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Effects of Two Serine Proteases from Bothrops Pirajai Snake Venom on the Complement System and the Inflammatory Response

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Effects of Two Serine Proteases from Bothrops Pirajai Snake Venom on the Complement System and the Inflammatory Response View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector International Immunopharmacology 15 (2013) 764–771 Contents lists available at SciVerse ScienceDirect International Immunopharmacology journal homepage: www.elsevier.com/locate/intimp Effects of two serine proteases from Bothrops pirajai snake venom on the complement system and the inflammatory response Danilo L. Menaldo a,⁎, Carolina P. Bernardes a, Juliana C. Pereira a, Denise S.C. Silveira a, Carla C.N. Mamede b,c, Leonilda Stanziola b,c, Fábio de Oliveira b,c, Luciana S. Pereira-Crott a, Lúcia H. Faccioli a, Suely V. Sampaio a,⁎ a Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo (FCFRP-USP), Ribeirão Preto, SP, Brazil b Instituto de Ciências Biomédicas, Universidade Federal de Uberlândia (ICBIM-UFU), Uberlândia, MG, Brazil c Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte, MG, Brazil article info abstract Article history: The present study aimed to evaluate the effects of two serine proteases from Bothrops pirajai snake venom, Received 12 October 2012 named BpirSP27 and BpirSP41, on the complement system and the inflammatory response. The effects of Received in revised form 2 February 2013 these enzymes on the human complement system were assessed by kinetic hemolytic assays, evaluating Accepted 27 February 2013 the hemolysis promoted by the classical/lectin (CP/LP) and alternative (AP) pathways after incubation of nor- Available online 15 March 2013 mal 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 Keywords: Snake venoms activity of CP/LP than BpirSP27, with inhibition values close to 40% and 20%, respectively, for the highest con- Bothrops pirajai centration assayed. Regarding AP, both enzymes showed percentages of inhibition of the hemolytic activity Serine proteases around 20% for the highest concentrations tested, indicating similar effects on this complement pathway. Thrombin-like enzymes The proinflammatory effects of B. pirajai serine proteases were evaluated regarding their ability to induce Complement system paw edema, variations in the pain threshold and leukocyte recruitment at the site of injection. Both showed fl In ammation 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 in- flammation caused by B. pirajai snake venom. © 2013 Elsevier B.V. Open access under the Elsevier OA license. 1. Introduction pain, heat, redness and edema, accompanied or not by loss of function of the affected tissue or organ [2]. Envenomation by Bothrops snakes is characterized by severe local The inflammatory response promoted by Bothrops snake venoms tissue damage, hemorrhage, myonecrosis and prominent inflamma- is strictly related to the progress of tissue damage, resulting in tion. The inflammatory response is an adaptive process in which the edema and pain, leukocyte infiltration and release of cytokines body responds to tissue injury or local infection in order to reestablish and other proinflammatory mediators [3–5]. Although most of the homeostasis, allowing the healing and restoration of damaged sites available studies indicate a predominant role of phospholipases A2 [1].Inflammation is initiated and conducted by mediators of plasma and metalloproteases in the inflammatory effects promoted by or cellular origin, which promote the typical signs of this response: snake venoms [6,7], the role of serine proteases and other compo- nents of the venom on the inflammatory process should not be discarded [1]. The toxic effects promoted by snake venom serine proteases Abbreviations: AP, alternative pathway; CP/LP, classical/lectin pathways; LPS, lipo- polysaccharides; NHS, normal human serum; PBS, phosphate buffered saline; SVSPs, (SVSPs) are mainly related to their actions on hemostasis, acting on snake venom serine proteases. several components of the coagulation cascade and the fibrinolytic ⁎ Corresponding authors at: Departamento de Análises Clínicas, Toxicológicas e and kallikrein–kinin systems, which leads to a hemostatic imbalance Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de on preys [8,9]. The vast majority of SVSPs are able to promote blood São Paulo, FCFRP-USP, Av. do Café, s/nº, CEP 14040-903, Ribeirão Preto-SP, Brazil. clotting and resemble, at least partially, thrombin, a multifunctional Tel.: +55 16 36024286; fax: +55 16 36024725. E-mail addresses: [email protected] (D.L. Menaldo), [email protected] protease with essential role in coagulation, thereby being referred (S.V. Sampaio). to as snake venom thrombin-like enzymes [10,11]. 1567-5769 © 2013 Elsevier B.V. Open access under the Elsevier OA license. http://dx.doi.org/10.1016/j.intimp.2013.02.023 D.L. Menaldo et al. / International Immunopharmacology 15 (2013) 764–771 765 Considering the similar chemical nature of the components of the 2.3. Normal human serum (NHS) coagulation and complement systems, both of which contain series of serine proteases that form proteolytic cascades, one would expect that NHS used in the assays on the complement system was obtained SVSPs could also present significant effects on the complement system. from blood of healthy volunteers of both sexes, aged 20 to 40 years, Also, interactions between both systems have often been proposed collected in the absence of anticoagulants. The blood was allowed to [12,13], which could play an important role after snake envenomations clot at room temperature for 1 h, and the serum was separated from and for subsequent inflammatory reactions and complications. the clot by centrifugation at 500 ×g for 10 minutes at 4 °C. Then, serum The human complement system is composed of more than 30 was pooled, aliquoted and frozen at −80 °C until the experiments. All plasma and cell surface proteins that participate in many important procedures involving humans were approved by the Research Ethics biological processes, including the activation of the inflammatory pro- Committee of FCFRP-USP (CEP/FCFRP nº. 123/2011). cess in response to the generation of proteolytic fragments of its compo- nents, and the promotion of phagocytosis and lysis of pathogens and 2.4. Effects on the complement system altered cells by opsonization processes and formation of the membrane attack complex (MAC). Depending on the stimulus, the activation of the The effects of B. pirajai serine proteases on the human comple- complement system can occur by three main paths: the classical (CP), ment system were observed using in vitro assays to assess the hemo- alternative (AP) or lectin (LP) pathways [14].Somestudiesalsoindicate lytic activity promoted by NHS, source of complement components, the existence of additional complement activation paths in the plasma, preincubated for 1 h at 37 °C with different concentrations of the which are dependent of different coagulation factors such as thrombin, enzymes. Prior to these assays, the serine proteases were investigated FXa, FXIa and plasmin [13,15]. for their ability to induce direct hemolysis by incubation with rabbit Although several snake venoms present activity on the complement or sheep erythrocytes in the absence of NHS. system [16–18], studies on the action of isolated toxins, especially from Bothrops venoms, are still scarce. Most snake venom toxins described 2.4.1. Preparation of erythrocyte suspensions with anticomplementary action belong to the class of metalloproteases For CP/LP, blood from three sheep was collected by venipuncture [19–21], and in relation to SVSPs, one of the few published studies is of the jugular vein into plastic tubes containing the same volume of that of Yamamoto and coworkers [22], which showed that flavoxobin Alsever sterile solution (2.05% glucose, 0.8% sodium citrate and from Trimeresurus flavoviridis snakevenomwasabletospecifically 0.42% NaCl). Aliquots of blood were centrifuged at 500 ×g for 10 mi- cleave human complement protein C3, thus acting as a C3 convertase nutes and the pellet of red cells was then washed with triethanolamine −4 −4 enzyme. buffer pH 7.4 containing 1.4 × 10 MCaCl2,5×10 MMgSO4 and Bothrops pirajai serine proteases, called BpirSP27 and BpirSP41, 0.1% gelatin (TEA–Ca2+–Mg2+ buffer), preparing a 5% erythrocyte have recently been characterized by our research group, presenting suspension with approximately 1.2 × 109 cells/mL [24].Then,this significant differences in their molecular masses, N-glycosylation suspension was sensitized with rabbit anti-sheep erythrocyte antibod- levels and N-terminal sequences, besides different fibrin(ogen)olytic, ies (hemolysin), kept at 4 °C for 15 minutes and the absorbance at coagulant and platelet-aggregating activities [23]. Considering the few 700 nm was adjusted to 0.7–0.8 in a spectrophotometer (Beckman data available in the literature regarding the action of SVSPs on the com- Coulter, model DU-70). plement system and the inflammatory response, this study aimed at the For AP, blood from two rabbits was collected by puncture of the evaluation of the effects of B. pirajai serine proteases on the different central ear artery into plastic tubes containing the same volume of human complement pathways, as well as the proinflammatory poten- Alsever sterile solution. Then, blood was incubated with the same vol- tial of these enzymes by the examination of their ability to induce ume of a TEA–EDTA chelating solution for 15 minutes at 37 °C. After edema, pain and recruitment of immune cells. centrifugation, the red cells were washed with TEA–Mg2+ buffer, suspended in Alsever’s solution and stored at 4 °C. For the hemolytic assays, aliquots of this suspension were washed with triethanolamine 2.
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