The anticoagulant fraction from the leaves of Diospyros Kaki L. has an antithrombotic activity

Archives of Pharmacal Research

Volumn 28, Issue 6, 2005, Pages 667-674

  You, Seon Sa ^a   Kim, Soo Jin ^a   Choi, Hye Seon ^a  

^a University of Ulsan   (South Korea)

Author keywords

Anticoagulant; Antithrombotic; Leaves of persimmon (Diospyros kaki L); Thrombin time

Indexed keywords

ANTICOAGULANT AGENT; FIBRINOLYTIC AGENT; PLANT EXTRACT; PROTEINASE; SUBTILISIN;

ARTICLE; BLOOD CLOTTING; CHEMISTRY; DRUG EFFECT; HUMAN; IN VITRO STUDY; ISOLATION AND PURIFICATION; PARTIAL THROMBOPLASTIN TIME; PERSIMMON; PLANT LEAF; PROTHROMBIN TIME; THROMBIN TIME;

ANTICOAGULANTS; BLOOD COAGULATION; DIOSPYROS; ENDOPEPTIDASES; FIBRINOLYTIC AGENTS; HUMANS; PARTIAL THROMBOPLASTIN TIME; PLANT EXTRACTS; PLANT LEAVES; PROTHROMBIN TIME; SUBTILISINS; THROMBIN TIME;

EID: 24944520079     PISSN: 02536269     EISSN: 02536269     Source Type: Journal    
DOI: 10.1007/BF02969356     Document Type: Article

References (31)

1. Carter, W. J., Myles, T., Gibbs, C. S., Leung, L. L., and Huntington, J. A., Crystal structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery. J. Biol. Chem., 279, 26387-26394 (2004).
2. Cho, J., Seo, H., Yun, C., Koo, B., Yoshida, S., Koga, T., Dan, T., and Kim, H., In vitro and in vivo stuies of AT-1362, a newly synthesized and orally active inhibitor of thrombin. Thromb. Res., 100, 97-107 (2000).
3. Cho, H. R. and Choi, H. S. Effects of anticoagulant from Spirodela polyrhiza in rats. Biosci. Biotechnol. Biochem., 67, 881-883 (2003).
4. Choi, H. S. and Sa, Y. S., Fibrinolytic and antithrombotic protease from Spirodela polyrhiza. Biosci. Biotechnol. Biochem., 65, 781-786 (2001).
5. 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).
6. Herbert, J. M., Herault, J. P., Bernat, A., van Amsterdam, R. G. M., lormeau, J. C., Petitou, M., van Boeckel, C., Hoffmann, P., and Meuleman, D. G., Biochemical and pharmacological properties of Sanorg 34006, a potent and long-acting synthetic pentasaccharide. Blood, 91, 4197-4205 (1998).
7. 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).
8. 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).
9. 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).
10. Kang, K. T., Jung, B. I., Bae, O. N., Lee, M. Y., Chung, S. M., Lee, J. Y., Lee, S. K., Kim, I. C., and Chung, J. H., Antithrombotic activity of LB30057, a newly synthesized direct thrombin inhibitor. Thromb. Haemost., 89,104-111 (2003).
11. Lettino, M. and Toschi, V., Direct antithrombins: new perspectives in cardiovascular medicine. Curr. Med. Chem. Cardiovasc. Hematol. Agents, 2, 267-275 (2004).
12. Liu, F., Craft, R. M., Morris, S. A., and Carroll, R. C., Lotrafiban: an oral platelet glycoprotein IIb/IIIa blocker. Expert. Opin. Investig. Drugs, 9, 2673-2687 (2000).
13. Markwardt, F., Hirudin as alternative anticoagulant-a historical review. Semin. Thromb. Hemost., 28, 405-414 (2002).
14. McClanahan, T. B., Hicks, G. W., Morrison, A. L., Peng, Y. W., Janiczek-Dolphin, N., Mertz, T. E., Sullivan, M. E., Morser, J., Juneau, P. L., and Leadley, R., The antithrombotic effects of CI-1031 (ZK-807834) and enoxaparin in a canine electrolytic injury model of arterial and venous thrombosis. Eur. J. Pharmacol., 432,187-194 (2001).
15. McGowan, E. B. and Detwiler, T. C., Modified platelet responses to thrombin. Evidence for two types of receptors or coupling mechanisms. J. Biol. Chem., 261, 739-746 (1986).
16. Moon, K. S., In Usage of Herbal Medicine (ed. Choi, O. J.), pp 466-468, Ilwolseogak (1991).
17. Muramatsu, R., Sasaki, M., Watanabe, N., Goto, Y., Okayama, T., Nukui, E., Morikawa, T., and Hayashi, H., Antithrombotic effects of NE-6505, a novel anion-binding exosite inhibitor. Thromb. Res., 86, 453-460 (1997).
18. 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).
19. Noeske-Jungblut, C., Haendler, B., Donner, P., Alagon, A., Possani, L., and Schleu ning, W-D., Triabin, a highly potent exosite inhibitor of thrombin. J. Biol. Chem., 270, 28629-28634 (1995).
20. Okonogi, T., Hattori, Z., Ogiso, A., and Mitsui, S., Detoxification by persimmon tannin of snake venoms and bacterial toxins. Toxicon, 17, 524-527 (1979).
21. Olson, S. T., Bjo, I., Sheffer, R., Craig, P. A., Shore, J. D., and Choay, J., Role of the antithrombin-binding pentasaccharides in heparin acceleration of antithrombin-proteinase reactions. J. Biol. Chem., 267, 12528-12538 (1992).
22. Rezaie, A. R., Cooper, S. T., Church, F. C., and Esmon, C. T., Protein C inhibitor is a potent inhibitor of the thrombinthrombomodulin complex. J. Biol. Chem., 270, 25336-25339 (1995).
23. Renda, G., Rocca, B., Crocchiolo, R., Cristofaro, R.D., and Landolfi, R., Effect of fibrinogen concentration and platelet count on the inhibitory effect of abciximab and tirofiban. Thromb. Haemost., 89, 348-354 (2003).
24. Richardson, J. L., Kroger, B., Hoeffken, W., Sadler, J. E., Pereira, P., Huber, R., Bode, W., and Fuentes-Prior, P., Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor. EMBO J., 19, 5650-5660 (2000).
25. Sa, Y. S., Kim, K. A., and Choi, H. S., Purification and characterization of anti-coagulant activity from persimmon stem. J. Kor. Soc. Food Sci. Nutr., 32, 1323-1327 (2003).
26. Strube, K.-H., Kroger, B., Bialojan, S., Otte, M., and Dodt, J., Isolation, sequence analysis, and cloning of haemadin. J. Biol. Chem., 268, 8590-8595 (1993).
27. Stubbs, M. T., 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).
28. Tsiang, M., Lentz, S. R., Dittman, W. A., Wen, D., Scarpati, E. M., and Sadler, J. E., Equilibrium binding of thrombin to recombinant human thrombomodulin: effect of hirudin, fibrinogen, factor Va, and peptide analogues. Biochemistry, 29, 10602-10612 (1990).
29. Wall, D., Douglas, S., Ferro, V., Cowden, W., and Parish, C., Characterisation of the anticoagulant properties of a range of structurally diverse sulfated oligosaccharides. Thromb. Res., 103, 325-335 (2001).
30. Wong, P. C., Crain, E. J., Watson, C. A., Zaspel, A. M., Wright, M. R., Lam, P. Y., Pinto, D. J., Wexler, R. R., and Knabb, R. M., Nonpeptide factor Xa inhibitors III: effects of DPC423, an orally-active pyrazole antithrombotic agent, on arterial thrombosis in rabbits. J. Pharmacol. Exp. Ther., 303, 993-1000 (2002).
31. Yuk, D. Y., Ryu, C. K., Hong, J. T., Chung, K. H., Kang, W. S., Kim, Y., Yoo, H. S., Lee, M. K., Lee, C. K., and Yun, Y. P., Antithrombotic and antiplatelet activities of 2-chloro-3-[4-(ethylcarboxy)-phenyl]-amino-1,4- naphthoquinone (NQ12), a newly synthesized 1,4-naphthoquinone derivative. Biochem. Pharmacol., 60, 1001-1008 (2000).