Purification and Characterization of Jararassin-I, A Thrombin-like Enzyme from &amp;lt;italic&amp;gt;Bothrops jararaca&amp;lt;/italic&amp;gt; Snake Venom

Vieira, Débora; Watanabe, Leandra; Sant’Ana, Carolina D.; Marcussi, Silvana; Sampaio, Suely Vilela; Soares, Andreimar Martins; Arni, R.K.

doi:10.1093/abbs/36.12.798

Cited by 25 publications

(17 citation statements)

References 20 publications

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“…), BpirSP-39 presented a higher coagulant potential. Other purified serine proteases such as PA-BJ and Jararassin-I from Bothrops jararaca venom show considerably reduced coagulant activity, with MCDs of 5 of 10 μ g, respectively [55, 56]. …”

Section: Discussionmentioning

confidence: 99%

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Zaqueo

Kayano

Simões-Silva

et al. 2014

BioMed Research International

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This paper presents a novel serine protease (SP) isolated from Bothrops pirajai, a venomous snake found solely in Brazil that belongs to the Viperidae family. The identified SP, named BpirSP-39, was isolated by three chromatographic steps (size exclusion, bioaffinity, and reverse phase chromatographies). The molecular mass of BpirSP-39 was estimated by SDS-PAGE and confirmed by mass spectrometry (39,408.32 Da). The protein was able to form fibrin networks, which was not observed in the presence of serine protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF). Furthermore, BpirSP-39 presented considerable thermal stability and was apparently able to activate factor XIII of the blood coagulation cascade, unlike most serine proteases. BpirSP-39 was capable of hydrolyzing different chromogenic substrates tested (S-2222, S-2302, and S-2238) while Cu2+ significantly diminished BspirSP-39 activity on the three tested substrates. The enzyme promoted platelet aggregation and also exhibited fibrinogenolytic, fibrinolytic, gelatinolytic, and amidolytic activities. The multiple alignment showed high sequence similarity to other thrombin-like enzymes from snake venoms. These results allow us to conclude that a new SP was isolated from Bothrops pirajai snake venom.

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Section: Discussionmentioning

confidence: 99%

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Zaqueo

Kayano

Simões-Silva

et al. 2014

BioMed Research International

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“…In addition, C. durissus terrificus and Lachesis sp. venoms could also clot human fibrinogen, with no action upon B. jararaca fibrinogen [31]. …”

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of the Ontogenetic Variability in Plasma Composition of Juvenile and AdultBothrops jararacaSnakes

Grego

Tanaka

Tanaka-Azevedo

2013

International Journal of Proteomics

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The ontogenetic variability in venom composition of some snake genera, including Bothrops, as well as the biological implications of such variability and the search of new molecules that can neutralize the toxic components of these venoms have been the subject of many studies. Thus, considering the resistance of Bothrops jararaca to the toxic action of its own venom and the ontogenetic variability in venom composition described in this species, a comparative study of the plasma composition of juvenile and adult B. jararaca snakes was performed through a proteomic approach based on 2D electrophoresis and mass spectrometry, which allowed the identification of proteins that might be present at different levels during ontogenetic development. Among the proteins identified by mass spectrometry, antihemorrhagic factor Bj46a was found only in adult plasma. Moreover, two spots identified as phospholipase A2 inhibitors were significantly increased in juvenile plasma, which can be related to the higher catalytic PLA2 activity shown by juvenile venom in comparison to that of adult snakes. This work shows the ontogenetic variability of B. jararaca plasma, and that these changes can be related to the ontogenetic variability described in its venom.

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“…Chemical treatments for inhibition of specific enzymatic activities of L. obliqua venom Samples of Lobe (0.3 mg/ml) or thrombin (0.2 mg/ml) were added to well plates containing: (a) phenylmethanesulfonyl fluoride (PMSF) and (b) D-Phe-ProArg-chloromethylketone (PPACK) for serine proteases inhibition [20]; (c) trans-epoxysuccinyl-L-leucylamido (4-guanidino)-butane (E-64) for cysteine proteases inhibition [21]; (d) p-bromophenacyl bromide (p-BPB) for phospholipases A 2 inhibition [22] or (e) ethylene glycolbis(aminoethyl ether)-N,N,N 0 ,N 0 -tetraacetic acid (EGTA) for inhibition of metal-dependent proteases [21]. Samples were incubated for 2 h at 37°C, followed by overnight dialysis against 20 mM Tris.HCl, pH 7.4.…”

Section: Platelet Adhesion Assaymentioning

confidence: 99%

Lonomia obliqua venomous secretion induces human platelet adhesion and aggregation

Berger

Reck

Terra

et al. 2010

J Thromb Thrombolysis

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The caterpillar Lonomia obliqua is a venomous animal that causes numerous accidents, especially in southern Brazil, where it is considered a public health problem. The clinical manifestations include several haemostatic disturbances that lead to a hemorrhagic syndrome. Considering that platelets play a central role in hemostasis, in this work we investigate the effects of L. obliqua venomous secretion upon blood platelets responses in vitro. Results obtained shows that L. obliqua venom directly induces aggregation and ATP secretion in human washed platelets in a dose-dependent manner. Electron microscopy studies clearly showed that the venomous bristle extract was also able to produce direct platelets shape change and adhesion as well as activation and formation of platelet aggregates. Differently from other enzyme inhibitors, the venom-induced platelet aggregation was significatively inhibited by p-bromophenacyl bromide, a specific inhibitor of phospholipases A2. Additional experiments with different pharmacological antagonists indicate that the aggregation response triggered by the venom active components occurs through a calcium-dependent mechanism involving arachidonic acid metabolite(s) of the cyclooxygenase pathway and activation of phosphodiesterase 3A, an enzyme that leads to the consumption of intracellular cAMP content. It was additionally found that L. obliqua-induced platelet aggregation was independent of ADP release. Altogether, these findings are in line with the need for a better understanding of the complex hemorrhagic syndrome resulting from the envenomation caused by L. obliqua caterpillars, and can also give new insights into the management of its clinical profile.

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Purification and Characterization of Jararassin-I, A Thrombin-like Enzyme from <italic>Bothrops jararaca</italic> Snake Venom

Cited by 25 publications

References 20 publications

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Proteomic Analysis of the Ontogenetic Variability in Plasma Composition of Juvenile and AdultBothrops jararacaSnakes

Lonomia obliqua venomous secretion induces human platelet adhesion and aggregation

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