Purification and Characterization of Serine Protease Inhibitors from Dolichos lablab Seeds; Prevention Effects on Pseudomonal Elastase-Induced Septic Hypotension

Journal of Biochemistry and Molecular Biology

Volumn 33, Issue 2, 2000, Pages 112-119

  Koo, Sun Hyang ^a   Choi, Yun Lim ^b   Choi, Su Kyung ^a   Shin, Young Hee ^b   Kim, Byeong Gee ^a   Lee, Bok Luel ^a  

^a Pusan National University   (South Korea)

^b Kyungsung University   (South Korea)

Author keywords

Dolichos lablab; Plant; Pseudomonal elastase; Septic shock; Serine protease inhibitors

Indexed keywords

EID: 0034395902     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (38)

1. Bensky, D. and Gamble, A. (1993) Chinese herbal medicine; Materia Medica, 2nd ed., Eastland Press, Inc. Seattle, Washington.
2. Birk, Y. (1985) The Bowman-Birk inhibitors: Trypsin-and chymotrypsin-inhibitor from soybeans. Int. J. Peptide protein Res. 25, 113-131.
3. Blauhut, B., Gross, C., Necek, S., Doran, J. E., Spath, P. and Lundsgaard-Hansen, P. (1991) Effects of high-dose aprotinin on blood loss, platelet function, fibrinolysis, complement, and renal function after cardiopulmonary bypass. J. Thorac. Cardiovasc. Surg. 101, 958-967.
4. Cho, M. Y., Lee, H. S., Lee, K. M., Homma, K., Natori, S. and Lee, B. L. (1999) Molecular cloning and functional properties of two early-stage encapsulation-relating proteins from the coleopteran insect, Tenebrio molitor larvae. Eur. J. Biochem. 262, 737-744.
5. Colman, R. W. (1984) Surface-mediated defense reactions. The plasma contact activation system. J. Clin. Invest. 73, 1249-1253.
6. Dixon, M. (1953) Determination of enzyme-inhibitor constants. Biochem. J. 55, 170-171.
7. Erlanger, B. F., Kokowsky, N. and Cohen, E. (1961) Preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278.
8. Fritz, H. (1979) Proteinase inhibitors in severe inflammatory processes (septic shock and experimental endotoxaemia): biochemical, pathophysiological and therapeutic aspects. Ciba Found. Symp. 75, 351-379.
9. Goode, H. F., P.D., H., Walker, B. E. and Webster, N. R. (1995) Nitric oxide synthase activity is increased in patients with sepsis syndrome. Clin. Sci. 88, 131-133.
10. Harle, H. and Rahman, S. (1989) The effect of aprotinin administration on the intraoperative histamine release and haemostatic disorders. Adv. Exp. Med. Biol. 240, 509-514.
11. Hwa, J. J., Ghibaudi, L., Williams, P., Chintala, M., Zhang, R., Chatterjee, M. and Sybertz, E. (1996) Evidence for the presence of a proteinase-activated receptor distinct from the thrombin receptor in vascular endothelial cells. Circ. Res. 78, 581-588.
12. Ikenaka, T., Odani, S. and Koide, T. (1974) Chemical structure and inhibitory activity of soybean proteinase inhibitors, in. Bayer-symposium V proteinase inhibitors (Springer-Verlag)., 325.
13. Ishikawa, C., Watanabe, K., Sakata, N., Nakagaki, C., Nakamura, S. and Takahashi, K. (1985) Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. J. Biochem. (Tokyo) 97, 55-70.
14. Jang, K. S., Cho, M. Y., Choi, H. W., Lee, K. M., Kim, M. H., Lee, Y. U., Kurata, S., Natori, S. and Lee, B. L. (1998) Purification and characterization of a 25 kDa cathepsin L-like protease from the hemocyte of coleopteran insect, Tenebrio molitor larvae. J. Biochem. Mol. Biol. 31, 364-369.
15. Joubert, F. J., Kruger, H., Townshend, G. S. and Botes, D. P. (1979) Purification, some properties and the complete primary structures of two protease inhibitors (DE-3 and DE-4) from Macrotyloma axillare seed. Eur. J. Biochem. 97, 85-91.
16. Kaminishi, H., Tanaka, M., Cho, T., Maeda, H. and Hagihara, Y. (1990) Activation of the plasma kallikrein-kinin system by Candida albicans proteinase. Infect. Immun. 58, 2139-2143.
17. Katori, M., Majima, M., Odoi-Adome, R., Sunahara, N. and Uchida, Y. (1989) Evidence for the involvement of a plasma kaliikrein-kinin system in the immediate hypotension produced by endotoxin in anaesthetized rats. Br. J. Pharmacol. 98, 1383-1391.
18. Khan, M. M. H., Yamamoto, T., Araki, H., Shibuya, Y. and Kambara, T. (1993a) Role of Hageman factor/kallikrein-kinin system in pseudomonal elastase-induced shock model. Biochim. Biophys. Acta. 1157, 119-126.
19. Khan, M. M. H., Yamamoto, T., Araki, H., Shibuya, Y., Okamato, M. and Kambara, T. (1993b) Pseudomonal elastase injection causes low vascular resistant shock in guinea pigs. Biochim. Biophys. Acta. 1182, 83-93.
20. Khan, M. M. H., Shibuya, Y., Kambara, T. and Yamamoto, T. (1995) Role of alpha-2-macroglobulin and bacterial elastase in guinea-pig pseudomonal septic shock. Int. J. Exp. Pathol. 76, 21-28.
21. Koide, T. and Ikenaka, T. (1973) Studies on soybean trypsin inhibitors, Amino acid sequence of the carboxy-terminal region and the complete amino acid sequence of soybean trypsin inhibitors.(Kunitz). Eur. J. Biochem. 32, 417-431.
22. Kunitz, m. (1947a) Crystalline soybean trypsin inhibitor. Am. J. Physiol. 218, 1113-1117.
23. Kunitz, M. (1947b) Isolation of a crystalline protein compound of trypsin and of soybean trypsin-inhibitor. J. Gen. Physiol. 30, 311-320.
24. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
25. Laskowski, M. and Kato, I. (1980) Protein inhibitors of proteinases. Ann. Rev. Biochem. 49, 593-626.
26. Maeda, H. and Yamamoto, T. (1996) Pathogenic mechanisms induced by microbial proteases in microbial infections. Biol. Chem. Hoppe Seyler 377, 217-226.
27. Maruo, K., Akaike, T., Inada, Y., Ohkubo, I. and Maeda, H. (1993) Effect of microbial and mite protease on low and high molecular weight kininogens. J. Biol. Chem. 268, 17711-17715.
28. Ochoa, J. B., Curti, B. and Peitzman, A. B. (1992) Increased circulating nitrogen oxides after human tumor immunotherapy: correlation with toxic hemodynamic changes. J. Natl. Cancer Inst. 84, 864-867.
29. Odani, S. and Ikenaka, T. (1972) Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence and the anti-proteinase sites of Bowman-Birk soybean proteinase inhibitor. J. Biochem. (Tokyo) 71, 839-848.
30. Odani, S. and Ikenaka, T. (1977) Studies on soybean trypsin inhibitors. XI. Complete amino acid sequence of a soybean trypsin-chymotrypsin-elastase inhibitor, C-II. J. Biochem. (Tokyo) 82, 1523-1531.
31. Odani, S. and Ikenaka, T. (1978) Studies on soybean trypsin inhibitors. XIII. Preparation and characterization of active fragments from Bowman-Birk proteinase inhibitor. J. Biochem. (Tokyo) 83, 747-753.
32. Redl, H., Schlag, G., Paul, E. and Schiesser, A. (1986) Cellular (thrombocytes, granulocytes) effects of proteinase inhibitors -gabexylate, gabexate mesilate (FOY) and aprotinin. Resuscitation 14, 81-90.
33. Roberts, F. J., Greere, I. W. and Coldman, A. (1991) A three year study of positive blood culture, with emphasis on prognosis. Rev. Infect. Dis. 13, 34-43.
34. Ryan, C. A. (1990) Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Ann. Rev. Phytopathol. 28, 425-429.
35. Shin, Y. H., Kojma, Y. and Maeda, H. (1996a) Conjugation of succinylated gelatin to soybean trypsin inhibitor. J. Bioact. Compat. Polymers. 11, 3-16.
36. 1/2. Immunopharmacology 33, 369-373.
37. Takakura, Y., Fujita, T., Hashida, M., Maeda, H. and Sezaki, H. (1989) Control pharmaceutical properties of soybean trypsin inhibitor by conjugation with Dextran II: Biopharmaceutical and pharmacological properties. Pharm. Sci. 78, 219-222.
38. Travis, J., Potempa, J. and Maeda, H. (1995) Are bacterial proteinases pathogenic factors? Trends Microbiol. 3, 405-407.