Human coagulation factor Xa prevents oligomerization of anti-coagulant phospholipases A₂

References

• Berg OG, Gelb MH, Tsai MD, Jain MK. (2001). Interfacial enzymology: the secreted phospholipase A2-paradigm. Chem Rev 101:2613–53
   PubMed Web of Science ®Google Scholar
• Boilard E, Bourgoin SG, Bernatchez C, Surette ME. (2003). Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2. Blood 102:2901–9
   PubMed Web of Science ®Google Scholar
• Bon C, Saliou B. (1983). Ceruleotoxin: identification in the venom of Bungarus multicinctus, molecular properties and importance of phospholipase A2 activity for neurotoxicity. Toxicon 21:681–98
   PubMed Web of Science ®Google Scholar
• Dixon M. (1953). The determination of enzyme inhibitor constants. Biochem J 55:170–1
   PubMed Web of Science ®Google Scholar
• Doley R, Kini RM. (2009). Potein complexes in snake venom. Cell Mol Life Sci 66:2851–71
   PubMed Web of Science ®Google Scholar
• Faure G, Bon C. (1988). Crotoxin, a phospholipase A2 neurotoxin from the South American Rattlesnake, Crotalus durissus terrificus: purification of several isoforms and comparison of their molecular structure and of their biological activities. Biochemistry 27:730–8
   PubMed Web of Science ®Google Scholar
• Faure G, Fourier A. (2006). SPR study to characterize the snake venom phospholipases A2 mechanism of action. [Etude du mécanisme d’action des phospholipases A2 de venins de serpents par la résonance plasmonique de surface]. In: Goudey-Perrière F, Benoit E, Goyffon, M, Marchot P, eds. “Toxines and cancer”, SFET collection. Paris, France: Elsevier, 313–18
   Google Scholar
• Faure G, Saul F. (2010). Three-dimensional structures of two neurotoxic phospholipases A2, ammodytoxin and crotoxin, are resolved: impact of structural differences on functional effects. In: Barbier J, Benoit E, Marchot P, et al., eds. Advances and new technologies in Toxinology. E-book RT-18 2010, 105–8. Available at: http://www.sfet.asso.fr
   Google Scholar
• Faure G, Saul F. (2011). Structural and functional characterization of anticoagulant, FXa-binding Viperidae snake venom phospholipase A2. Acta Chim Slov 58:671–77
   PubMedGoogle Scholar
• Faure G, Saul F. (2012). Crystallographic characterization of functional sites of crotoxin and ammodytoxin, potent β-neurotoxin from Viperidae venom. Toxicon 60:531–8
   Google Scholar
• Faure G, Guillaume JL, Camoin L, et al. (1991). Multiplicity of acidic subunit isoforms of crotoxin, the phospholipase A2 neurotoxin from Crotalus durissus terrificus venom: results from postranlational modifications. Biochemistry 30:8074–83
   PubMed Web of Science ®Google Scholar
• Faure G, Gowda VT, Maroun RC. (2007). Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics. BMC Struct Biol 7:82
   Google Scholar
• Faure G, Harvey AL, Thomson E, et al. (1993). Comparison of crotoxin isoforms reveals the stability of the complex plays a major role in its pharmacological action. Eur J Biochem 214:491–6
   Google Scholar
• Faure G, Xu H, Saul F. (2011). Crystal structure of crotoxin reveals key residues involved in stability and toxicity of this potent heterodimeric β-neurotoxin. J Mol Biol 412:176–91
   Google Scholar
• Faure G, Xu H, Saul F. (2010). Anticoagulant phospholipases A2 which bind to the specific soluble receptor coagulation factor Xa. In: Kini RM, Clemetson K, Markland FS, et al. eds. Toxins and hemostasis: from bench to bedside. Springer Science+Business Media B.V., 201–17
   Google Scholar
• Fohlman J, Eaker D, Karlsson E, Thesleff S. (1976). Taipoxin, an extremely potent presynaptic neurotoxin from the venom of Australian snake Taipan (Oxyuranus scutellatus). Isolation, characterization, quarternary structure and pharmacological properties. Eur J Biochem 68:457–69
   PubMedGoogle Scholar
• Gao W, Starkov VG, He Z-X, et al. (2009). Functions, structures and Triton X-100 effect for the catalytic subunits of heterodimeric phospholipases A2 from Vipera nikolskii venom. Toxicon 54:709–16
   Google Scholar
• Georgieva DN, Perbandt M, Rypniewski W, et al. (2004). The X-ray structure of a snake venom Gln48 phospholipase A2 at 1.9 Å resolution reveals anion-binding sites. Biochem Biophys Res Commun 316:33–8
   PubMedGoogle Scholar
• Gubenšek F, Ritonja A, Zupan J, Turk V. (1980). Basic proteins of Vipera ammodytes venom. Studies of structure and function. Period Biol 82:443–7
   Web of Science ®Google Scholar
• Jan V, Maroun RC, Robbe-Vincent A, et al. (2002). Toxicity evolution of Vipera aspis aspis venom: identification and molecular modeling of a novel phospholipase A2 heterodimer neurotoxin. FEBS Lett 527:263–8
   PubMed Web of Science ®Google Scholar
• Kerns RT, Kini RM, Stefansson S, Evans HJ. (1999). Targeting of venom phospholipases: the strongly anticoagulant phospholipase A (2) from Naja nigricollis venom binds to a coagulation factor Xa to inhibit the prothrombinase complex. Arch Biochem Biophys 369:107–13
   PubMed Web of Science ®Google Scholar
• Kini RM. (2005). Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms. Toxicon 45:1147–61
   PubMed Web of Science ®Google Scholar
• Kini RM. (2006). Anticoagulant proteins from snake venoms: structure, function and mechanism. Biochem J 397:377–87
   PubMed Web of Science ®Google Scholar
• Kovačič L, Novinec M, Petan T, et al. (2010). Structural basis of the significant calmodulin-induced increase in the enzymatic activity of secreted phospholipases A2. Prot Eng Design Select 23:479–87
   PubMed Web of Science ®Google Scholar
• Kumar JR, Basavarajappa BS, Arancio O, et al. (2008). Isolation and characterization of “Reprotoxin”, a novel protein complex from Daboia russelii snake venom. Biochimie 90:1545–59
   PubMed Web of Science ®Google Scholar
• Kuruppu S, Reeva S, Banerjee Y, et al. (2005). Isolation and pharmacological characterization of cannitoxin, a presynaptic neurotoxin from the venom of Papuan Taipan (Oxyuranus scutellatus canni). J Pharmacol Exp Ther 3:1196–202
   Google Scholar
• Magro AJ, Murakami MT, Marcussi S, et al. (2004). Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state. Biochem Biophys Res Commun 323:24–31
   Google Scholar
• Marchi-Salvador DP, Correa LC, Magro AJ, et al. (2008). Insights into the role of oligomeric state on the biological activities of crotoxin: crystal structure of a tetrameric phospholipase A2 formed by two isofroms of crotoxin B from Crotalus durissus terrificus venom. Proteins 72:883–91
   Google Scholar
• Mounier CM, Hackeng TM, Schaeffer F, et al. (1998). Inhibition of prothrombinase by human secretory phospholipase A2 involves binding to factor Xa. J Biol Chem 273:23764–72
   Google Scholar
• Mounier CM, Luchetta P, Lecut C, et al. (2000). Basic residues of human group IIA phospholipase A2 are important for binding to factor Xa and prothrombinase inhibition. Comparison with other mammalian secreted phospholipases A2. Eur J Biochem 267:4960–9
   PubMedGoogle Scholar
• Murakami M, Kudo I. (2002). Phospholipase A2. J Biochem 131:285–92
   PubMed Web of Science ®Google Scholar
• Murakami M, Kudo I. (2003). Another way for sPLA2 to meet with cells. Blood 102:2714–15
   Google Scholar
• Plocki S, Aoun D, Azali Ahamada-Himidi A, et al. (2005). Molecular modeling, design, and synthesis of less lipophilic derivatives of 3-(4-tetradecyloxybenzyl)-4H-1,2,4-oxadiazol-5-one (PMS1062) specific for Group II enzyme. Eur J Org Chem 2005(13):2747–57
   Google Scholar
• Prijatelj P, Charnay M, Ivanovski G, et al. (2006). The C-terminal and beta-wing regions of ammodytoxin A, a neurotoxic phospholipase A2 from Vipera ammodytes ammodytes, are critical for binding to factor Xa and for anticoagulant effect. Biochimie 88:69–76
   PubMedGoogle Scholar
• Prijatelj P, Pražnikar Jenko Z, Petan T, et al. (2008). Mapping the structural determinants of presynaptic neurotoxicity of snake venom phospholipases A2. Toxicon 51:1520–9
   Google Scholar
• Pungerčar J, Križaj I. (2007). Understanding the molecular mechanism underlying the presynaptic toxicity of secreted phospholipases A2. Toxicon 50:871–92
   PubMed Web of Science ®Google Scholar
• Radvanyi F, Jordan L, Russo-Marie F, Bon C. (1989). A sensitive and continuous fluorometric assay for phospholipase A2 using pyrene-labeled phospholipids in the presence of serum albumin. Anal Biochem 177:103–9
   PubMedGoogle Scholar
• Salvador GHM, Fernandes CAH, Magro AJ, et al. (2013). Structural and phylogenetic studies with MjTX-I reveal a multi-oligomeric toxin – a novel feature in Lys49-PLA2s protein class. PLoS ONE 8:e60610
   Google Scholar
• Saul F, Prijatelj-Žnidaršič P, Vulliez-le Normand B, et al. (2010). Comparative structural studies of two natural isofoms of ammodytoxin, phospholipases A2 from Vipera ammodytes ammodytes which differ in neurotoxicity and anticoagulant activity. J Struct Biol 169:360–9
   PubMed Web of Science ®Google Scholar
• Singh G, Sarvanan GK, Sharma S, et al. (2005). Crystal structure of carbohydrate induced homodimer of phospholipase A2 from Bungarus caeruleus at 2.1Å resolution. J Struct Biol 149:264–72
   Google Scholar
• Sribar J, Križaj I. (2011). Secreted phospholipases A2 -- not just enzymes. Acta Chim Slov 58:678--88
   Google Scholar
• Yegueswaran S, Hackeng TM, Dawson PE, Griffin JH. (2008). The thrombin-sensitive region of protein S mediates phospholipid-dependent interaction with factor Xa. J Biol Chem 283:33046–52
   Google Scholar