Abstract
Venoms of snakes belonging to families Viperidae (viper) and Crotalidae (pit viper) produce striking local effects, consisting of hemorrhage, necrosis, and edema, and often induce marked alterations of blood coagulation system as well (Iwanaga and Suzuki, 1979). Among these pathological effects, hemorrhage is a most common occurrence in a victim bitten by crotalid and viperid snakes and various components, such as hemorrhagic factors and metalloproteinases, involved in these venoms have been isolated and characterized (Osaka, 1979). The hemorrhagic metalloproteinases cause localized hemorrhage by direct action on the blood vessel wall. Electron microscopic studies indicate that erythrocytes are leaked in a one-by-one fashion through widened inter-endothelial gaps when capillaries are exposed to these hemorrhagic proteins. Hemorrhagic metalloproteinases degrade basement membrane preparation, in addition to the isolated components including type IV collagen, laminin, nidogen, and fibronectin (Baramova et al., 1989). The enzymes may disrupt the pericellular basement membrane through a proteolytic activity and with subsequent damage to the integrity of the vessel wall after which hemorrhage occurs. On the other hand, crotalid and viperid venoms contain an abundance of metalloproteinases which are completely free from hemorrhagic activity (Iwanaga et al., 1976). Some of them have originally been reported as anticoagulant proteases with fibrinogenolytic or fibrinolytic activity (Markland, 1991). Additional group of venom metalloproteinases are procoagulants having very strict substrate specificities. Two well known examples of this type are Russell’s viper venom factor X activator (RVV-X) and Echis carinatus venom prothrombin activator (Morita and Iwanaga, 1981; Furie and Furie, 1976).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adler, M., Lazarus, R. A., Dennis, M. S. and Wagner, G., 1991 Solution structure of kistrin, a potent platelet aggregation inhibitor and GP Ilb–IIIa antagonist, Science 253:445.
Atoda, H., Hyuga, M. and Morita, T., 1991 The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis, J. Biol. Chem. 266:4903.
Au, L.-C., Huang, Y.-B., Huang, T.-F., Teh, G.-W. Liu, H.-H. and Choo, K.-B., 1991 A common precursor of a putative hemorrhagic protein and rhodostomin, a platelet inhibitor of the venom of Calloselasma rhodostoma, Biochem. Biophys. Res. Commun. 181:585.
Baramova, E. N., Shannon, J. D., Bjarnason, J. B. and Fox, J. W., 1989 Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases, Arch. Biophys. Biochem. 275:63.
Blobel, C. P., Wolfsberg, T. G., Turck, C. W., Myles, D. G., Primakoff, P. and White, J. M., 1992 A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion, Nature 356:248.
Bode, W., Gomis-Rutll, F. X., Huber, R., Zwilling, R. and Stocker, W., 1992 Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases, Nature 358:164.
Furie, B. C. and Furie, B., 1976 Coagulant protein of Russell’s viper venom, Methods Enzymol. 45:191.
Gould, R. J., Polokoff, M. A., Friedman, P. A., Huang, T.-F., Holt, J. C., Cook, J. J. and Niewiarowski, S., 1990 Disintegrins: a family of integrin inhibitory proteins from viper venoms, Proc. Soc. Exp. Biol. Med. 195:168.
Hite, L. A., Shannon, J. D., Bjarnason, J. B. and Fox, J. W., 1992 Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox, Biochemistry 31:6203.
Iwanaga, S., Oshima, G., and Suzuki, T., 1976 Proteinases from the venom of Agkistrodon halys blomhoffii, Methods Enzymol. 45:459.
Iwanaga, S. and Suzuki, T., 1979 Enzymes in snake venom, in: Handbook of Experimental Pharmacology Vol. 52, Snake Venoms, Lee, C.-Y., ed, pp. 61–158, Springer Verlag, New York.
Markland, F.S., Jr., 1991 Inventry of, α-and β-fibrinogenases from snake venoms, Thromb. Haemostas. 65:438.
Miyata, T., Takeya, H., Ozeki, Y., Arakawa, M., Tokunaga, F., Iwanaga, S. and Omori-Satoh, T., 1989 Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis, J. Biochem. (Tokyo) 105:847.
Morita, T. and Iwanaga, S., 1981 Prothrombin activator from Echis carinatus venom, Methods Enzymol. 80:303.
Neeper, M. P. and Jacobson, M. A., 1990 Sequence of a cDNA clone encoding the platelet aggregation inhibitor trigramin, Nucleic Acids Res. 18:4255.
Ohsaka, A., 1979 Hemorrhagic, necrotizing and edema-forming effects of snake venoms, in: Handbook of Experimental Pharmacology Vol. 52, Snake Venoms, Lee, C.-Y., ed, pp. 480–546, Springer Verlag, New York.
Retzios, A. D. and Markland, F. S. Jr., 1992 Purification, characterization, and fibrinogen cleavage sites of three fibrinolytic enzymes from the venom of Crotalus basiliscus basiliscus, Biochemistry 31:4547.
Sanchez, E. F., Diniz, C. R. and Richardson, M., 1991 The complete amino acid sequence of the haemorrhagic factor LHFII, a metalloproteinase isolated from the venom of the bushmaster snake (Lachesis muta muta), FEBS Lett. 282:178.
Scarborough, R. M., Rose, J. W., Hsu, M. A., Phillips, D. R., Fried V. A., Campbell, A. M., Hannizzi, L. and Charo, I. F., 1991 Barbourin: a GPIIb–IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri, J. Biol. Chem. 266:9359.
Shannon, J. D., Baramova, E. N., Bjarnason, J. B. and Fox, J. W., 1989 Amino acid Sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin, J. Biol. Chem. 264:11575.
Takeya, H., Arakawa, M., Miyata, T., Iwanaga, S. and Omori-Satoh, T., 1989 Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of habu snake, Trimeresurus flavoviridis, J. Biochem. (Tokyo) 106:151.
Takeya, H., Oda, K., Miyata, T., Omori-Satoh, T. and Iwanaga, S., 1990a The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis, J. Biol. Chem. 265:16068.
Takeya, H., Onikura, A., Nikai, T., Sugihara, H. and Iwanaga, S., 1990b Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber, J. Biochem. (Tokyo) 108:711.
Takeya, H., Kubo, J., Omori-Satoh, T. and Iwanaga, S., 1991 Snake venom platelet aggregation inhibitor, trigramin-like polypeptide, originates in the high molecular mass hemorrhagic protein, Thomb. Haemostas. 65:842.
Takeya, H., Nishida, S., Miyata, T., Kawata, S., Saisaka, Y., Morita, T. and Iwanaga, S., 1992a Coagulation factor X activating enzyme from Russell’s viper venom (RVV-X), J. Biol. Chem. 267:14109.
Takeya, H., Nishida, S., Nishino, N., Makinose, Y., Omori-Satoh, T., Nikai, T., Sugihara, H. and Iwanaga, S., 1992b Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes, J. Biochem. (Tokyo), in press.
Takeya, H., Nishino, K., Miyata, T., Omori-Satoh, T. and Iwanaga, S., 1992c Snake venom hemorrhagic and non-hemorrhagic metalloendopeptidases, Methods Enzymol., in press.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media New York
About this chapter
Cite this chapter
Iwanaga, S., Takeya, H. (1993). Structure and Function of Snake Venom Metalloproteinase Family. In: Imahori, K., Sakiyama, F. (eds) Methods in Protein Sequence Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1603-7_14
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1603-7_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1605-1
Online ISBN: 978-1-4899-1603-7
eBook Packages: Springer Book Archive