Fibrinolytic and antithrombotic protease from Spirodela polyrhiza

Bioscience, Biotechnology and Biochemistry

Volumn 65, Issue 4, 2001, Pages 781-786

  Choi, Hye Seon ^a   Sa, You Seon ^a  

^a University of Ulsan   (South Korea)

Author keywords

Anticoagulatory; Antithrombotic; Fibrinolytic protease; Spirodela polyrhiza; Thrombin time

Indexed keywords

FIBRINOLYTIC AGENT; PROTEINASE;

ARTICLE; BLOOD CLOTTING; CHEMISTRY; CHINA; DRUG EFFECT; ENZYME SPECIFICITY; HUMAN; IN VITRO STUDY; MEDICINAL PLANT; POLYACRYLAMIDE GEL ELECTROPHORESIS; SPECIES DIFFERENCE;

BLOOD COAGULATION; CHINA; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASES; FIBRINOLYTIC AGENTS; HUMANS; PLANTS, MEDICINAL; SPECIES SPECIFICITY; SUBSTRATE SPECIFICITY;

EID: 0035320981     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.781     Document Type: Article

References (26)

1. Sherry, S., Recombinant tissue plasminogen activator (rt-PA): is it the thrombolytic agent of choice for an evolving acute myocardial infarction? Am. J. Cardiol., 59, 984-989 (1987).
2. Duval-Jobe, C. and Parmely, M. J., Regulation of plasminogen activation by human U937 promyelocytic cells. J. Biol. Chem., 269, 21353-21357 (1994).
3. Stringer, H. A. and Pannekoek, H., The significance of fibrin binding by plasminogen activaotor inhibitor 1 for the mechanism of tissue-type plasminogen activator-mediated fibrinolysis. J. Biol. Chem., 270, 11205-11208 (1995).
4. Olson, S. T., Bjo, I., Sheffer, R., Craig, P. A., Shore, J. D., and Choay, J., Role of the antithrombin-binding pentasaccharides in heparin accerleration of antithrombin-proteinase reactions. J. Biol. Chem., 267, 12528-12538 (1992).
5. Strube, K.-H., Kroger, B., Bialojan, S., Otte, M., and Dodt, J., Isolation, sequence anlysis, and cloning of haemadin. J Biol. Chem., 268, 8590-8595 (1993).
6. Noeske-Jungblut, C., Haendler, B., Donner, P., Alagon, A., Possani, L., and Schleuning, W.-D., Triabin, a highly potent exosite inhibitor of thrombin. J. Biol. Chem., 270, 28629-28634 (1995).
7. Nikai, T., Mori, N., Kishida, M., Sugihara, H., and Tu, A., T. Isolation and biochemical characterization of hemorragic toxin f from the venom of Crotalus atrox. Arch. Biochem. Biophys., 231, 309-319 (1984).
8. Jeon, O.-H., Moon, W.-J., and Kim, D.-S., An anticoagulant/fibrinolytic protease from Lumbricus rubellus. J. Biochem. Molec. Biol., 28, 138-142 (1995).
9. Kim, W., Choi, K., Kim, Y., Park, H., Choi, J., Lee, Y., Oh, H., Kwon, I., and Lee, S., Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from chungkook-jang. Appl. Environ. Microbiol., 62, 2482-2488 (1996).
10. Sumi, H., Hamada, H., Tsushima, H., Mihara, H., and Muraki, H., A novel fibrinolytic enzyme in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experimentia, 43, 1110-1111 (1987).
11. Sumi, H., Hamada, H., Nakanishi, K., and Hiratani, H., Enhancement of the fibrinolytic activity in plasma by oral administration of NK. Acta Haematol., 84, 139-143 (1990).
12. Naski, M. C., Fenton II, J. W., Maraganore, J. M., Olson, S. T., and Shafer, J. A., The COOH-terminal domain of hirudin. J. Biol. Chem., 265, 13484-13489 (1990).
13. Choi, H. S. and Shin, H. H., Purification and characterization of a fibrinolytic protease in Pleurotus ostreatus. Mycologia, 90, 674-679 (1998).
14. Shin, H. H. and Choi, H. S., Purification and partial characterization of a metalloprotease in Flammulina velutipes. J. Microbiol., 36, 20-25 (1998).
15. Choi, H. S. and Sa, Y. S., Fibrinolytic and antithrombotic protease from Ganoderma lucidum. Mycologia, 92, 545-552 (2000).
16. Hofmann, W. and Bon, C., Blood coagulation induced by the venom of Bothrops atrox. 1. Identification, purification, and properties of a prothrombin activator. Biochemistry, 26, 772-776 (1987).
17. Bode, W., Turk, D., and Karshikov, A., The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human thrombin: structure analysis, overall structure, electrostatic properties, detailed active site geometry, and structure-function relationships. Protein science, 1, 426-471 (1992).
18. Tasset, D. M., Kubik, M. F., and Steiner, W., Oligonucleotide inhibitors of human thrombin that bind distinct epitopes. J. Mol. Biol., 272, 688-698 (1997).
19. Dahlback, B., Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system. Thromb. Haemost., 66, 49-61 (1991).
20. Maraganore, J. R., Healy, J. F., and Parker, E. T., Inhibition of thrombin activation of factor VIII by a synthetic peptide corresponding to residues 1675-1686 in factor VIII. Circulation, 86, 413-416 (1992).
21. Stubbs, M., Oschkinat, H., Mayr, I., Huber, R., Angliker, H., Stone, S. R., and Bode, W., The interaction of thrombin with fibrinogen-A structural basis for its specificity. Eur. J. Biochem., 206, 187-195 (1992).
22. Rezaie, A. R., Cooper, S. T., Church, F. C., and Esmon, C. T., Protein C inhibitor is a potent inhibitor of the thrombin-thrombomodulin complex. J. Biol. Chem., 270, 25336-25339 (1995).
23. Jakubowski, J. A. and Maraganore, J. M., Inhibition of coagulation and thrombin-induced platelet activities by a synthetic dodecapeptide modeled on the carboxy-terminus of hirudin. Blood, 75, 399-406 (1990).
24. Tsiang, M., Lentz, S. R., Dittman, W. A., Scarpati, E. M., and Sadler, J. E., Equilibrium binding of thrombin to recombinant human thrombomodulin: Effects of hirudin, fibrinogen, factor Va, and peptide analogues. Biochemistry, 29, 10602-10612 (1990).
25. Friedrich, T., Kroger, B., Bialojan, S., Lemaire, H. G., Hoffken, H. W., Reuschenbach, P., Otte, M., and Dodt, J., A kazal-type inhibitor with thrombin specificity from Rhodnius prolixus. J. Biol. Chem., 268, 16216-16222 (1993).
26. Holsat, J., Lindblad, B., and Bergqvist, D., Antithrombotic effect of recombinant truncated tissue factor pathway inhibitor (TFPI1-161) in experimental venous thrombosis-a comparison with low molecular weight heparin. Thromb. Haemost, 71, 214-219 (1994).