Amyloid-degrading ability of nattokinase from bacillus subtilis natto

Journal of Agricultural and Food Chemistry

Volumn 57, Issue 2, 2009, Pages 503-508

  Hsu, Ruei Lin ^a,b   Lee, Kung Ta ^b   Wang, Jung Hao ^b   Lee, Lily Y L ^a   Chen, Rita P Y ^a,b  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

Amyloid; Amyloid degradation; Amyloidosis; Fibril; Natto; Nattokinase; Subtilisin nat

Indexed keywords

BACILLUS SUBTILIS;

AMYLOID; BACTERIAL PROTEIN; NATTOKINASE; SERINE PROTEINASE; SUBTILISIN;

ALZHEIMER DISEASE; ARTICLE; BACILLUS SUBTILIS; BACTERIUM; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; HUMAN; METABOLISM; PRION DISEASE;

ALZHEIMER DISEASE; AMYLOID; BACILLUS SUBTILIS; BACTERIA; BACTERIAL PROTEINS; ENZYME STABILITY; HUMANS; PRION DISEASES; SERINE ENDOPEPTIDASES; SUBTILISINS;

EID: 59849097376     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf803072r     Document Type: Article

References (30)

1. Ueda, S. Industrial applications of B. subtilis: utilization of soybean as natto, a traditional Japanese food. In Bacillus subtilis: molecular biology and industrial applications; Maruo, B., Yoshikawa, H., Eds.; Elsevier Science B. V.: Amsterdam, the Netherlands, 1989; pp 143-161.
2. Peng, Y.; Yang, X.; Zhang. Y. Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo. Appl. Microbiol, Biotechnol. 2005, 69, 126-132.
3. Sumi, H.; Hamada, H.; Tsushima, H.; Mihara, H.; Muraki, H. A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia 1987, 43, 1110-1111.
4. Kamata. H.; Yamagata. Y.; Nakamura, T.; Nakajima, T.; Oda, K.; Murao, S.; Ichishima, E. Characterization of the complex between a2-macroglobulin and a serine proteinase from Bacillus natto. Agri. Biol. Chem. 1989, 53, 2695-2702.
5. Fujita, M.; Nomura, K.; Hong, K.; Ito, Y.; Asada, A.; Nishimuro, S. Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan. Biochem. Biophys. Res. Commun. 1993, 197, 1340-1347.
6. Nakamura, T.; Yamagata, Y.; Ichishima, E. Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto). Biosci., Biotechnol., Biochem. 1992, 56, 1869-1871.
7. Fujita, M.; Hong, K.; Ito, Y.; Fujii. R.; Kariya, K.; Nishimuro. S. Thrombolytic effect of nattokinase on a chemically induced thrombosis model in rat. Biol. Pharm. Bull. 1995, 18, 1387-1391.
8. Urano, T.; Ihara, H.; Umemura, K.; Suzuki, Y.; Oike, M.; Akita, S.; Tsukamoto, Y.; Suzuki, I.; Takada, A. The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis cleaves and inactivates plasminogen activator inhibitor type 1. J. Biol. Chem. 2001, 276, 24690-24696.
9. Chang, C. T.; Fan, M. H.; Kuo, F. C.; Sung, H. Y. Potent fibrinolytic enzyme from a mutant of Bacillus subtilis IMR-NK1. J. Agric. Food Chem. 2000, 48, 3210-3216.
10. Fujita, M.; Hong, K.; Ito, Y.; Misawa, S.; Takeuchi, N.; Kariya, K.; Nishimuro, S. Transport of nattokinase across the rat intestinal tract. Biol. Pharm. Bull. 1995, 18, 1194-1196.
11. Sumi, H.; Hamada, H.; Nakanishi, K.; Hiratani, H. Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase. Acta Haematol. 1990, 84, 139-143.
12. Suzuki, Y.; Kondo. K.; Matsumoto, Y.; Zhao. B. Q.; Otsuguro, K.; Maeda, T.; Tsukamoto, Y.; Urano, T.; Umemura, K. Dietary supplementation of fermented soybean, natto, suppresses intimal thickening and modulates the lysis of mural thrombi after endothelial injurv in rat femoral arterv. Life Sci. 2003, 73, 1289-1298.
13. Banerjee, A.; Chisti, Y.; Banerjee, U. C. Streptokinase - a clinically useful thrombolytic agent. Biotechnol. Adv. 2004, 22, 287-307.
14. Uversky, V. N.; Fink, A. L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 2004, 1698, 131-153.
15. Chen, P. Y.; Lin, C. C.; Chang, Y. T.; Lin, S. C.; Chan, S. I. One O-linked sugar can affect the coil-to-β structural transition of the prion peptide. Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 12633-12638.
16. Zhang, H.; Kaneko, K.; Nguyen, J. T.; Livshits, T. L.; Baldwin, M. A.; Cohen, F. E.; James, T. L.; Prusiner, S. B. Conformational transformations in peptides containing two putative α-helices of the prion protein. J. Mol. Biol. 1995, 250, 514-526.
17. Kuo, L. C.; Cheng, W. Y.; Wu, R. Y.; Huang, C. J.; Lee, K. T. Hydrolysis of black soybean isoflavone glycosides by Bacillus subtilis natto. Appl. Microbiol. Biotechnol. 2006, 73, 314-320.
18. Kuo, L. C.; Lee, K. T. Cloning, expression, and characterization of two β-glucosidase from isoflavone glucoside-hydrolyzing Bacillus subtilis natto. J. Agric. Food Chem. 2008, 56, 119-125.
19. Friberger, P.; Knos, M.; Gustavsson, S.; Aurell, L.; Claeson, G. Methods for determination of plasmin. antiplasmin and plasminogen by means of substrate S-2251. Haemostasis 1978, 7, 138-145.
20. Chang, E. S.; Liao, T. Y.; Lim, T. S.; Fann, W.; Chen, R. P. A new amyloid-like β-aggregate with most of the amyloid characteristics except fibril morphology. J. Mol. Biol. 2008, 10.1016/j.jmb.2008.11.009.
21. Groenning, M.; Norrman, M.; Flink, J. M.; van de Weert, M.; Bukrinsky, J. T.; Schluckebier, G.; Frokjaer, S. Binding mode of Thioflavin T in insulin amyloid fibrils. J. Struct. Biol. 2007, 159, 483-497.
22. Nielsen, L.; Khurana, R.; Coats, A.; Frokjaer, S.; Brange, J.; Vyas, S.; Uversky, V. N.; Fink, A. L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001, 40, 6036-6046.
23. Tucker. H. M.; Kihiko, M.; Caldwell. J. N.; Wright, S.; Kawarabayashi, T.; Price, D.; Walker, D.; Scheff, S.; McGillis, J. P.; Rydel, R. E.; Estus, S. The plasmin system is induced by and degrades amyloid-beta aggregates. J. Neurosci. 2000, 20, 3937-3946.
24. Krebs. M. R. H.; Bromley, E. H. C.; Donald, A. M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 2005, 149, 30-37.
25. Langeveld, J. P. M.; Wang, J. J.; Van de Wiel, D. F. M.; Shih. G. C; Garssen, G. J.; Bossers, A.; Shih, J. C. H. Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J. Infect. Dis. 2003, 188, 1782-1789.
26. Coll, B. A.; Garcia, R. A.; Manner, W. N. Diffusion of protease into meat and bone meal for solubility improvement and potential inactivation of the BSE prion. PLoS ONE 2007, 2, e245.
27. Gupta, R.; Ramnani, P. Microbial keratinases and their prospective applications: an overview. Appl. Microbiol. Biotechnol. 2006, 70, 21-33.
28. Chiti, F.; Dobson. C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333-366.
29. Wang. Y. J.; Zhou, H. D.; Zhou. X. F. Clearance of amyloidbeta in Alzheimer's disease: progress, problems and perspectives. Drug Discovery Today 2006, 11, 931-938.
30. Hunter, N.; Foster, J.; Chong, A.; McCutcheon. S.; Parnham. D.; Eaton, S.; MacKenzie. C.; Houston, F. Transmission of prion diseases by blood transfusion. J. Gen. Virol. 2002, 83, 2897-2905.