Importance of jararhagin disintegrin-like and cysteine-rich domains in the early events of local inflammatory response

Clissa, Patrı́cia Bianca; Lopes-Ferreira, Mônica; Della-Casa, Maisa S.; Farsky, Sandra Helena Poliselli; Moura-da-Silva, Ana Maria

doi:10.1016/j.toxicon.2006.02.001

Cited by 61 publications

(42 citation statements)

References 23 publications

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“…2 The presence of these enzymes in a wide variety of snakes suggests that they play important roles in toxicity. SVMPs possess multidomain functions, and it has been shown that the catalytic site is not the only crucial domain enabling this class of toxin to cause hemorrhage and inflammation (58). This is evidenced by a form of SVMP, jararhagin C, that lacks the catalytic domain yet is capable of activating an acute inflammatory response in a mouse model (58).…”

Section: Discussionmentioning

confidence: 99%

“…SVMPs possess multidomain functions, and it has been shown that the catalytic site is not the only crucial domain enabling this class of toxin to cause hemorrhage and inflammation (58). This is evidenced by a form of SVMP, jararhagin C, that lacks the catalytic domain yet is capable of activating an acute inflammatory response in a mouse model (58). Platelets are the main target of these enzymes in the disruption of hemostasis that occurs by inhibition of interaction with collagen and/or von Willebrand factor using various mechanisms that result in systemic bleeding.…”

Section: Discussionmentioning

confidence: 99%

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The Diversity of Bioactive Proteins in Australian Snake Venoms

Birrell

Earl

Wallis

et al. 2007

Molecular & Cellular Proteomics

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Australian elapid snakes are among the most venomous in the world. Their venoms contain multiple components that target blood hemostasis, neuromuscular signaling, and the cardiovascular system. We describe here a comprehensive approach to separation and identification of the venom proteins from 18 of these snake species, representing nine genera. The venom protein components were separated by two-dimensional PAGE and identified using mass spectrometry and de novo peptide sequencing. The venoms are complex mixtures showing up to 200 protein spots varying in size from <7 to over 150 kDa and in pI from 3 to >10. These include many proteins identified previously in Australian snake venoms, homologs identified in other snake species, and some novel proteins. In many cases multiple trains of spots were typically observed in the higher molecular mass range (>20 kDa) (indicative of posttranslational modification). Venom proteins and their posttranslational modifications were characterized using specific antibodies, phosphoprotein-and glycoprotein-specific stains, enzymatic digestion, lectin binding, and antivenom reactivity. In the lower molecular weight range, several proteins were identified, but the predominant species were phospholipase A 2 and ␣-neurotoxins, both represented by different sequence variants. The higher molecular weight range contained proteases, nucleotidases, oxidases, and homologs of mammalian coagulation factors. This information together with the identification of several novel proteins (metalloproteinases, vespryns, phospholipase A 2 inhibitors, protein-disulfide isomerase, 5-nucleotidases, cysteinerich secreted proteins, C-type lectins, and acetylcholinesterases) aids in understanding the lethal mechanisms of elapid snake venoms and represents a valuable resource for future development of novel human therapeutics.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The Diversity of Bioactive Proteins in Australian Snake Venoms

Birrell

Earl

Wallis

et al. 2007

Molecular & Cellular Proteomics

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“…SVMPs, c-type lectins and other toxins are known to induce inflammation by recruiting inflammatory cells and mediators. These actions activate the early events of an acute inflammatory response at bitten site as well as the systemic target sites Clissa et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Propensity of crocin to offset Vipera russelli venom induced oxidative stress mediated neutrophil apoptosis: a biochemical insight

et al. 2014

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Viper envenomation results in inflammation at the bitten site as well as target organs. Neutrophils and other polymorphonuclear leukocytes execute inflammation resolving mechanism and will undergo apoptosis after completing the task. However, the target specific toxins induce neutrophil apoptosis at the bitten site and in circulation prior to their function, thus reducing their number. Circulating activated neutrophils are major source of inflammatory cytokines and leakage of reactive oxygen species (ROS)/other toxic intermediates resulting in aggravation of inflammatory response at the bitten/target site. Therefore, neutralization of venom induced neutrophil apoptosis reduces inflammation besides increasing the functional neutrophil population. Therefore, the present study investigates the venom induced perturbances in isolated human neutrophils and its neutralization by crocin (Crocus sativus) a potent antioxidant carotenoid. Human neutrophils on treatment with venom resulted in altered ROS generation, intracellular Ca 2? mobilization, mitochondrial membrane depolarization, cyt-c translocation, caspase activation, phosphatidylserine externalization and DNA damage. On the other hand significant protection against oxidative stress and apoptosis were evidenced in crocin pre-treated groups. In conclusion the viper venom induces neutrophil apoptosis and results in aggravation of inflammation and tissue damage. The present study demands the necessity of an auxiliary therapy in addition to antivenin therapy to treat secondary/overlooked complications of envenomation.

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“…Os domínios tipo-disintegrina/rico em cisteínas da jararhagina são suficientes para ativar localmente os eventos iniciais da resposta inflamatória aguda (CLISSA et al, 2006 -8 (COELHO et al, 2004). Além disso, a alternagina-C, composta pelos domínios tipo-disintegrina e rico em cisteínas, purificada do veneno de B. alternatus, induz a migração de neutrófilos (MARIANO-OLIVEIRA et al, 2003).…”

Section: Domínios Não Catalíticos Das Metaloproteinases De Venenos Deunclassified

Estudo sobre a função dos domínios não catalíticos do HF3, uma metaloproteínase do veneno da serpente Bothrops jararaca, na sua interação com alvos celulares e plasmáticos.

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Importance of jararhagin disintegrin-like and cysteine-rich domains in the early events of local inflammatory response

Cited by 61 publications

References 23 publications

The Diversity of Bioactive Proteins in Australian Snake Venoms

The Diversity of Bioactive Proteins in Australian Snake Venoms

Propensity of crocin to offset Vipera russelli venom induced oxidative stress mediated neutrophil apoptosis: a biochemical insight

Estudo sobre a função dos domínios não catalíticos do HF3, uma metaloproteínase do veneno da serpente Bothrops jararaca, na sua interação com alvos celulares e plasmáticos.

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