA. The abnormal polymerization could be explained by the loss of one of the two complementary polymerization sites required for side-by-side association of fibrin protofibrils. Jararhagin-induced inhibition of platelet function, an important cause of haemorrhage in envenomed patients, is not caused by proteolysis of fibrinogen, as had been thought, and the mechanism remains to be elucidated.

Ineffectiveness of the inhibition of the main haemorrhagic metalloproteinase from Bothrops jararaca venom by its only plasma inhibitor, α2-macroglobulin

1994 ◽  
Vol 1200 (3) ◽  
pp. 307-314 ◽  
Author(s):  
Aura S. Kamiguti ◽  
Howard P. Desmond ◽  
R.David G. Theakston ◽  
Charles R.M. Hay ◽  
Mirko Zuzel
Keyword(s):  
Bothrops Jararaca ◽  
Α2 Macroglobulin

scholarly journals Correction: Inhibitory Effects of Hydroethanolic Leaf Extracts of Kalanchoe brasiliensis and Kalanchoe pinnata (Crassulaceae) against Local Effects Induced by Bothrops jararaca Snake Venom

PLoS ONE ◽  
2017 ◽  
Vol 12 (2) ◽  
pp. e0172598 ◽  
Author(s):  
Júlia Morais Fernandes ◽  
Juliana Félix-Silva ◽  
Lorena Medeiros da Cunha ◽  
Jacyra Antunes dos Santos Gomes ◽  
Emerson Michell da Silva Siqueira ◽  
...  
Keyword(s):  
Snake Venom ◽  
Inhibitory Effects ◽  
Leaf Extracts ◽  
Local Effects ◽  
Bothrops Jararaca ◽  
Kalanchoe Pinnata

Therapeutic possibilities of Bothrops jararaca in high dilution

2021 ◽  
Vol 10 (36) ◽  
pp. 215-217
Author(s):  
Eduardo Costa Gaia Nazareth ◽  
Francisco José De Freitas
Keyword(s):  
Bacterial Infections ◽  
Complement C3 ◽  
Clinical Aspects ◽  
High Dilution ◽  
Complement Components ◽  
Physical Description ◽  
Bothrops Jararaca ◽  
High Dilutions ◽  
The Many ◽  
Therapeutic Possibilities

Introduction: The knowledge and use of the venom of Bothrops jararaca in high dilutions is still quite limited. One of the important properties is the use of one of its components, bradykinin, for the development of antihypertensive medication known as captopril. Other situations, such as clinical, local and systemic should receive more depth to the composition of Materia Medica related to various medical actions on the man and mammals in general. The systemic action of the bite of this snake, includes hemostasis disorders, culminating as bleeding gums, in addition to sweating, hypertension, and hypothermia. The action includes local pain and swelling with bruising, bleeding and often blistering and tissue necrosis. The action on the immune system, through action on the complement C3 and other complement components may show its possible use in cases of bacterial infections, including mycobacteria, as presented in the study of 1970 Vanessa Birdsey, "Interactions of poisons toxic with the addition, "the journal of Immunology 1971. Today, this poison has a toxicology published by Anibal Melgarejo, "Venomous Animals of Brazil", 2003, which subsidizes the development of study for its use in high dilutions, and a comprehensive study of the biology of the animal itself. Published studies on biomolecular analysis add more details about the relations of the poison and mammals. All these characteristics suggest the use of poison as a homeopathic remedy. Objective: To investigate the therapeutic possibilities in high dilutions of the venom of the snake Bothrops jararaca, expanding its clinical use. Methodology: Methodological description of this poison in contemporary bases including: Origin, physical description chemistry, toxicology, pharmacology and medicine in preparation of high dilution, general action, specific actions on systems or organs, sensations, modalities, concomitants, etiological indications relations main clinics. Results: Defining the therapeutic indications such as modulation of the complement system, action on the cardiovascular system, among other uses, by Bothrops jararaca in high dilution. Conclusion: This evaluation can be used for different sources of products and allows the rational use of Bothrops jararaca in high dilution. The results can and should be complemented by clinical studies and pathogenetic. Bacterial infectious diseases such as tuberculosis and leprosy, and autoimmune disease LES and may receive treatment studies with the drug based on Bothrops jararaca snake venom because they are indirectly associated with them via similarity of the failure of complement, an important marker for bacterial the defense of mammals. Action on clinical aspects like hypertension, sweating, hypothermia and necrosis shall be seen. Perhaps the search for the stimulation of complement show a new pathway for the harmonization, long-predicted by Hahnemann, Hering and searched for among the many that followed the creator of this therapy.

Bothrops jararaca fibrinogen and its resistance to hydrolysis evoked by snake venoms

2008 ◽  
Vol 151 (4) ◽  
pp. 428-432 ◽  
Author(s):  
Carolina O. Vieira ◽  
Aparecida S. Tanaka ◽  
Ida S. Sano-Martins ◽  
Karen B. Morais ◽  
Marcelo L. Santoro ◽  
...  
Keyword(s):  
Snake Venoms ◽  
Bothrops Jararaca

An in-depth snake venom proteopeptidome characterization: Benchmarking Bothrops jararaca

2017 ◽  
Vol 151 ◽  
pp. 214-231 ◽  
Author(s):  
Carolina A. Nicolau ◽  
Paulo C. Carvalho ◽  
Inácio L.M. Junqueira-de-Azevedo ◽  
André Teixeira-Ferreira ◽  
Magno Junqueira ◽  
...  
Keyword(s):  
Snake Venom ◽  
Bothrops Jararaca
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