Fibrin(ogen)olytic enzymes in scorpion (Tityus discrepans) venom

Brazón, Josmary; Guerrero, Belsy; D’Suze, Gina; Sevcik, Carlos; Arocha-Piñango, Carmen Luisa

doi:10.1016/j.cbpb.2013.11.007

Cited by 27 publications

(10 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Several fibrin(ogen)olytic enzymes were partially purified from T. discrepans venom by different types of liquid chromatography [11]. Two fractions had fibrinolytic, fibrinogenolytic (Aα-chains degradation) and tissue plasminogen activator (t-PA)-like activities; one was only fibrinogenolytic (fast degradation of fibrinogen Aα-chains and slower degradation of Bβ-chains).…”

Section: Introductionmentioning

confidence: 99%

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Tran

Hoang

Nguyen

et al. 2017

Toxins

View full text Add to dashboard Cite

Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagulant activity. Determination of their structure has shown that one of them is adenosine, and two others are dipeptides LeuTrp and IleTrp. The anticoagulant properties of adenosine, an inhibitor of platelet aggregation, are well known, but its presence in scorpion venom is shown for the first time. The dipeptides did not influence the coagulation time in standard plasma coagulation tests. However, similarly to adenosine, both peptides strongly prolonged the bleeding time from mouse tail and in vitro clot formation in whole blood. The dipeptides inhibited the secondary phase in platelet aggregation induced by ADP, and IleTrp decreased an initial rate of platelet aggregation induced by collagen. This suggests that their anticoagulant effects may be realized through the deterioration of platelet function. The ability of short peptides from venom to slow down blood coagulation and their presence in scorpion venom are established for the first time. Further studies are needed to elucidate the precise molecular mechanism of dipeptide anticoagulant activity.

show abstract

Section: Introductionmentioning

confidence: 99%

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Tran

Hoang

Nguyen

et al. 2017

Toxins

View full text Add to dashboard Cite

show abstract

“…Fibrin(ogen)olytic enzymes have been categorized into two classes, serine proteases and metalloproteases (28) both of which were previously identified in H. lepturus venom gland (18,24,29). Similar enzymes with fibrin(ogen)olytic and plasminogen activator-like potential were also purified from the venom of Tityus discrepans (28) and Androctonus crassicauda (30).…”

Section: Discussionmentioning

confidence: 99%

The Effect of Various Fractions of Hemiscorpius lepturus Scorpion (Scorpionida: Hemiscorpiidae) Venom on Hemostatic System in Peripheral Blood of Rats in Comparison to Whole Venom

Khataminia

Jalali

et al. 2020

Jundishapur J Health Sci

View full text Add to dashboard Cite

Background: Hemiscorpius lepturus is the most critical scorpion in Khuzestan, Iran, responsible for the majority of deaths caused by scorpion stings. Objectives: This prospective randomized experimental study was performed from June to August 2019 to investigate the effects of various venom fractions on the hemostatic system. Methods: Lyophilized venom of H. lepturus was separated into six fractions by Sephadex G-50 gel chromatography. A total of 96 Albino male rats were treated in eight equal groups; Control: 0.5 ml normal saline (IP); Whole venom group: H. lepturus Lyophilized venom, one mg/kg, IP; F1-F6 groups: Isolated venom fraction 1-6, 0.12 mg/kg, 0.43 mg/kg, 0.08 mg/kg, 0.18 mg/kg, 0.06 mg/kg and 0.13 mg/kg, IP, respectively. Blood sampling was performed at 1, 3, and 24 hours after injection. Results: Plasma fibrinogen was significantly elevated in the whole venom group, while it was significantly decreased in F3, F5, and F6 groups compared to the control group. Prothrombin time (PT) and activated partial thromboplastin time (APTT) assessment revealed that there was a significant prolongation of both tests in whole venom and fraction 5 and 6 receiving groups while fraction 2 only caused a significant PT extension, compared to the control group. Conversely, fraction 3 and 4 resulted in PT and APTT in comparison to the control group. The concentration of FDP and D-dimer was significantly increased in whole venom and F2 group compared to the control group at all sampling times. Conclusions: It seems that H. lepturus venom has both procoagulant and anticoagulant properties which are distinct characteristics of it. Further purification and sequencing of the amino acids in the fraction of peptides can lead to a more precise identification of the mechanisms of venom-induced coagulopathies.

show abstract

“…Como es conocido, el fibrinógeno es una proteína plasmática formada por 6 cadenas polipeptídicas (2Aα, 2Bβ y 2γ), que participa en la etapa final de la coagulación sanguínea y que muchas veces es el blanco de acción de ciertas enzimas proteolíticas. Nuestros resultados mostraron que el veneno de P. papillosa hidrolizó completamente las cadenas Aα y Bβ del fibrinógeno, pero no la cadena γ. Las proteasas con acción sobre fibrinógeno también denominadas fibrinogenasas o enzimas fibrinogenolíticas, han sido reportadas ampliamente en venenos de serpientes y de escorpiones (Swenson & Markland 2005, Brazón et al 2014, pero no en anémonas de mar, por lo que este hallazgo constituye el primer reporte de ese tipo. La actividad proteolítica que tienen algunos venenos sobre el fibrinógeno, se ha asociado a la capacidad anticoagulante que tiene ese veneno (Brazón et al 2014).…”

Section: Discussionunclassified

“…Nuestros resultados mostraron que el veneno de P. papillosa hidrolizó completamente las cadenas Aα y Bβ del fibrinógeno, pero no la cadena γ. Las proteasas con acción sobre fibrinógeno también denominadas fibrinogenasas o enzimas fibrinogenolíticas, han sido reportadas ampliamente en venenos de serpientes y de escorpiones (Swenson & Markland 2005, Brazón et al 2014, pero no en anémonas de mar, por lo que este hallazgo constituye el primer reporte de ese tipo. La actividad proteolítica que tienen algunos venenos sobre el fibrinógeno, se ha asociado a la capacidad anticoagulante que tiene ese veneno (Brazón et al 2014). Por otro lado en este estudio también se ha demostrado que el EDTA, un quelante de iones metálicos divalentes como Ca ++ y Mg ++ , inhibe completamente la actividad fibrinogenolítica del veneno de P. papillosa, lo que indicaría que este tipo de enzima es una metaloproteasa.…”

Section: Discussionunclassified

Estudio bioquímico del veneno de la anémona de mar Phymactis papillosa (Actiniidae)

Cuya¹,

Escobar²

2017

Rev peru biol

View full text Add to dashboard Cite

En este trabajo se ha estudiado bioquímicamente el veneno de Phymactis papillosa, colectadas en la bahía de Ancón. El veneno fue obtenido mediante shock hipotónico y luego se liofilizó. El análisis electroforético del veneno soluble mostró la presencia de 5 bandas proteicas con pesos moleculares entre 5 y 25.1 kDa.El veneno soluble fue fraccionado por cromatografía de filtración en una columna de Sephadex G-50, obteniéndose cuatro picos de proteína (I, II, III y IV). Tanto en el veneno soluble como en las fracciones colectadas se midió actividad de proteasa, fosfolipasa, hialuronidasa, fosfatasa ácida y fosfatasa alcalina; así como, actividad hemolítica y neurotóxica. Se encontró actividad proteolítica sobre caseína, en el veneno soluble y en los picos I y III. No se detectó actividad de fosfolipasa, hialuronidasa, fosfatasa ácida y fosfatasa alcalina. La actividad hemolítica, ensayada sobre eritrocitos humanos, se encontró en el veneno soluble y en el pico II. Finalmente, tanto el veneno soluble como el pico III mostraron ser neurotóxicos al ser inyectados en ratones albinos vía intraperitoneal. Se concluye que el veneno soluble de P. papillosa tiene actividad proteolítica, hemolítica y neurotóxica.

show abstract

Fibrin(ogen)olytic enzymes in scorpion (Tityus discrepans) venom

Cited by 27 publications

References 47 publications

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

The Effect of Various Fractions of Hemiscorpius lepturus Scorpion (Scorpionida: Hemiscorpiidae) Venom on Hemostatic System in Peripheral Blood of Rats in Comparison to Whole Venom

Estudio bioquímico del veneno de la anémona de mar Phymactis papillosa (Actiniidae)

Contact Info

Product

Resources

About