Some pharmacological studies on the effects of Cerastes vipera (Sahara sand viper) snake venom

Alzahaby, M; Rowan, Edward G.; Young, Louise; Al-Zahaby, A.S.; Abu-Sinna, G.; Harvey, Alan L.

doi:10.1016/0041-0101(95)00073-u

Cited by 7 publications

(5 citation statements)

References 23 publications

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“…Suramin blocks cell surface binding of various growth factors and increases tissue glycosaminoglycans (12)(13)(14). There are also studies showing that suramin can inhibit the neurotoxic effect of ß-bungarotoxin and partially inhibit some pharmacological effects of Cerastes vipera venom (15,16).…”

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confidence: 99%

Effect of suramin on myotoxicity of some crotalid snake venoms

Arruda

Silva

Moraes

et al. 2002

Braz J Med Biol Res

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We investigated the protective effect of suramin, an enzyme inhibitor and an uncoupler of G protein from receptors, on the myotoxic activity in mice of different crotalid snake venoms (A.c. laticinctus, C.v. viridis, C.d. terrificus, B. jararacussu, B. moojeni, B. alternatus, B. jararaca, L. muta). Myotoxicity was evaluated in vivo by injecting im the venoms (0.5 or 1.0 mg/kg) dissolved in physiological saline solution (0.1 ml) and measuring plasma creatine kinase (CK) activity. Two experimental approaches were used in mice (N = 5 for each group). In protocol A, 1 mg of each venom was incubated with 1.0 mg suramin (15 min, 37ºC, in vitro), and then injected im into the mice at a dose of 1.0 mg/kg (in vivo). In protocol B, venoms, 1.0 mg/kg, were injected im 15 min prior to suramin (1.0 mg/kg, iv). Before and 2 h after the im injection blood was collected by orbital puncture. Plasma was separated and stored at 4ºC for determination of CK activity using a diagnostic kit from Sigma. Preincubation of some venoms (C.v. viridis, A.c. laticinctus, C.d. terrificus and B. jararacussu) with suramin reduced (37-76%) the increase in plasma CK, except for B. alternatus, B. jararaca or L. muta venoms. Injection of suramin after the venom partially protected (34-51%) against the myotoxicity of B. jararacussu, A.c. laticinctus and C.d. terrificus venom, and did not protect against C.v. viridis, L. muta, B. moojeni, B. alternatus or B. jararaca venoms. These results show that suramin has an antimyotoxic effect against some, but not all the North and South American crotalid snake venoms studied here.

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confidence: 99%

Effect of suramin on myotoxicity of some crotalid snake venoms

Arruda

Silva

Moraes

et al. 2002

Braz J Med Biol Res

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“…The toxicities cause substantial physiopathological changes in liver, skin and heart. Phospholipases A2 (PLA2) from Cerastes cerastes for example, has been associated with some toxicities including neurotoxicity, lung toxicity, nephrotoxicity, hepatotoxicity and cardio toxicity [4][5][6]. The lethal cause of snake venom mainly results from its active ingredients such as PLA2.…”

Section: Introductionmentioning

confidence: 99%

“…The lethal cause of snake venom mainly results from its active ingredients such as PLA2. Phospholipid hydrolysis by PLA2 releases arachidonic acid whose metabolism results in the formation of potentially toxic reactive oxygen species (ROS) and lipid peroxides [6,7]. The increase in the activity of liver enzymes indicating injures of the heart, liver and other organs could be accredited to the synergistic action of the venom components [3,6].…”

Section: Introductionmentioning

confidence: 99%

Olea Europaea Leaves Delay the Onset of Toxicity of Cerastes Cerastes Venom in Albino Mice

2019

JPR

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To investigate the anti-Cerastes cerastes venom effect of aqueous olive leaf extract. The mitigation in the mean survival time of the male Albino Swiss mice were used to deduce the antivenom property of the aqueous olive leaf extract after challenging with LD99 of snake venom. The aqueous extract of olive leaf significantly increases mean survival time and the protection fold, but could not protect mice from death when used alone. The higher dose, i.e., 33 g/kg was better than that of the lower dose of 15 g/kg. The anti-snake venom was found to be more effective than the aqueous olive leaf extract.

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“…The toxicities cause substantial physiopathological changes in the liver, skin and heart. Phospholipases A2 (PLA2) from Cerastes cerastes for example, has been associated with numerous toxicities including neurotoxicity, nephrotoxicity, lung toxicity, hepatotoxicity, and cardiotoxicity [3][4][5]. The lethal effect of snake venom mainly results from its active ingredients such as phospholipase A2 (PLA2).…”

Section: Introductionmentioning

confidence: 99%

“…The lethal effect of snake venom mainly results from its active ingredients such as phospholipase A2 (PLA2). Phospholipid hydrolysis by PLA2 releases arachidonic acid whose metabolism results in the formation of potentially toxic Reactive Oxygen Species (ROS) and lipid peroxides [5,6]. The increase in the activity of liver enzymes indicating the damage of heart, liver and other organs could be attributed to the synergistic action of the venom components [2,5].…”

Section: Introductionmentioning

confidence: 99%

Differentiation between Snake and Bee Venom using Fluorescence Spectroscopy and Computational Approach

Hashkel

Sadawe

Mohamed

et al. 2018

COJRR

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Phospholipase A2 (PLA2) represents a major venom component of snakes and bees and exhibits a broad range of biological effects including myotoxicity, neurotoxicity, hemolysis, cardiotoxicity, anticoagulant and antiplatelet activities. Melittin, is the main component and the major pain producing substance of honeybee venom. The aim of the present study was to differentiate between snake and bee venoms using Aqueous Olive Leaf Extract (AOLE) employing fluorescence techniques. Tryptophan, which is contained in both snake and bee venoms is fluorescent at UV wavelength and hence widely used as a tool to monitor conformational changes in proteins and to draw inferences regarding local structure and dynamics. Fluorescence spectroscopy and molecular modeling have been used to analyze enzyme activity in the absence and presence of AOLE and to verify potential binding of AOLE components to the enzyme. Changes in the fluorescence intensities with blue and red shifts were obtained with bee and snake venoms, respectively. Binding of AOLE constituents near the active site of the enzyme could be evidenced and possible modes of interaction are discussed. The fluorescence method used was rapid and sensitive and was able to differentiate between snake and bee venoms utilizing AOLE.

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Some pharmacological studies on the effects of Cerastes vipera (Sahara sand viper) snake venom

Cited by 7 publications

References 23 publications

Effect of suramin on myotoxicity of some crotalid snake venoms

Effect of suramin on myotoxicity of some crotalid snake venoms

Olea Europaea Leaves Delay the Onset of Toxicity of Cerastes Cerastes Venom in Albino Mice

Differentiation between Snake and Bee Venom using Fluorescence Spectroscopy and Computational Approach

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