Literature DB >> 23499645

Effects of two serine proteases from Bothrops pirajai snake venom on the complement system and the inflammatory response.

Danilo L Menaldo1, Carolina P Bernardes, Juliana C Pereira, Denise S C Silveira, Carla C N Mamede, Leonilda Stanziola, Fábio de Oliveira, Luciana S Pereira-Crott, Lúcia H Faccioli, Suely V Sampaio.   

Abstract

The present study aimed to evaluate the effects of two serine proteases from Bothrops pirajai snake venom, named BpirSP27 and BpirSP41, on the complement system and the inflammatory response. The effects of these enzymes on the human complement system were assessed by kinetic hemolytic assays, evaluating the hemolysis promoted by the classical/lectin (CP/LP) and alternative (AP) pathways after incubation of normal human serum with the serine proteases. The results suggested that these enzymes were able to induce modulation of CP/LP and AP at different levels: BpirSP41 showed higher inhibitory effects on the hemolytic activity of CP/LP than BpirSP27, with inhibition values close to 40% and 20%, respectively, for the highest concentration assayed. Regarding AP, both enzymes showed percentages of inhibition of the hemolytic activity around 20% for the highest concentrations tested, indicating similar effects on this complement pathway. The proinflammatory effects of B. pirajai serine proteases were evaluated regarding their ability to induce paw edema, variations in the pain threshold and leukocyte recruitment at the site of injection. Both showed mild effects on these inflammatory processes, leading to low levels of increase of paw volumes and decrease in pain thresholds in rats up to 6 h after injection, and inducing neutrophil recruitment without significant increases in the total number of leukocytes in the inflammatory exudates after 6 and 24 h of administration into mice peritoneal cavity. These results suggest that serine proteases must present a minor role in the inflammation caused by B. pirajai snake venom.
Copyright © 2013 Elsevier B.V. All rights reserved.

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Year:  2013        PMID: 23499645     DOI: 10.1016/j.intimp.2013.02.023

Source DB:  PubMed          Journal:  Int Immunopharmacol        ISSN: 1567-5769            Impact factor:   4.932


  13 in total

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2.  Bothrops snake venoms and their isolated toxins, an L-amino acid oxidase and a serine protease, modulate human complement system pathways.

Authors:  Lorena Rocha Ayres; Alex Dos Reis Récio; Sandra Mara Burin; Juliana Campos Pereira; Andrea Casella Martins; Suely Vilela Sampaio; Fabíola Attié de Castro; Luciana Simon Pereira-Crott
Journal:  J Venom Anim Toxins Incl Trop Dis       Date:  2015-08-13

3.  P-I snake venom metalloproteinase is able to activate the complement system by direct cleavage of central components of the cascade.

Authors:  Giselle Pidde-Queiroz; Fábio Carlos Magnoli; Fernanda C V Portaro; Solange M T Serrano; Aline Soriano Lopes; Adriana Franco Paes Leme; Carmen W van den Berg; Denise V Tambourgi
Journal:  PLoS Negl Trop Dis       Date:  2013-10-31

4.  CR-LAAO, an L-amino acid oxidase from Calloselasma rhodostoma venom, as a potential tool for developing novel immunotherapeutic strategies against cancer.

Authors:  Tássia R Costa; Danilo L Menaldo; Karina F Zoccal; Sandra M Burin; Alexandre F Aissa; Fabíola A de Castro; Lúcia H Faccioli; Lusânia M Greggi Antunes; Suely V Sampaio
Journal:  Sci Rep       Date:  2017-02-16       Impact factor: 4.379

5.  Venom from Bothrops lanceolatus, a Snake Species Native to Martinique, Potently Activates the Complement System.

Authors:  Marie Delafontaine; Isadora Maria Villas-Boas; Giselle Pidde; Carmen W van den Berg; Laurence Mathieu; Joël Blomet; Denise V Tambourgi
Journal:  J Immunol Res       Date:  2018-07-15       Impact factor: 4.818

6.  Effect of Vipera ammodytes ammodytes Snake Venom on the Human Cytokine Network.

Authors:  Francisc Boda; Krisztina Banfai; Kitti Garai; Augustin Curticapean; Lavinia Berta; Emese Sipos; Krisztian Kvell
Journal:  Toxins (Basel)       Date:  2018-06-25       Impact factor: 4.546

7.  Cytotoxic and inflammatory potential of a phospholipase A2 from Bothrops jararaca snake venom.

Authors:  Rafhaella C A Cedro; Danilo L Menaldo; Tássia R Costa; Karina F Zoccal; Marco A Sartim; Norival A Santos-Filho; Lúcia H Faccioli; Suely V Sampaio
Journal:  J Venom Anim Toxins Incl Trop Dis       Date:  2018-11-23

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

Authors:  Caroline R C Costa; Mariana Novo Belchor; Caroline F B Rodrigues; Daniela de Oliveira Toyama; Marcos A de Oliveira; Danielle P Novaes; Marcos Hikari Toyama
Journal:  Int J Mol Sci       Date:  2018-08-15       Impact factor: 5.923

9.  Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi.

Authors:  Maria Teresa Romero-Gutiérrez; Carlos Eduardo Santibáñez-López; Juana María Jiménez-Vargas; Cesar Vicente Ferreira Batista; Ernesto Ortiz; Lourival Domingos Possani
Journal:  Toxins (Basel)       Date:  2018-09-05       Impact factor: 4.546

10.  New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom.

Authors:  Fernanda G Amorim; Danilo L Menaldo; Sante E I Carone; Thiago A Silva; Marco A Sartim; Edwin De Pauw; Loic Quinton; Suely V Sampaio
Journal:  Toxins (Basel)       Date:  2018-11-28       Impact factor: 4.546

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