Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity

Siigur, Ene; Tõnismägi, Külli; Trummal, Katrin; Samel, Mari; Vija, Heiki; Subbi, Juhan; Siigur, Jüri

doi:10.1016/s0304-4165(01)00206-9

Cited by 56 publications

(44 citation statements)

References 40 publications

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“…As for factor X, we observed that MooA induced the cleavage of the zymogen heavy chain at Arg 194 -Ile 195 , which led to the formation of enzymatically active factor Xa. A similar pattern of proteolytic activation has also been observed for endogenous factor VII/Tissue factor complex and other SVMPs (Hofmann and Bon 1987b;Takeya et al 1992;Siigur et al 2001;Samel et al 2003;Sun et al 2010).…”

Section: Discussionsupporting

confidence: 70%

“…Other SVMPs show a similar versatile ability to promote activation of blood coagulation factors. RVV-X and VLFXA are PIIId SVMPs that activate factors IX and X but preferentially the latter (Takeya et al 1992;Siigur et al 2001). Additionally, insularinase-A, another PIII metalloprotease isolated from Bothrops insularis venom, preferentially activates prothrombin but also activates factor X (Modesto et al 2005).…”

Section: Discussionmentioning

confidence: 99%

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Moojenactivase, a novel pro-coagulant PIIId metalloprotease isolated from Bothrops moojeni snake venom, activates coagulation factors II and X and induces tissue factor up-regulation in leukocytes

et al. 2015

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Coagulopathies following snakebite are triggered by pro-coagulant venom toxins, in which metalloproteases play a major role in envenomation-induced coagulation disorders by acting on coagulation cascade, platelet function and fibrinolysis. Considering this relevance, here we describe the isolation and biochemical characterization of moojenactivase (MooA), a metalloprotease from Bothrops moojeni snake venom, and investigate its involvement in hemostasis in vitro. MooA is a glycoprotein of 85,746.22 Da, member of the PIIId group of snake venom metalloproteases, composed of three linked disulfide-bonded chains: an N-glycosylated heavy chain, and two light chains. The venom protease induced human plasma clotting in vitro by activating on both blood coagulation factors II (prothrombin) and X, which in turn generated α-thrombin and factor Xa, respectively. Additionally, MooA induced expression of tissue factor (TF) on the membrane surface of peripheral blood mononuclear cells (PBMC), which led these cells to adopt pro-coagulant characteristics. MooA was also shown to be involved with production of the inflammatory mediators TNF-α, IL-8 and MCP-1, suggesting an association between MooA pro-inflammatory stimulation of PBMC and TF up-regulation. We also observed aggregation of washed platelets when in presence of MooA; however, the protease had no effect on fibrinolysis. Our findings show that MooA is a novel hemostatically active metalloprotease, which may lead to the development of coagulopathies during B. moojeni envenomation. Moreover, the metalloprotease may contribute to the development of new diagnostic tools and pharmacological approaches applied to hemostatic disorders.

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Section: Discussionsupporting

confidence: 70%

Section: Discussionmentioning

confidence: 99%

Moojenactivase, a novel pro-coagulant PIIId metalloprotease isolated from Bothrops moojeni snake venom, activates coagulation factors II and X and induces tissue factor up-regulation in leukocytes

et al. 2015

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“…In addition, it was noted that these activators cleave the heavy chain of factor X at two additional positions, an activity not seen with RVV-X. Very recently, an RVV-X like activator was purified from the venom of Vipera lebetina which, like RVV-X, was found capable of activating factor IX [33].…”

Section: Metalloprotease Activatorsmentioning

confidence: 99%

Snake Venom Activators of Factor X: An Overview

Tans

Rosing²

2001

Pathophysiol Haemos Thromb

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Activators of blood coagulation factor X have been described in the venom of many snake species belonging to the genus Viperidae and Crotalidae as well as from a few Elapid species. Based on the structural and functional properties of purified activating principles, factor X activators are either metalloproteases or serine proteases. The best known activator is RVV-X from Russell’s viper (Daboia russelli), a metalloprotease consisting of a heavy chain containing the catalytic domain and two light chains which share homology with C-type lectins and which are thought to exert a regulatory function in the Ca²⁺-dependent activation of factor X. This activator is also one of the best examples of the use of exogenous activators in coagulation research and in addition it is used in many diagnostic research kits. In this paper, an overview is given of the structural and functional properties of snake venom factor X activators thus far described in the literature.

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“…Among these, Elapidea family enjoys a strong hemorrhage effect, whose hemorrhage factor has been derived (25,26).…”

Section: Discussionmentioning

confidence: 99%

Properties of biological and biochemical effects of the Iranian saw-scaled viper (Echis carinatus) venom

Babaie¹,

Salmanizadeh²,

Zolfagharian³

et al. 2014

BLL

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Abstract:The venom of Echis carinatus is rich in proteins and peptides effective on the hemostatic system. This venom is contains metalloproteinase which convert prothrombin to meizothrombin. The prothrombin activator which leads to the formation of small blood clots inside the blood vessels throughout the body. To understand the mechanism of the effects of Iranian Echis carinatus venom, the effects of E. carinatus on human and Wistar rat plasma, plasma proteins (prothrombin and fi brinogen) and blood coagulation were studied. Proteolytic activity of the crude venom on blood coagulation factors such as prothrombin, partial thromboplastin and fi brinogen times were studied. In the present study the PT test for human plasma was reduced from 13.4 s (± 0.59) to 8.6 s (± 0.64) when human plasma was treated with crude venom (concentration of venom was 1 mg/ml) and for rat plasma PT was reduced from 14.5 s (± 0.47) to 8 s (± 0.49). Some possible biological and biochemical effects of IEc crude venom were investigated. The blood coagulation in human and in rat were investigated in vivo and in-vitro. In this paper, we show that the procoagulant action of Echis carinatus venom is due in part to a protein component that activates prothrombin and the procoagulant activity on human and rat plasma was evaluated (Tab. 2, Fig. 2, Ref. 31). Text in PDF www.elis.sk.

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Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity

Cited by 56 publications

References 40 publications

Moojenactivase, a novel pro-coagulant PIIId metalloprotease isolated from Bothrops moojeni snake venom, activates coagulation factors II and X and induces tissue factor up-regulation in leukocytes

Moojenactivase, a novel pro-coagulant PIIId metalloprotease isolated from Bothrops moojeni snake venom, activates coagulation factors II and X and induces tissue factor up-regulation in leukocytes

Snake Venom Activators of Factor X: An Overview

Properties of biological and biochemical effects of the Iranian saw-scaled viper (Echis carinatus) venom

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