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Anticoagulant and Membrane Damaging Properties of Snake Venom Phospholipase A2 Enzymes

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Snake Venoms

Part of the book series: Toxinology ((TOXI))

Abstract

Snake venom is a complex mixture of pharmacologically active proteins and polypeptides in addition to containing some minor nonprotein components. Snake venom plays an important role in incapacitating and immobilizing, as well as in digesting prey after being swallowed. Phospholipase A2 (PLA2) is one of the major toxic enzymes present invariably in all snake venoms. Despite their structural similarities, snake venom PLA2 enzymes differ greatly in their pharmacological properties and biological activities. Venom PLA2s most likely prolong the blood coagulation through hydrolysis of and/or binding to procoagulant phospholipids essential for clotting process. In addition to enzymatic mechanism of anticoagulant effect, anticoagulant PLA2 enzymes strongly extend blood coagulation by a mechanism that is independent of phospholipids hydrolysis and is achieved mostly by inhibiting the blood coagulation factor(s). Studies on such anticoagulant PLA2s may contribute to understand different “vulnerable” sites in the coagulation cascade which may further help to design novel strategies to develop anticoagulant therapeutics to treat cardiovascular disorder (CVD).

Further, most of the toxic effects of snake venom PLA2s are exerted by hydrolysis of membrane phospholipids. Different isoforms of venom PLA2 can display dramatically different affinities for bio-membranes, composed of different phospholipids polar head groups and fatty acyl chains, resulting in their differential membrane damaging activity. This differential affinity of PLA2s towards phospholipids of different bio-membranes has been used extensively to explore the physical structure of phospholipids in biological membranes. Study of membrane damaging activities of venom PLA2s will be helpful in exploring different membrane properties. It is exemplary to mention that only a few reports on membrane hydrolyzing property of snake venom PLA2s are available. Therefore, more precise studies are required to understand the complete mechanism(s) of membrane damage and subsequent toxicity of PLA2 enzymes from snake venom.

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Authors and Affiliations

  1. Microbial Biotechnology and Protein Research Laboratory, Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur, Assam, 784028, India

    Debashree Saikia

  2. Department of Molecular Biology and Biotechnology, Research and Development, ONGC-Centre for Petroleum Biotechnology, DBT Nodal Centre for Medical Colleges and Biomedical Research Institutes of North-East India (Unit of Department of Biotechnology, Govt. of India), Tezpur University, Tezpur, Assam, 784028, India

    Ashis K. Mukherjee

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  1. Debashree Saikia
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  2. Ashis K. Mukherjee
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Correspondence to Ashis K. Mukherjee .

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Editors and Affiliations

  1. Biomedical Research Institute National Institute of Advanced Industria, Tsukuba, Ibaraki, Japan

    Hidetoshi Inagaki

  2. University of Hawaii Cancer Center, Honolulu, Hawaii, USA

    Carl-Wilhelm Vogel

  3. Department of Molecular Biology and Biot, Tezpur University, Tezpur, Assam, India

    Ashis K. Mukherjee

  4. Egyptian Society of Natural Toxins and Z, Faculty of Science Suez Canal University, Ismailia, Egypt

    Tarek R. Rahmy

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Saikia, D., Mukherjee, A.K. (2017). Anticoagulant and Membrane Damaging Properties of Snake Venom Phospholipase A2 Enzymes. In: Inagaki, H., Vogel, CW., Mukherjee, A., Rahmy, T. (eds) Snake Venoms. Toxinology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6410-1_18

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