Identification of pro-drug type ACE inhibitory peptide sourced from porcine myosin B: Evaluation of its antihypertensive effects in vivo

Food Chemistry

Volumn 114, Issue 2, 2009, Pages 516-522

  Muguruma, Michio ^a   Ahhmed, Abdulatef M ^a   Katayama, Kazunori ^a   Kawahara, Satoshi ^a   Maruyama, Masugi ^b   Nakamura, Toyoo ^c  

^a UNIVERSITY OF MIYAZAKI   (Japan)

^b UNIVERSITY OF MIYAZAKI   (Japan)

^c Unicafe Inc   (Japan)

Author keywords

ACE inhibitory activity; Actin; Antihypertensive activity; Myosin; Myosin B; Pro drug peptide

Indexed keywords

ACTIN; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; LEUCYLLYSYLPROLYLASPARAGINYLMETHIONINE; LYSYLARGINYLVALYLISOLEUCYLGLUTAMINYLTYROSINE; MYOSIN; MYOSIN B; PEPSIN A; PEPTIDE; PRODRUG; PROTEIN HYDROLYSATE; UNCLASSIFIED DRUG; VALYLLYSYLALANYLGLYCYLPHENYLALANINE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIHYPERTENSIVE ACTIVITY; ARTICLE; BLOOD PRESSURE REGULATION; CHROMATOGRAPHY; CONTROLLED STUDY; DRUG EFFECT; DRUG EFFICACY; DRUG IDENTIFICATION; DRUG MECHANISM; DRUG SCREENING; HYPERTENSION; IC 50; IN VIVO STUDY; KINETICS; NONHUMAN; PROTEIN HYDROLYSIS; PROTEIN ISOLATION; SEQUENCE HOMOLOGY;

RATTUS; SUS;

EID: 58749096162     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.09.081     Document Type: Article

References (30)

1. Ahhmed, M. A., Kawahara, S., & Muguruma, M. (2008). Evaluation of the discrepancy of physiochemical and rheological properties of cross-linked myosin B proteins and biopolymers catalyzed by transglutaminase in meats. In Proceeding of the 54th international congress of meat science and technology (pp. 117). August 10-15, 2008. Cape Town, South Africa.
2. Arihara K., Nakashima Y., Mukai T., Ishikawa T., and Itoh M. Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins. Meat Science 57 (2001) 319-324
3. Asihda T., Yoshimi H., Kawano Y., Matsuoka H., and Omae T. Effects of dietary salt and angiotensin-converting enzyme inhibitor on ATP-driven Ca pump and Na/Ca exchange in aortic rings of Dahl rats. Clinical and Experimental Hypertension 18 (1996) 851-871
4. Cheung H.S., Wang M.A., Ondetti E., Sabo F., and Cushman D.W. Binding of peptide substrate and inhibitors of angiotensin-converting enzyme. Journal of Biological Chemistry 255 (1980) 401-407
5. Cinq-Mars C.D., Hu C., Kitts D.D., and Li-Chan E.C.Y. Investigations into inhibitor type and mode, simulated gastrointestinal digestion, and cell transport of the angiotensin I-converting enzyme - inhibitory peptides in pacific hake (merluccius productus) fillet hydrolysate. Journal of Agricultural and Food Chemistry 56 (2008) 410-419
6. Cushman D.W., and Cheung H.S. Spectrophotometric assay and properties of the angiotensin-I converting enzyme of rabbit lung. Biochemical Pharmacology 20 (1971) 1637-1648
7. Fujita H., Yokoyama K., and Yoshikawa M. Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins. Journal of Food Science 65 (2000) 564-569
8. Haws R.M., Shaul P.W., Arant B.S., Atiyeh B.A., and Seikaly M.G. Glomerular losartan (Dup753)-sensitive angiotensin II receptor density is increased in young spontaneously hypertensive rats. Pediatric Research 35 (1994) 671-676
9. Hazato T., and Kase R. Isolation of angiotensin-converting enzyme inhibitor from porcine plasma. Biochemical Biophysical Research Communications 139 (1986) 52-55
10. Ishikawa N., Yamashiata S., and Omiya S. Iodination of carnosine and its biological activity. Yakugaku Zashi 92 (1972) 1423-1425
11. Jung W., Mendis E., Je J., Park P., Son W.B., Kim C.H., et al. Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats. Food Chemistry 94 (2006) 26-32
12. Katayama K., Fuchu H., Sakata A., Kawahara S., Yamauchi K., Kawamura Y., et al. Angiotensin-I converting enzyme inhibitory activity of porcine skeletal muscle proteins following enzyme digestion. Asian-Australasian Journal of Animal Science 16 (2003) 417-424
13. Katayama K., Tomatsu M., Fuchu H., Sugiyama M., Kawahara S., Yamauchi K., et al. Purification and characterization of angiotensin I-converting enzyme inhibitory peptide derived from porcine troponin C. Animal Science Journal 74 (2003) 53-58
14. Katayama K., Tomatsu M., Kawahara S., Yamauchi K., Fuchu H., Sugiyama M., et al. Inhibitory profile of nonapeptide derived from porcine troponin C against angiotensin I-converting enzyme. Journal of Agricultural and Food Chemistry 52 (2004) 771-775
15. Katayama K., Jamhari, Mori T., Kawahara S., Miake K., Kodama Y., et al. Angiotensin I-converting enzyme Inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats. Journal of Food Science 72 (2007) S702-S706
16. Katayama K., Henny E.A., Mori T., Ahhmed M.A., Kawahara S., Sugiyama M., et al. Porcine skeletal muscle troponin is a good source of peptides with Angiotensin I-converting enzyme Inhibitory activity and antihypertensive effects in spontaneously hypertensive rats. Journal of Agricultural and Food Chemistry 56 (2008) 355-360
17. Kostis J.B. The effect of enalapril on mortal and morbid events in patients with hypertension and left ventricular dysfunction. American Journal of Hypertension 8 9 (1995) 909-914
18. Lineweaver H., and Burk D. The determination of enzyme association constants. Journal of American Chemical Society 56 (1934) 658-666
19. Manger W.M., and Page I.H. An overview of current concepts regarding the pathogenesis and pathophysiology of hypertension. In: Rosenthal J. (Ed). Arterial hypertension: Pathogenesis, diagnosis, and therapy (1982), Springer-Verlag, New York 1-40
20. Maoa X., Ni J., Sun W., Hao P., and Fan L. Value-added utilization of yak milk casein for the production of angiotensin-I-converting enzyme inhibitory peptides. Food Chemistry 103 (2007) 1282-1287
21. Miguel A.S., and Fidel T. Evaluation of ACE inhibitory activity of dipeptides generated by the action of porcine muscle dipeptidyl peptidases. Food Chemistry 102 (2007) 511-515
22. Miguel M., Alonso J.M., Salaices M., Aleixandre A., and Lopez-Fandin R. Antihypertensive, ACE-inhibitory and vasodilator properties of an egg white hydrolysate: Effect of a simulated intestinal digestion. Food Chemistry 104 (2007) 163-168
23. Miguel M., Contreras M.M., Recio I., and Aleixandre A. ACE-inhibitory and antihypertensive properties of a bovine casein hydrolysates. Food Chemistry 112 (2009) 211-214
24. Muguruma, M., Ahhmed, M. A., & Kawahara, S. (2008). Identification of pro-drug type ACE inhibitory peptide from porcine myosin B: Antihypertensive effects of its hydrolysates in vivo. In Proceeding of the 54th international congress of meat science and technology (pp. 114). August 10-15, 2008. Cape Town, South Africa.
25. Nakashima Y., Arihara K., Sasaki A., Mio H., Ishikawa S., and Itoh M. Antihypertensive activities of peptides derived from porcine skeletal muscle myosin in spontaneously hypertensive rats. Journal of Food Science 67 (2002) 434-437
26. Ondetti M., Rubin B., and Cushman D.W. Design of specific inhibitors of Angiotensin Iconverting enzyme: New class of orally active antihypertensive agents. Science 196 (1977) 441-444
27. Papadimitriou G.C., Vafopoulou-Mastrojiannaki A., Silva V.S., Gomes A., Malcata X.F., and Alichanidis E. Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity. Food Chemistry 105 (2007) 647-656
28. Skeggs L.T., Khan J.E., and Shumaay N.P. The preparation and function of the hypertensin-converting enzyme. Journal of Experimental Medicine 103 (1965) 295-299
29. Ukeda H., Matsuda H., Osajima K., Matsufuji H., Matsui T., and Osajima Y. Peptides from peptic hydrolysate of heated sardine meat that inhibit angiotensin I converting enzyme. Nippon Nogei Kagaku Kaishi 66 (1992) 25-29
30. Wang J., Hu J., Cui J., Bai X., Du Y., Miyaguchi Y., et al. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysates in spontaneously hypertensive rats. Food Chemistry 111 (2008) 302-308