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Review Article

Differential action of Indian BIG FOUR snake venom toxins on blood coagulation

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Pages 23-32 | Received 02 Aug 2013, Accepted 15 Oct 2013, Published online: 21 Nov 2013

References

  • Ahmed NK, Tennant KD, Markland FS, Lacz JP. (1990). Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom. Haemostasis 20:147–54
  • Alexander G, Grothusen J, Zepeda H, Schwartzman RJ. (1988). Gyroxin, a toxin from the venom of Crotalus durissus terrificus, is a thrombin-like enzyme. Toxicon 26:953–60
  • Amiconi G, Amoresano A, Boumis G, et al. (2000). A novel venombin B from Agkistrodon contortrix contortrix: evidence for recognition properties in the surface around the primary specificity pocket different from thrombin. Biochemistry 39:10294–308
  • Andrião-Escarso SH, Soares AM, Fontes MR, et al. (2002). Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom. Biochem Pharmacol 64:723–32
  • Ariaratnam CA, Sheriff MH, Arambepola C, et al. (2009). Syndromic approach to treatment of snakebite in Sri Lanka based on results of prospective national based survey of patients envenomed by identified snakes. Am J Trop Med Hyg 81:725–31
  • Baker BJ, Tu AT. (1996). Atroxase – a fibrinolytic enzyme isolated from the venom of western diamondback rattlesnake. Isolation, characterization and cloning. Adv Exp Med Biol 391:203–11
  • Barrett AJ, Rawlings ND, Woessner JF. (2004). Handbook of proteolytic enzymes, 2nd edn. London: Academic Press
  • Barbouche R, Marrakchi N, Mabrouk K, et al. (1998). Anti-platelet activity of the peptides composing the lebetin 1 family, a new class of inhibitors of platelet aggregation. Toxicon 36:1939–47
  • Bawaskar HS, Bawaskar PH. (2002). Profile of snakebite envenoming in Western Maharashtra, India. Trans R Soc Trop Med Hyg 96:79–84
  • Bawaskar HS, Bawaskar PH. (2004). Envenoming by the common Krait (Bungarus caeruleus) and asian Cobra (Naja naja): clinical manifestations and their management in a rural setting. Wilderness Environ Med 15:257–66
  • Braud S, Bon C, Wisner A. (2000). Snake venom proteins acting on hemostasis. Biochimie 82:851–9
  • Chakrabarty D, Datta K, Gomes A, Bhattacharyya D. (2000). Haemorrhagic protein of Russell's viper venom with fibrinolytic and esterolytic activities. Toxicon 38:1475–90
  • Chang MC, Huang TF. (1995). The antiplatelet activity of ancrod on administration to rabbits. J Lab Clin Med 125:508–16
  • Chen HS, Tsai HY, Wang YM, Tsai IH. (2008). P-III hemorrhagic metalloproteinases from Russell's viper venom: cloning, characterization, phylogenetic and functional site analyses. Biochimie 90:1486–98
  • Cho SY, Hahn BS, Yang KY, Kim YS. (2001). Purification and characterization of calobin II, a second type of thrombin-like enzyme from Agkistrodon caliginosus (Korean viper). Toxicon 39:499–506
  • Costa FL, Rodrigues RS, Izidoro LF, et al. (2009). Biochemical and functional properties of a thrombin-like enzyme isolated from Bothrops pauloensis snake venom. Toxicon 54:725–35
  • Da Silva M, Lucena S, Aguilar I, et al. (2009). Anti-platelet effect of cumanastatin 1, a disintegrin isolated from venom of South American Crotalus rattlesnake. Thromb Res 123:731–9
  • de Groot PG, Urbanus RT, Roest M. (2012). Platelet interaction with the vessel wall. Handb Exp Pharmacol 210:87–110
  • Dhananjaya BL, Nataraju A, Rajesh R, et al. (2006). Anticoagulant effect of Naja naja venom 5'nucleotidase: demonstration through the use of novel specific inhibitor, vanillic acid. Toxicon 48:411–21
  • Doley R, Mukherjee AK. (2003). Purification and characterization of an anticoagulant phospholipase A(2) from Indian monocled cobra (Naja kaouthia) venom. Toxicon 41:81–91
  • Estêvão-Costa MI, Diniz CR, Magalhães A, et al. (2000). Action of metalloproteinases mutalysin I and II on several components of the hemostatic and fibrinolytic systems. Thromb Res 99:363–76
  • Evans HJ. (1984). Purification and properties of a fibrinogenase from the venom of Naja nigricollis. Biochim Biophys Acta 802:49–54
  • Farid TM, Tu AT, el-Asmar MF. (1989). Characterization of cerastobin, a thrombin-like enzyme from the venom of Cerastes vipera (Sahara sand viper). Biochemistry 28:371–7
  • Francischetti IM, Saliou B, Leduc M, et al. (1997). Convulxin, a potent platelet-aggregating protein from Crotalus durissus terrificus venom, specifically binds to platelets. Toxicon 35:1217–28
  • Gan ZR, Gould RJ, Jacobs JW, et al. (1988). A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus. J Biol Chem 263:19827–32
  • Gerads I, Tans G, Yukelson LYa, et al. (1992). Activation of bovine factor V by an activator purified from the venom of Naja naja oxiana. Toxicon 30:1065–79
  • Gomes A, De P. (1999). Hannahpep: a novel fibrinolytic peptide from the Indian King Cobra (Ophiophagus hannah) venom. Biochem Biophys Res Commun 266:488–91
  • Guo YW, Chang TY, Lin KT, et al. (2001). Cloning and functional expression of the mucrosobin protein, a beta-fibrinogenase of Trimeresurus mucrosquamatus (Taiwan Habu). Protein Expr Purif 23:483–90
  • Gutierrez JM, Rucavado A. (2000). Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 82:841–50
  • Hamako J, Matsui T, Nishida S, et al. (1998). Purification and characterization of kaouthiagin, a von Willebrand factor-binding and -cleaving metalloproteinase from Naja kaouthia cobra venom. Thromb Haemost 80:499–505
  • Hamako J, Matsui T, Suzuki M, et al. (1996). Purification and characterization of bitiscetin, a novel von Willebrand factor modulator protein from Bitis arietans snake venom. Biochem Biophys Res Commun 226:273–9
  • Hofmann H, Bon C. (1987). Blood coagulation induced by the venom of Bothrops atrox. 2. Identification, purification, and properties of two factor X activators. Biochemistry 26:780–7
  • Hoffman MM, Monroe DM. (2005). Rethinking the coagulation cascade. Curr Hematol Rep 4:391–6
  • Hsu CC, Wu WB, Huang TF. (2008). A snake venom metalloproteinase, kistomin, cleaves platelet glycoprotein VI and impairs platelet functions. J Thromb Haemost 6:1578–85
  • Huang TF, Wang WJ, Teng CM, Ouyang C. (1991). Mechanism of action of the antiplatelet peptide, arietin, from Bitis arietans venom. Biochim Biophys Acta 1074:144–50
  • Iwasaki A, Shieh TC, Shimohigashi Y, et al. (1990). Purification and characterization of a coagulant enzyme, okinaxobin I, from the venom of Trimeresurus okinavensis (Himehabu snake) which releases fibrinopeptide B. J Biochem 1990:822–8
  • Jayanthi GP, Gowda TV. (1990). Synergistic interaction of a protease and protease inhibitors from Russell's viper (Vipera russelii) venom. Toxicon 28:65–74
  • Jenne CN, Urrutia R, Kubes P. (2013). Platelets: bridging hemostasis, inflammation, and immunity. Int J Lab Hematol 35:254–61
  • Jin Y, Lu QM, Wang WY, Xiong YL. (2002). Actions of two serine proteases from Trimeresurus jerdonii venom on chromogenic substrates and fibrinogen. Comp Biochem Physiol B Biochem Mol Biol 132:529–34
  • Joseph JS, Thirumangalathu S, Tsang F, et al. (2003). Trocarin, a blood coagulation factor Xa homologue from snake venom, causes inflammation and mitogenesis. Toxicon 42:769–76
  • Kamiguti AS, Hay CR, Zuzel M. (1996). Inhibition of collagen-induced platelet aggregation as the result of cleavage of alpha 2 beta 1-integrin by the snake venom metalloproteinase jararhagin. Biochem J 320:635–41
  • Kemparaju K, Krishnakanth TP, Veerabasappa Gowda T. (1999). Purification and characterization of a platelet aggregation inhibitor acidic phospholipase A2 from Indian saw-scaled viper (Echis carinatus) venom. Toxicon 37:1659–71
  • Kikushima E, Nakamura S, Oshima Y, et al. (2008). Hemorrhagic activity of the vascular apoptosis-inducing proteins VAP1 and VAP2 from Crotalus atrox. Toxicon 52:589–93
  • Kini RM, Evans HJ. (1989). Role of cationic residues in cytolytic activity: modification of lysine residues in the cardiotoxin from Naja nigricollis venom and correlation between cytolytic and antiplatelet activity. Biochemistry 28:9209–15
  • Komori Y, Nikai T, Ohara A, et al. (1993). Effect of bilineobin, a thrombin-like proteinase from the venom of common cantil (Agkistrodon bilineatus). Toxicon 31:257–70
  • Kornalik F, Blombäck B. (1975). Prothrombin activation induced by Ecarin – a prothrombin converting enzyme from Echis carinatus venom. Thromb Res 6:57–63
  • Kumar KPG. (2011). Haematotoxic snake envenomation – prothrombin time is better predictor of toxicity. Amrita J Med 7:1–3
  • Kumar MS, Devaraj VR, Vishwanath BS, Kemparaju K. (2010). Anti-coagulant activity of a metalloprotease: further characterization from the Indian cobra (Naja naja) venom. J Thromb Thrombolysis 29:340–8
  • Kumar MS, Girish KS, Vishwanath BS, Kemparaju K. (2011). The metalloprotease, NN-PF3 from Naja naja venom inhibits platelet aggregation primarily by affecting α2β1 integrin. Ann Hematol 90:569–77
  • Laraba-Djebari F, Martin-Eauclaire MF, Mauco G, Marchot P. (1995). Afaâcytin, an alpha beta-fibrinogenase from Cerastes cerastes (horned viper) venom, activates purified factor X and induces serotonin release from human blood platelets. Eur J Biochem 233:756–65
  • Lee JW, Seu JH, Rhee IK, et al. (1999). Purification and characterization of brevinase, a heterogeneous two-chain fibrinolytic enzyme from the venom of Korean snake, Agkistrodon blomhoffii brevicaudus. Biochem Biophys Res Commun 260:665–770
  • Loría GD, Rucavado A, Kamiguti AS, et al. (2003). Characterization of ‘basparin A,' a prothrombin-activating metalloproteinase, from the venom of the snake Bothrops asper that inhibits platelet aggregation and induces defibrination and thrombosis. Arch Biochem Biophys 418:13–24
  • Lu Q, Clemetson JM, Clemetson KJ. (2005). Snake venoms and hemostasis. J Thromb Haemost 3:1791–9
  • Lundblad RL, Bradshaw RA, Gabriel D, et al. (2004). A review of the therapeutic uses of thrombin. Thromb Haemost 91:851–60
  • Markland FS. (1998). Snake venoms and the hemostatic system. Toxicon 36:1749–800
  • Masuda S, Hayashi H, Atoda H, et al. (2001). Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis. Eur J Biochem 268:3339–45
  • Matsui T, Fujimura Y, Titani K. (2000). Snake venom proteases affecting hemostasis and thrombosis. Biochim Biophys Acta 1477:146–56
  • Meier J, Stocker K. (1991). Effects of snake venoms on hemostasis. Crit Rev Toxicol 21:171–82
  • Michiels C. (2003). Endothelial cell functions. J Cell Physiol 196:430–43
  • Mukherjee AK. (2008). Characterization of a novel pro-coagulant metalloprotease (RVBCMP) possessing alpha-fibrinogenase and tissue haemorrhagic activity from venom of Daboia russelii russelii (Russell's viper): evidence of distinct coagulant and haemorrhagic sites in RVBCMP. Toxicon 51:923–33
  • Nahas L, Kamiguti AS, Barros MA. (1979). Thrombin-like and factor X-activator components of Bothrops snake venoms. Thromb Haemost 41:314–28
  • Nakagaki T, Lin P, Kisiel W. (1992). Activation of human factor VII by the prothrombin activator from the venom of Oxyuranus scutellatus (Taipan snake). Thromb Res 65:105–16
  • Naves de Souza DL, Gomes MS, Ferreira FB, et al. (2012). Biochemical and enzymatic characterization of BpMP-I, a fibrinogenolytic metalloproteinase isolated from Bothropoides pauloensis snake venom. Comp Biochem Physiol B Biochem Mol Biol 161:102–9
  • Newell-Caito JL, Laha M, Tharp AC, et al. (2011). Notecarin D binds human factor V and factor Va with high affinity in the absence of membranes. J Biol Chem 286:38286–97
  • Nishida S, Fujimura Y, Miura S, et al. (1994). Purification and characterization of bothrombin, a fibrinogen-clotting serine protease from the venom of Bothrops jararaca. Biochemistry 33:1843–9
  • Ouyang C, Teng CM. (1979). The action mechanism of the purified platelet aggregation principle of Trimeresurus mucrosquamatus venom. Thromb Haemost 41:475–90
  • Pan H, Du X, Yang G, et al. (1999). cDNA cloning and expression of acutin. Biochem Biophys Res Commun 255:412–5
  • Pereira AL, Fritzen M, Faria F, et al. (2006). Releasing or expression modulating mediator involved in hemostasis by Berythractivase and Jararhagin (SVMPs). Toxicon 47:788–96
  • Pirkle H, Theodor I, Miyada D, Simmons G. (1986). Thrombin-like enzyme from the venom of Bitis gabonica. Purification, properties, and coagulant actions. J Biol Chem 261:8830–5
  • Prasad BN, Kemparaju K, Bhatt KG, Gowda TV. (1996). A platelet aggregation inhibitor phospholipase A2 from Russell's viper (Vipera russelii) venom: isolation and characterization. Toxicon 34:1173–85
  • Prasad NB, Uma B, Bhat SKG, Gowda TV. (1999). Comparative characterization of Russell's viper (Daboia/Vipera russelii) venoms from different regions of Indian peninsula. Biochim Biophys Acta 1428:121–36
  • Ramos OH, Selistre-de-Araujo HS. (2006). Snake venom metalloproteases – structure and function of catalytic and disintegrin domains. Comp Biochem Physiol C Toxicol Pharmacol 142:328–46
  • Rao VS, Joseph JS, Kini RM. (2003). Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa. Biochem J 369:635–42
  • Rao VS, Kini RM. (2002). Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor Xa-Va complex. Thromb Haemost 88:611–9
  • Rosing J, Govers-Riemslag JW, Yukelson L, Tans G. (2001). Factor V activation and inactivation by venom proteases. Haemostasis 31:241–6
  • Saidi N, Samel M, Siigur J, Jensen PE. (1999). Lebetase, an alpha(beta)-fibrin(ogen)olytic metalloproteinase of Vipera lebetina snake venom, is inhibited by human alpha-macroglobulins. Biochim Biophys Acta 1434:94–102
  • Saikia D, Thakur R, Mukherjee AK. (2011). An acidic phospholipase A(2) (RVVA-PLA(2)-I) purified from Daboia russelii venom exerts its anticoagulant activity by enzymatic hydrolysis of plasma phospholipids and by non-enzymatic inhibition of factor Xa in a phospholipids/Ca(2+)-independent manner. Toxicon 57:841–50
  • Sajevic T, Leonardi A, Križaj I. (2011). Haemostatically active proteins in snake venoms. Toxicon 57:627–45
  • Sakurai Y, Fujimura Y, Kokubo T, et al. (1998). The cDNA cloning and molecular characterization of a snake venom platelet glycoprotein Ib-binding protein, mamushigin, from Agkistrodon halys blomhoffii venom. Thromb Haemost 79:1199–207
  • Satish S, Tejaswini J, Krishnakantha TP, Gowda TV. (2004). Purification of a class B1 platelet aggregation inhibitor phospholipase A2 from Indian cobra (Naja naja) venom. Biochimie 86:203–10
  • Schattner M, Fritzen M, de Ventura JS, et al. (2005). The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells. Biol Chem 386:369–74
  • Sekhar CC, Chakrabarty D. (2011). Fibrinogenolytic toxin from Indian monocled cobra (Naja kaouthia) venom. J Biosci 36:355–61
  • Shashidharamurthy R, Jagadeesha DK, Girish KS, Kemparaju K. (2002). Variations in biochemical and pharmacological properties of Indian cobra (Naja naja naja) venom due to geographical distribution. Mol Cell Biochem 229:93–101
  • Shebuski RJ, Ramjit DR, Bencen GH, Polokoff MA. (1989). Characterization and platelet inhibitory activity of bitistatin, a potent arginine-glycine-aspartic acid-containing peptide from the venom of the viper Bitis arietans. J Biol Chem 264:21550–6
  • Shieh TC, Tanaka S, Kihara H, et al. (1985). Purification and characterization of a coagulant enzyme from Trimeresurus flavoviridis venom. J Biochem 98:713–21
  • Shimokawa K, Takahashi H. (1997). Capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (kankoku-mamushi): activity resulting from the release of peptides from fibrinogen. Toxicon 35:597–605
  • Siigur E, Aaspõllu A, Siigur J. (2003). Anticoagulant serine fibrinogenases from Vipera lebetina venom: structure-function relationships. Thromb Haemost 89:826–31
  • Siigur E, Samel M, Tõnismägi K, et al. (1998). Isolation, properties and N-terminal amino acid sequence of a factor V activator from Vipera lebetina (Levantine viper) snake venom. Biochim Biophys Acta 1429:239–48
  • Silva MB, Schattner M, Ramos CR, et al. (2003). A prothrombin activator from Bothrops erythromelas (jararaca-da-seca) snake venom: characterization and molecular cloning. Biochem J 369:129–39
  • Stocker K, Fischer H, Meier J. (1982). Thrombin-like snake venom proteinases. Toxicon 20:265–73
  • Stocker K, Fischer H, Meier J, et al. (1987). Characterization of the protein C activator Protac from the venom of the southern copperhead (Agkistrodon contortrix) snake. Toxicon 25:239–52
  • Stocker K, Hauer H, Müller C, Triplett DA. (1994). Isolation and characterization of Textarin, a prothrombin activator from eastern brown snake (Pseudonaja textilis) venom. Toxicon 32:1227–36
  • Sun HH, Chen Q, Lin X, et al. (2007). Purification and partial characterizations of coagulant protein Fla from Daboia russelii siamensis (Myanmar) venom. Acta Pharm Sin 28:1580–4
  • Swenson S, Markland FS Jr. (2005). Snake venom fibrin(ogen)olytic enzymes. Toxicon 45:1021–39
  • Szántó T, Joutsi-Korhonen L, Deckmyn H, Lassila R. (2012). New insights into von Willebrand disease and platelet function. Semin Thromb Hemost 38:55–63
  • Teng CM, Hung ML, Huang TF, Ouyang C. (1989). Triwaglerin: a potent platelet aggregation inducer purified from Trimeresurus wagleri snake venom. Biochim Biophys Acta 992:258–64
  • Tokunaga F, Nagasawa K, Tamura S, et al. (1988). The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences. J Biol Chem 263:17471–81
  • Wu WB, Chang SC, Liau MY, Huang TF. (2001a). Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells. Biochem J 357:719–28
  • Wu WB, Peng HC, Huang TF. (2001b). Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox. Thromb Haemost 86:1501–11
  • Wang WJ. (2007). Purification and functional characterization of AAV1, a novel P-III metalloproteinase, from Formosan Agkistrodon acutus venom. Biochimie 89:105–15
  • Wang WJ, Shih CH, Huang TF. (2005). Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom. Biochimie 87:1065–77
  • Yamada D, Morita T. (1997). Purification and characterization of a Ca2+-dependent prothrombin activator, multactivase, from the venom of Echis multisquamatus. J Biochem 122:991–7
  • Yamada D, Sekiya F, Morita T. (1996). Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism. J Biol Chem 271:5200–7
  • Yamamoto C, Tsuru D, Oda-Ueda N, et al. (2002). Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase. Immunology 107:111–7
  • Yamazaki Y, Morita T. (2007). Snake venom components affecting blood coagulation and the vascular system: structural similarities and marked diversity. Curr Pharm 13:2872–786
  • Zhang Y, Gao R, Lee WH, et al. (1998). Characterization of a fibrinogen-clotting enzyme from Trimeresurus stejnegeri venom, and comparative study with other venom proteases. Toxicon 36:131–42
  • Zhou Q, Smith JB, Grossman MH. (1995). Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen. Biochem J 307:411–7

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