Snake venom fibrin(ogen)olytic enzymes

Swenson, Stephen D.; Markland, Francis S.

doi:10.1016/j.toxicon.2005.02.027

Cited by 245 publications

(159 citation statements)

References 93 publications

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“…Preferences in the digestion of fibrinogen chains of AMP48; Codiase and StSBTc-3 make a difference between these plant proteases and proteases with fibrinogenolytic activity from other sources. a-fibrinogenase from different sources including snake venom [32], Lampetra japonica [33], Codium species [34,35], Paecilomyces tenuipes [36], and Perenniporia fraxinea [37] preferentially hydrolyze a-subunit. However, the g-chain does not appear to be a second specific target.…”

Section: Demonstrate Thatmentioning

confidence: 99%

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

et al. 2016

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a b s t r a c tPlant serine proteases have been widely used in food science and technology as well as in medicine. In this sense, several plant serine proteases have been proposed as potential anti-coagulants and antiplatelet agents. Previously, we have reported the purification and identification of a plant serine protease from Solanum tuberosum leaves. This potato enzyme, named as StSBTc-3, has a molecular weight of 72 kDa and it was characterized as a subtilisin like protease. In this work we determine and characterize the biochemical and medicinal properties of StSBTc-3. Results obtained show that, like the reported to other plant serine proteases, StSBTc-3 is able to degrade all chains of human fibrinogen and to produces fibrin clot lysis in a dose dependent manner. The enzyme efficiently hydrolyzes b subunit followed by partially hydrolyzed a and g subunits of human fibrinogen. Assays performed to determine StSBTc-3 substrate specificity using oxidized insulin b-chain as substrate, show seven cleavage sites: Asn3-Gln4; Cys7-Gly8; Glu13-Ala14; Leu15-Tyr16; Tyr16-Leu17; Arg22-Gly23 and Phe25-Tyr26, all of them were previously reported for other serine proteases with fibrinogenolytic activity. The maximum StSBTc-3 fibrinogenolytic activity was determined at pH 8.0 and at 37 C. Additionally, we demonstrate that StSBTc-3 is able to inhibit platelet aggregation and is unable to exert cytotoxic activity on human erythrocytes in vitro at all concentrations assayed. These results suggest that StSBTc-3 could be evaluated as a new agent to be used in the treatment of thromboembolic disorders such as strokes, pulmonary embolism and deep vein thrombosis.

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Section: Demonstrate Thatmentioning

confidence: 99%

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

et al. 2016

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“…A large number of fibrinogenolytic enzymes that induce alterations in the blood coagulation cascade have been isolated from the venoms of Viperidae snake species and characterized (Markland, 1998;Swenson Markland, 2005). These metalloproteinases that are not inhibited by human serum proteinase inhibitors cleave preferentially the Aα-or Bβ-chain of fibrinogen (Swenson Markland, 2005).…”

mentioning

confidence: 99%

“…These metalloproteinases that are not inhibited by human serum proteinase inhibitors cleave preferentially the Aα-or Bβ-chain of fibrinogen (Swenson Markland, 2005).…”

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confidence: 99%

Electrophoretic Characterization of Venom Proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)

Arıkan

Keskin²,

Çiçek³

2017

bah

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In this study, with the aim of evaluating coagulant activities in the venom of Mo ntivipera xanthina, we analyzed venom proteins, digestion patterns of fibrinogen chains incubated with venom, and the effects of protease inhibitors on M. xanthina venom proteases. Venom samples were obtained from four adult specimens collected in Gümüldür (Izmir, Turkey). SDS-PAGE analysis showed the presence of 17 protein bands or band groups in the molecular mass range of 20 to 200 kDa. The specific digestion patterns of fibrinogen chains revealed that M. xanthina venom possesses fibrinogenolytic enzymes, which could be involved in coagulation processes during envenomation. Fibrinogenolytic activity affected the Aα-chain and showed a time-dependent effect on Bβ-chains, which suggests the presence of both metalloproteinases and serine proteases in M. xanthina venom. After observing the fibrinogenolytic activity of M. xanthina venom, further research should focus on the isolation, identification, and characterization of individual venom components in order to provide insight into their function and biological roles.

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“…Contrary to this, in a review, Jalali et al claimed that following the injection of Hemiscorpius lepturus scorpion venom in rats, PT and PTT were within the normal limits and no significant difference was found regarding coagulation parameters between the control group and the group receiving poison (15). Swenson and Markland claimed that Tityus discrepans scorpion venom is active in fibrinogenolysis, which can destroy fibrinogen and affect the coagulation system (16). The results of this study showed no significant difference between PTT factor and fibrinogen levels of treatment groups (2, 3 and 4) and control group.…”

Section: Discussionmentioning

confidence: 46%

Effects of Different Time Protocols Treatment on Coagulation Parameters of Sheep Injected With Hemiscorpius lepturus Venom

Koupaei

Mashhadi

Rasooli

et al. 2016

Jundishapur J Nat Pharm Prod

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Background: Hemiscorpius lepturus is one of the most dangerous scorpion species, endemic in Khuzestan province. Its venom has hemolytic activity and can lead to hemoglobinuria and death. Objectives: The aim of this study was to determine the effects of three different time treatment protocols on changes of coagulation parameters in sheep received Hemiscorpius lepturus venom. Materials and Methods: Sixteen healthy male lambs were divided randomly into four groups. Hemiscorpius lepturus venom (0.01 mg/kg of body weight) injected subcutaneously. Blood samples were taken at 30 minutes before and 1, 6, 12, 24, 48, 96 and 168 hours after injection. The sheep of group 1 were treated only by injection of Hemiscorpius lepturus venom. In groups 2, 3 and 4 (Experimental groups), treatment of animals began at 1, 24 and 48 hours respectively after the venom injection. In addition to intravenous injection of 5 mL antivenom, supportive therapy was performed as well. Prothrombin time (PT), activated partial thromboplastin time (APTT) and fibrinogen were measured by commercial kit and platelet (PLT) count was performed by hematology analyzer. All results were statistically analyzed using two way repeated measures analysis of variance. Results: In the studied groups, the effect of time on PT and platelets counts was significant (P < 0.05); however, it did not have a significant effect on the amounts of PTT and fibrinogen. No significant statistic difference was found regarding four factors measured between different treatment groups. Interaction of time and treatment groups had significant effect only on the platelet counts (P < 0.05). Conclusions: Hemiscorpius lepturus venom in sheep can cause severe changes in some of the coagulation factors. This should be considered as part of the pathogenesis of scorpion sting and seriously in the treatment protocol of scorpion sting victims.

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Snake venom fibrin(ogen)olytic enzymes

Cited by 245 publications

References 93 publications

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

Electrophoretic Characterization of Venom Proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)

Effects of Different Time Protocols Treatment on Coagulation Parameters of Sheep Injected With Hemiscorpius lepturus Venom

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