Pulmonary mechanic and lung histology injury induced by Crotalus durissus terrificus snake venom

Toxicon ◽  
2008 ◽  
Vol 51 (7) ◽  
pp. 1158-1166 ◽  
Author(s):  
Paula Naomi Nonaka ◽  
César Ferreira Amorim ◽  
Ana Claudia Paneque Peres ◽  
César Augusto Melo e Silva ◽  
Stella R. Zamuner ◽  
...  
Keyword(s):  
Snake Venom ◽  
Crotalus Durissus Terrificus ◽  
Lung Histology ◽  
Pulmonary Mechanic ◽  
Crotalus Durissus

Pulmonary mechanic and lung histology induced by Crotalus durissus cascavella snake venom

Toxicon ◽  
2017 ◽  
Vol 137 ◽  
pp. 144-149 ◽  
Author(s):  
Joselito de Oliveira Neto ◽  
João Alison de Moraes Silveira ◽  
Daniel Silveira Serra ◽  
Daniel de Araújo Viana ◽  
Diva Maria Borges-Nojosa ◽  
...  
Keyword(s):  
Snake Venom ◽  
Lung Histology ◽  
Pulmonary Mechanic ◽  
Crotalus Durissus Cascavella ◽  
Crotalus Durissus

L-aminoacid oxidase from Crotalus durissus terrificus snake venom and its antibacterial potential

Toxicon ◽  
2019 ◽  
Vol 168 ◽  
pp. S13
Author(s):  
Leonardo Melo ◽  
Lidiane Nunes Barbosa ◽  
Rui Seabra Ferreira Junior ◽  
Benedito Barraviera ◽  
Luciana Curtolo De Barros ◽  
...  
Keyword(s):  
Snake Venom ◽  
Crotalus Durissus Terrificus ◽  
Crotalus Durissus ◽  
Antibacterial Potential

scholarly journals Edema Induced by a Crotalus durissus terrificus Venom Serine Protease (Cdtsp 2) Involves the PAR Pathway and PKC and PLC Activation

2018 ◽  
Vol 19 (8) ◽  
pp. 2405 ◽  
Author(s):  
Caroline Costa ◽  
Mariana Belchor ◽  
Caroline Rodrigues ◽  
Daniela Toyama ◽  
Marcos de Oliveira ◽  
...  
Keyword(s):  
Serine Protease ◽  
Snake Venom ◽  
Serine Proteases ◽  
Three Dimensional ◽  
Negative Control ◽  
Protease Activated Receptors ◽  
Crotalus Durissus Terrificus ◽  
Three Dimensional Modeling ◽  
Cox 2 ◽  
Crotalus Durissus

Snake venom serine proteases (SVSPs) represent an essential group of enzymatic toxins involved in several pathophysiological effects on blood homeostasis. Some findings suggest the involvement of this class of enzymatic toxins in inflammation. In this paper, we purified and isolated a new gyroxin isoform from the Crotalus durissus terrificus (Cdt) venom, designated as Cdtsp 2, which showed significant proinflammatory effects in a murine model. In addition, we performed several studies to elucidate the main pathway underlying the edematogenic effect induced by Cdtsp 2. Enzymatic assays and structural analysis (primary structure analysis and three-dimensional modeling) were closely performed with pharmacological assays. The determination of edematogenic activity was performed using Cdtsp 2 isolated from snake venom, and was applied to mice treated with protein kinase C (PKC) inhibitor, phospholipase C (PLC) inhibitor, dexamethasone (Dexa), antagonists for protease-activated receptors (PARs), or saline (negative control). Additionally, we measured the levels of cyclooxygenase 2 (COX-2), malondialdehyde (MDA), and prostaglandin E2 (PGE2). Cdtsp 2 is characterized by an approximate molecular mass of 27 kDa, an isoelectric point (pI) of 4.5, and significant fibrinolytic activity, as well as the ability to hydrolyze Nα-benzoyl-l-arginine 4-nitroanilide (BAPNA). Its primary and three-dimensional structures revealed Cdtsp 2 as a typical snake venom serine protease that induces significant edema via the metabolism of arachidonic acid (AA), involving PARs, PKC, PLC, and COX-2 receptors, as well as inducing a significant increase in MDA levels. Our results showed that Cdtsp 2 is a serine protease with significant enzymatic activity, and it may be involved in the degradation of PAR1 and PAR2, which activate PLC and PKC to mobilize AA, while increasing oxidative stress. In this article, we provide a new perspective for the role of SVSPs beyond their effects on blood homeostasis.

Involvement of the cholinergic system in the antinociceptive activity of Crotalus durissus terrificus snake venom

Toxicon ◽  
1996 ◽  
Vol 34 (1) ◽  
pp. 22
Author(s):  
F.A. Hoffman ◽  
M.P. Moreira ◽  
R. Giorgi ◽  
M.M. Bernardi ◽  
Y. Curi
Keyword(s):  
Snake Venom ◽  
Cholinergic System ◽  
Antinociceptive Activity ◽  
Crotalus Durissus Terrificus ◽  
Crotalus Durissus

Insights into the structure, function and stability of bordonein-L, the first L-amino acid oxidase from Crotalus durissus terrificus snake venom

Biochimie ◽  
2019 ◽  
Vol 163 ◽  
pp. 33-49 ◽  
Author(s):  
Gisele A. Wiezel ◽  
Joane K. Rustiguel ◽  
David Morgenstern ◽  
Karina F. Zoccal ◽  
Lucia H. Faccioli ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structure Function ◽  
Snake Venom ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Crotalus Durissus Terrificus ◽  
Crotalus Durissus
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