CHARACTERIZATION OF TWO MAJOR FAMILIES OF FIBRINOGENOLYTIC PROTEASES FROM THE VENOM OF TAIWAN HABU WITH SPECIAL REFERENCE TO THEIR MEDICAL APPLICATIONS

References

• Au L.-C., Lin S.-B., Chou J.-S., Teh G.-W., Chang K.-J., Shih C.-M. Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma. Biochem. J. 1993; 294: 387–390, [PUBMED], [INFOTRIEVE]
   PubMedGoogle Scholar
• Barlaam B., Bird T. G., Lambert-Van Der Brempt C., Campbell D., Foster S. J., Maciewicz R. New a-substituted succinate-based hydroxamic acids as TNFa convertase inhibitors. J. Med. Chem. 1999; 42: 4890–4908, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Bjarnason J. B., Tu A. T. Hemorrhagic toxins from western diamondbackrattlesnake (Crotalus atrox) venom: Isolation and characterization of five toxins and therole of zinc in hemorrhagic toxin e. Biochemistry 1978; 17: 3395–3404, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Bjarnason J. B., Barish A., Direnzo G. S., Campbell R., Fox J. W. Kallikrein-like enzymes from Crotalus atrox venom. J. Biol. Chem. 1983; 258: 12566–12573, [PUBMED], [INFOTRIEVE]
   PubMedGoogle Scholar
• Bjarnason J. B., Barish A., Direnzo G. S., Cambell R., Fox J. W. Kallikrein-like enzyme from Crotalus atrox venom. J. Biol. Chem. 1983; 238: 12566–12573
   Google Scholar
• Black R. A., Rauch C. T., Kozlosky C. J., Peschon J. J., Slack J. L., Wolfson M. F., Castner B. J., Stocking K. L., Reddy P., Srinivasan S., Nelson N., Boiani N., Schooley K. A., Gerhart M., Davis R., Fitzner J. N., Johnson R. S., Paxton R. J., March C. J., Cerretti D. P. A metalloproteinase disintegrin that releases tumour-necrosis factor-a from cells. Nature 1997; 385: 729–733, London[PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Bode W., Grams F., Reinemer P., Gomis-Rüth F. X., Baumann U., McKay D. B., Stöcker W. The metzincin-superfamily of zinc-peptidases. Adv. Exp. Med. Biol. 1996; 389: 1–11, [PUBMED], [INFOTRIEVE], [CSA]
   PubMedGoogle Scholar
• Brinkhous K. M., Smith S. V. Platelet-aggregating noncoagulant snake venom fractions. Hemostasis and Animal Venoms, H. Pirkle, F. S. Markland, Jr. Marcel Dekker, New York 1988; 7: 363–376
   Google Scholar
• Burkhart W., Smith G. F. H., Su J. L., Parikh I., LeVine III H. Amino acidsequence determination of Ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma. FEBS Lett. 1992; 297: 297–301, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   Google Scholar
• Chiou S.-H. Fibrinogenolytic proteases with thrombolytic and antihypertensive activities: Medical application and novel process of expression and production. US Patent #6630139, Oct. 7. 2003
   Google Scholar
• Chiou S.-H., Hung C.-C., Lin C.-W. Isolation of a crotalase-like protease with -fibrinogenase activity from the Western diamondback rattlesnake, Crotalus atrox. Biochem. International 1992; 26: 105–112
   Google Scholar
• Chiou S.-H., Hung C.-C., Huang K.-F. Characterization of a protease with - and -fibrinogenase activity from the Western diamondback rattlesnake. Crotalus atrox. Biochem. Biophys. Res. Commun. 1992; 187: 389–396
   Google Scholar
• Fox J. W., Long C. The ADAMs/MDC family of proteins and their relationships to the snake venom metalloproteinases. Enzymes from Snake Venom, G. S. Bailey. Alaken, Inc., Fort Collins, Colorado 1998; 151–178
   Google Scholar
• Hite L. A., Shannon J. D., Bjarnason J. B., Fox J. W. Sequence of a cDNAencoding the Zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures. Biochemistry 1992; 31: 6203–6211, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMedGoogle Scholar
• Hite L. A., Jia L.-G, Bjarnason J. B., Fox J. W. cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys. 1994; 308: 182–191, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Huang K.-F., Hung C.-C., Chiou S.-H. Characterization of threefibrinogenolytic proteases isolated from the venom of Taiwan habu (Trimeresurusmucrosquamatus). Biochem. Mol. Biol. International 1993; 31: 1041–1050, [CSA]
   PubMedGoogle Scholar
• Huang K.-F., Hung C.-C., Pan F.-M., Chow L.-P., Tsugita A., Chiou S.-H. Characterization of multiple metalloproteinases with fibrinogenolytic activity from the venom of Taiwan habu (Trimeresurus mucrosquamatus): protein microsequencing coupled with cDNA sequence analysis. Biochem. Biophys. Res. Commun. 1995; 216: 223–233, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMedGoogle Scholar
• Huang K.-F., Hung C.-C., Wu S.-H., Chiou S.-H. Characterization of three endogenous peptide inhibitors for multiple metalloproteinases with fibrinogenolytic activityfrom the venom of Taiwan habu (Trimeresurus mucrosquamatus). Biochem. Biophys. Res. Commun. 1998; 248: 562–568, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   Google Scholar
• Huang K.-F., Chiou S.-H., Ko T.-P., Yuann J.-M., Wang A. H.-J. The 1.35Å crystal structure of cadmium-substituted TM-3, a snake venom metalloproteinase fromTaiwan habu: elucidation of a TNF converting enzyme–like active-site structure with adistorted octahedral geometry of cadmium. Acta Cryst. 2002; D58: 1118–1128, [CSA]
   Google Scholar
• Huang K.-F., Chiou S.-H., Ko T.-P., Wang A. H.-J. Determinants oftheinhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitorsrevealed by X-ray crystallography and synthetic inhibitor analogues. Eur. J. Biochem. 2002; 269: 3047–3056, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMedGoogle Scholar
• Hung C.-C., Huang K.-F., Chiou S.-H. Characterization of one novel venom protease with beta-fibrinogenase activity from the Taiwan habu (Trimeresurusmucrosquamatus): purification and cDNA sequence analysis. Biochem. Biophys. Res. Commun. 1994; 205: 1707–1715, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Hung C.-C., Chiou S.-H. Fibrinogenolytic proteases isolated from the snake venom of Taiwan habu: serine proteases with kallikrein-like and angiotensin-degrading activities. Biochem. Biophys. Res. Commun. 2001; 281: 1012–1018, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Itoh N., Tanaka N., Mihashi S., Yamashina I. Molecular cloning and sequence analysis of cDNA for Batroxobin, a thrombin-like snake venom enzyme. J. Biol. Chem. 1987; 262: 3132–3135, [PUBMED], [INFOTRIEVE]
   PubMed Web of Science ®Google Scholar
• Karlsson E. Chemistry of protein toxins in snake venoms. Snake Venoms, Handbook of Experimental Pharmacology, C. Y. Lee. Springer, Berlin 1979; 52: 159–212
   Google Scholar
• Kini R. M., Evans H. J. Effects of snake venom proteins on blood platelets. Toxicon 1990; 28: 1387–1422, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Lee C. Y. Recent advances in chemistry and pharmacology of snake toxins. Advances in Cytopharmacology, B. Ceccarelli, F. Clementi. Raven Press, New York 1979; 3: 1–16
   Google Scholar
• Lijnen H. R., Collen D. Strategies for the improvement of thrombolytic agents. Thrombos. Haemostas. 1991; 66: 88–110
   Google Scholar
• Markland F. S., Jr. Fibrinogenolytic and fibrinolytic enzymes. Enzymes from Snake Venom, G. S. Bailey. Alaken, Inc., Fort Collins, Colorado 1998; 71–149
   Google Scholar
• Markland F. S., Damus P. S. Purification and properties of a thrombin-likeenzyme from the venom of Crotalus adamanteus. J. Biol. Chem. 1971; 246: 6460–6473, [PUBMED], [INFOTRIEVE]
   PubMed Web of Science ®Google Scholar
• Maskos K., Fernandez-Catalan C., Huber R., Bourenkov G. P., Bartunik H., Ellestad G. A., Reddy P., Wolfson M. F., Rauch C. T., Castner B. J., Davis R., Clarke H. R., Petersen M., Fitzner J. N., Cerretti D. P., March C. J., Paxton R. J., Black R. A., Bode W. Crystal structure of the catalytic domain of human tumor necrosis factor-a-converting enzyme. Proc. Natl. Acad. Sci. U S A 1998; 95: 3408–3412, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Meaume J. Snake venoms as modifying agents of blood coagulation. Toxicon. 1966; 4: 25–58, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Moss M. L., Jin S. L. C., Milla M. E., Burkhart W., Carter H. L., Chen W. J., Clay W. C., Didsbury J. R., Hassler D., Hoffman C. R., Kost T. A., Lambert M. H., Leesnitzer M. A., McCauley P., McGeehan G., Mitchell J., Moyer M., Pahel G., Rocque W., Overton L. K., Schoenen F., Seaton T., Su J. L., Warner J., Willard D., Becherer J. D. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-a. Nature 1997; 385: 733–736, London[PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Neeper M. P., Jacobson M. A. cDNA sequence of the precursor of trigramin. Nucleic Acids Res. 1990; 18: 4255, [PUBMED], [INFOTRIEVE]
   PubMed Web of Science ®Google Scholar
• Ouyang C., Teng C.-M., Huang T.-F. Characterization of snake venom principles affecting blood coagulation and platelet aggregation. Adv. Exp. Med. Biol. 1990; 281: 151–163, [PUBMED], [INFOTRIEVE]
   Google Scholar
• Ouyang C., Teng C.-M. The effect of the purified anticoagulant principle of Agkistrodon acutus venom on blood coagulation. Toxicon. 1973; 11: 287–292, [PUBMED], [INFOTRIEVE], [CROSSREF]
   Google Scholar
• Ouyang C. The effects of Formosan snake venoms on blood coagulation in vitro. J. Formosan Med. Assoc. 1957; 56: 435–448
   Google Scholar
• Ouyang C., Teng C.-M. Purification and properties of the anticoagulantprinciple of Agkistrodon acutus venom. Biochim. Biophys. Acta 1972; 278: 155–162, [PUBMED], [INFOTRIEVE]
   Google Scholar
• Ouyang C., Yang F.-Y. Purification and properties of the thrombin-likeenzyme from Trimeresurus gramineus. Biochim. Biophys. Acta 1974; 351: 354–363, [PUBMED], [INFOTRIEVE]
   PubMedGoogle Scholar
• Ouyang C., Teng C.-M. Fibrinogenolytic enzymes of Trimeresurusmucrosquamatus venom. Biochim. Biophys. Acta 1976; 420: 298–308, [PUBMED], [INFOTRIEVE]
   PubMed Web of Science ®Google Scholar
• Ouyang C., Teng C.-M., Chen Y.-C. Physicochemical properties of - and -fibrinogenases of Trimeresurus mucrosquamatus venom. Biochim. Biophys. Acta 1977; 481: 622–630, [PUBMED], [INFOTRIEVE]
   PubMedGoogle Scholar
• Pandya B. V., Budzynski A. Z. Anticoagulant proteases from westerndiamondback (Crotalus atrox) venom. Biochemistry 1984; 23: 460–470, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Rooke J., Pan D., Xu T., Rubin G. M. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 1996; 273: 1227–1231, [PUBMED], [INFOTRIEVE]
   PubMed Web of Science ®Google Scholar
• Stocker K. F. Snake venom protein effects on hemostasis and fibrinolysis. Medical Use of Snake Venom Proteins, K. F. Stocker. CRC Press, Boca Raton, Florida 1990; 97–161
   Google Scholar
• Stöcker W., Grams F., Baumann U., Reinemer P., Gomis-Ruth F. X., Mckay D. B., Bode W. The metzincins–topological and sequential relations between theastacins, adamalysins, serralysins, and matrixins (collagenases). Protein Sci. 1995; 4: 823–840, [CSA]
   PubMed Web of Science ®Google Scholar
• Stöcker W., Bode W. Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 1995; 5: 383–390, [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar
• Tortorella M. D., Burn T. C., Pratta M. A., Abbaszade I., Hollis J. M., Liu R., Rosenfeld S. A., Copeland R. A., Decicco C. P., Wynn R., Rockwell A., Yang F., Duke J. L., Solomon K., George H., Bruckner R., Nagase H., Itoh Y., Ellis D. M., Ross H., Wiswall B. H., Murphy K., Hillman M. C., Hollis G. F., Newton R. C., Magolda R. L., Trzaskos J. M., Arner E. C. Purification and cloning of aggrecanase-1: amember of the ADAMTS family of proteins. Science 1999; 284: 1664–1666, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Tu A. T. Hemorrhagic factors from rattlesnakes. Rattlesnake Venoms: Their Actions and Treatment, A. T. Tu. Marcel Dekker, New York 1982; 247–312
   Google Scholar
• Tu A. T. Overview of snake venom chemistry. Adv. Exp. Med. Biol. 1996; 391: 37–62, [PUBMED], [INFOTRIEVE], [CSA]
   Google Scholar
• Wolfsberg T. G., White J. M. ADAMs in fertilization and development. Develop. Biol. 1996; 180: 389–401, [PUBMED], [INFOTRIEVE], [CROSSREF]
   PubMed Web of Science ®Google Scholar
• Xue C. B., Voss M. E., Nelson D. J., Duan J. J., Cherney R. J., Jacobson I. C., He X., Roderick J., Chen L., Corbett R. L., Wang L., Meyer D. T., Kennedy K., DeGradodagger W. F., Hardman K. D., Teleha C. A., Jaffee B. D., Liu R. Q., Copeland R. A., Covington M. B., Christ D. D., Trzaskos J. M., Newton R. C., Magolda R. L., Wexler R. R., Decicco C. P. Design, synthesis, and structure-activity relationships of macrocyclic hydroxamic acids that inhibit tumor necrosis factor a release in vitro and in vivo. J. Med. Chem. 2001; 44: 2636–2660, [PUBMED], [INFOTRIEVE], [CROSSREF], [CSA]
   PubMed Web of Science ®Google Scholar