Natural Product Sciences

  • 제26권4호
  • /
  • Pages.259-267
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  • 2020
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  • 1226-3907(pISSN)
  • /
  • 2288-9027(eISSN)
한국생약학회 (The Korean Society of Pharmacognosy)
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DOI QR코드

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Snake Venom Phospholipase A2 and its Natural Inhibitors

  • Singh, Pushpendra (ICAR- National Institute of High Security Animal Diseases Bhopal) ;
  • Yasir, Mohammad (Department of Nephrology, All India Institute of Medical Science Bhopal) ;
  • Khare, Ruchi (Department of Biological Science & Engineering, Maulana Azad National Institute of Technology) ;
  • Tripathi, Manish Kumar (Department of Biological Science & Engineering, Maulana Azad National Institute of Technology) ;
  • Shrivastava, Rahul (Department of Biological Science & Engineering, Maulana Azad National Institute of Technology)
  • 투고 : 2020.09.20
  • 심사 : 2020.11.27
  • 발행 : 2020.12.31
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초록

Snakebite is a severe medical, economic, and social problem across the world, mostly in the tropical and subtropical area. These regions of the globe have typical of the world's venomous snakes present where access to prompt treatment is limited or not available. Snake venom is a complex mixture of toxin proteins like neurotoxin and cardiotoxin, and other enzymes like phospholipase A2 (PLA2), haemorrhaging, transaminase, hyaluronidase, phosphodiesterase, acetylcholinesterase, cytolytic and necrotic toxins. Snake venom shows a wide range of biological effects like anticoagulation or platelet aggregation, hemolysis, hypotension and edema. Phospholipase A2 is the principal constituent of snake venom; it catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid, which is the precursor of eicosanoids including prostaglandins and leukotrienes. The information regarding the structure and function of the phospholipase A2 enzyme may help in treating the snakebite victims. This review article constitutes a brief description of the structure, types, mechanism occurrence, and tests of phospholipase A2 and role of components of medicinal plants used to inhibit phospholipase A2.

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