Abstract

We investigated the balance of free radicals in different tissues (liver, heart, brain and muscle) of rats in course of in vivo and in vitro processing by Macrovipera lebetina obtusa (MLO) and Montivipera raddei (MR) snake venoms. Chemiluminescence (ChL) levels were examined in tissue assays after incubation (at 37 &#176C for a period of 10 min) with venom for in vitro experiments and in tissue assays isolated of 10 min after venom injection for in vivo experiments. The TBA-test was also performed to confirm the free radical expression. The activities of antioxidant enzymes (such as superoxide dismutase and glutathione peroxidase) in isolated tissues were detected by spectro-photometry. During the in vitro processing chemiluminescence levels of tissue homogenates significantly decreased, while in course of in vivo intoxication the level of ChL was elevated in brain and liver; lipid peroxidation also increased in brain tissue, but there was no significant balance change in other tissues; the activity of superoxide dismutase mainly correlated with changes of free radical balance during intoxication. On the contrary, the activity of glutathione peroxidase showed the reverse tendencies to change. We suggest that free radicals and their oxidative stresses may play a role in the early stage of intoxication causing the so-named “spreading-effect”, which is very characteristic for the venom of vipers.

Highlights

  • Venoms produced by snakes of the family Viperidae contain proteins that interfere with the coagulation cascade, the normal haemostatic system, and tissue repair [1] [2]

  • Crude Macrovipera lebetina obtusa (MLO) and Montivipera raddei (MR) venoms were collected by milking snakes, vacuum dried at ambient temperature and stored at 4 ̊C until use

  • Our experiments revealed that snake venom intoxication in organism could reduce or enhance reactive oxygen species (ROS) generation in different tissues

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Summary

Introduction

Venoms produced by snakes of the family Viperidae (vipers and pit vipers) contain proteins that interfere with the coagulation cascade, the normal haemostatic system, and tissue repair [1] [2]. Viperidae venoms may contain well over 100 protein components [3] [4]. Snake venoms are medicinally effective at very low doses and their therapeutic properties are achieved by mechanisms which are different from those of known therapies. Obtusa venom is the first discovered α1β1 antagonist [7] It blocks the interaction of the α1β1 integrin with collagens IV and I in vitro with IC50s of 2 nM and 0.5 nM, respectively, and angiogenesis in vivo, and may represent a lead molecule for the development of novel anti-angiogenic therapeutic strategies to treat aggressive cancers [8]. Studies on the underlying mechanisms of membrane/peptide binding are of considerable theoretical interest in the field of molecular evolution, in the development of new research tools and drugs of potential clinical use, and for antivenom production strategies

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