Anticoagulant Activity and Plasma Phosphatidylserine Hydrolysis by Snake Venom Phospholipase A2

Condrea, Eleonora; Yang, Chen-Chung; Rosenberg, Philïp

doi:10.1055/s-0038-1657347

Cited by 55 publications

(25 citation statements)

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“…The coagulant activity was determined by the method described by Condrea et al (1983) where the formation of visible clot was taken as an end point. The clot formation was initiated by adding 30 μl of 0.25 MCaCl 2 to the mouse plasma.…”

Section: Plasma Clotting Activitymentioning

confidence: 99%

Proteins derived from latex of C. procera maintain coagulation homeostasis in septic mice and exhibit thrombin- and plasmin-like activities

Ramos

Viana

Silva

et al. 2012

Naunyn-Schmiedeberg's Arch Pharmacol

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The proteins derived from the latex (LP) of Calotropis procera are well known for their anti-inflammatory property. In view of their protective effect reported in the sepsis model, they were evaluated for their efficacy in maintaining coagulation homeostasis in sepsis. Intraperitoneal injection of LP markedly reduced the procoagulation and thrombocytopenia observed in mice infected with Salmonella; while in normal mice, LP produced a procoagulant effect. In order to understand its mechanism of action, the LP was subjected to ion-exchange chromatography, and the three subfractions (LPPI, LPPII, and LPPIII) thus obtained were tested for their proteolytic effect and thrombin- and plasmin-like activities in vitro. Of the three subfractions tested, LPPII and LPPIII exhibited proteolytic effect on azocasein and exhibited procoagulant effect on human plasma in a concentration-dependent manner. Like trypsin and plasmin, these subfractions produced both fibrinogenolytic and fibrinolytic effects that were mediated through the hydrolysis of the Aα, Bβ, and γ chains of fibrinogen and α-polymer and γ-dimer of fibrin clot, respectively. This study shows that the cysteine proteases present in the latex of C. procera exhibit thrombin- and plasmin-like activities and suggests that these proteins have therapeutic potential in various conditions associated with coagulation abnormalities.

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Section: Plasma Clotting Activitymentioning

confidence: 99%

Proteins derived from latex of C. procera maintain coagulation homeostasis in septic mice and exhibit thrombin- and plasmin-like activities

Ramos

Viana

Silva

et al. 2012

Naunyn-Schmiedeberg's Arch Pharmacol

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“…The clotting time was determined according to the method of Condrea et al (1983). Normal human citrated plasma (0.2 mL, n = 5) was incubated with venom (5 µg) and the clotting time was determined.…”

Section: Neutralization Of Indirect Hemolytic Activitymentioning

confidence: 99%

The anti‐snake venom properties of Tamarindus indica (leguminosae) seed extract

Ushanandini¹,

Nagaraju²,

Kumar

et al. 2006

Phytotherapy Research

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In Indian traditional medicine, various plants have been used widely as a remedy for treating snake bites. The aim of this study was to evaluate the effect of Tamarindus indica seed extract on the pharmacological as well as the enzymatic effects induced by V. russelli venom. Tamarind seed extract inhibited the PLA(2), protease, hyaluronidase, l-amino acid oxidase and 5'-nucleotidase enzyme activities of venom in a dose-dependent manner. These are the major hydrolytic enzymes responsible for the early effects of envenomation, such as local tissue damage, inflammation and hypotension. Furthermore, the extract neutralized the degradation of the Bbeta chain of human fibrinogen and indirect hemolysis caused by venom. It was also observed that the extract exerted a moderate effect on the clotting time, prolonging it only to a small extent. Edema, hemorrhage and myotoxic effects including lethality, induced by venom were neutralized significantly when different doses of the extract were preincubated with venom before the assays. On the other hand, animals that received extract 10 min after the injection of venom were protected from venom induced toxicity. Since it inhibits hydrolytic enzymes and pharmacological effects, it may be used as an alternative treatment to serum therapy and, in addition, as a rich source of potential inhibitors of PLA(2), metalloproteinases, serine proteases, hyaluronidases and 5 cent-nucleotidases, the enzymes involved in several physiopathological human and animal diseases.

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“…Recalcification time was determined according to the method of Condrea et al [28]. Nine parts of fresh human blood were mixed with one part of 0.11 M tri-sodium citrate.…”

Section: Coagulant Activitymentioning

confidence: 99%

Exploring a New Serine Protease from Cucumis sativus L

Nafeesa¹,

Shivalingu²,

Vivek³

et al. 2015

Appl Biochem Biotechnol

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Coagulation is an important physiological process in hemostasis which is activated by sequential action of proteases. This study aims to understand the involvement of aqueous fruit extract of Cucumis sativus L. (AqFEC) European burp less variety in blood coagulation cascade. AqFEC hydrolyzed casein in a dose-dependent manner. The presence of protease activity was further confirmed by casein zymography which revealed the possible presence of two high molecular weight protease(s). The proteolytic activity was inhibited only by phenyl methyl sulphonyl fluoride suggesting the presence of serine protease(s). In a dose-dependent manner, AqFEC also hydrolysed Aα and Bβ subunits of fibrinogen, whereas it failed to degrade the γ subunit of fibrinogen even at a concentration as high as 100 μg and incubation time up to 4 h. AqFEC reduced the clotting time of citrated plasma by 87.65%. The protease and fibrinogenolytic activity of AqFEC suggests its possible role in stopping the bleeding and ensuing wound healing process.

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Anticoagulant Activity and Plasma Phosphatidylserine Hydrolysis by Snake Venom Phospholipase A2

Cited by 55 publications

References 0 publications

Proteins derived from latex of C. procera maintain coagulation homeostasis in septic mice and exhibit thrombin- and plasmin-like activities

Proteins derived from latex of C. procera maintain coagulation homeostasis in septic mice and exhibit thrombin- and plasmin-like activities

The anti‐snake venom properties of Tamarindus indica (leguminosae) seed extract

Exploring a New Serine Protease from Cucumis sativus L

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