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Volumn 67, Issue 1, 2012, Pages 1-9

Multifunctional Cationic Peptide Fractions from Flaxseed Protein Hydrolysates

Author keywords

Angiotensin converting enzyme; Calmodulin dependent phosphodiesterase; Enzyme inhibition kinetics; Renin: Multifunctional peptides: Flaxseed proteins

Indexed keywords

CALMODULIN; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; PEPTIDE; PHOSPHODIESTERASE INHIBITOR; PROTEIN HYDROLYSATE; RENIN; SUBTILISIN; VEGETABLE PROTEIN;

EID: 84856784002     PISSN: 09219668     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11130-012-0275-3     Document Type: Article
Times cited : (47)

References (37)
  • 1
    • 76449101386 scopus 로고    scopus 로고
    • Changes in arterial blood pressure of a soluble cocoa fiber product on spontaneously hypertensive rats
    • Sanchez D, Quinones M, Moulay L, Muguerza B, Miguel M, Aleixandre A (2010) Changes in arterial blood pressure of a soluble cocoa fiber product on spontaneously hypertensive rats. J Agric Food Chem 58: 417-422.
    • (2010) J Agric Food Chem , vol.58 , pp. 417-422
    • Sanchez, D.1    Quinones, M.2    Moulay, L.3    Muguerza, B.4    Miguel, M.5    Aleixandre, A.6
  • 2
    • 38349128448 scopus 로고    scopus 로고
    • Renin inhibition in hypertension
    • Gradman AH, Kad R (2008) Renin inhibition in hypertension. J Am Coll Cardiol 51: 519-528.
    • (2008) J Am Coll Cardiol , vol.51 , pp. 519-528
    • Gradman, A.H.1    Kad, R.2
  • 3
    • 0029745055 scopus 로고    scopus 로고
    • Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells
    • Jiang X, Li J, Paskind M, Epstein PM (1996) Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells. Proc Natl Acad Sci USA 93: 11236-11241.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11236-11241
    • Jiang, X.1    Li, J.2    Paskind, M.3    Epstein, P.M.4
  • 5
    • 0024284168 scopus 로고
    • The renin-angiotensin system and treatment of heart failure
    • Fouad-Tarazi F, Bumpus M, Khosla M, Healy B (1988) The renin-angiotensin system and treatment of heart failure. Am J Med 84(suppl 3A): 83-86.
    • (1988) Am J Med , vol.84 , Issue.SUPPL. 3A , pp. 83-86
    • Fouad-Tarazi, F.1    Bumpus, M.2    Khosla, M.3    Healy, B.4
  • 6
    • 0017413556 scopus 로고    scopus 로고
    • Renin-angiotensin system: biochemistry and mechanisms of action
    • Peach MJ (1997) Renin-angiotensin system: Biochemistry and mechanisms of action. Physiol Rev 57: 313-370.
    • (1997) Physiol Rev , vol.57 , pp. 313-370
    • Peach, M.J.1
  • 7
    • 0014957830 scopus 로고
    • A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin
    • Yang HYT, Erdös EG, Levin Y (1970) A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim Biophys Acta 214: 374-376.
    • (1970) Biochim Biophys Acta , vol.214 , pp. 374-376
    • Yang, H.Y.T.1    Erdös, E.G.2    Levin, Y.3
  • 8
    • 33748686575 scopus 로고    scopus 로고
    • Nucleotide phosphodiesterase: molecular regulation to clinical use
    • Bender AT, Beavo JA (2006) Nucleotide phosphodiesterase: Molecular regulation to clinical use. Pharmacol Rev 58: 488-520.
    • (2006) Pharmacol Rev , vol.58 , pp. 488-520
    • Bender, A.T.1    Beavo, J.A.2
  • 9
    • 0032506166 scopus 로고    scopus 로고
    • Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms
    • Cho MJ, Vaghy PL, Kondo R, Lee SH, Davis JP, Rehl R, Heo WD, Johnson JD (1998) Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms. Biochemistry 37: 15593-15597.
    • (1998) Biochemistry , vol.37 , pp. 15593-15597
    • Cho, M.J.1    Vaghy, P.L.2    Kondo, R.3    Lee, S.H.4    Davis, J.P.5    Rehl, R.6
  • 10
    • 0042859823 scopus 로고    scopus 로고
    • Cyclic GMP phosphodiesterases and regulation of smooth muscle function
    • Rybalkin SD, Yan C, Bornfeldt KE, Beavo JA (2003) Cyclic GMP phosphodiesterases and regulation of smooth muscle function. Circ Res 93: 280-291.
    • (2003) Circ Res , vol.93 , pp. 280-291
    • Rybalkin, S.D.1    Yan, C.2    Bornfeldt, K.E.3    Beavo, J.A.4
  • 11
    • 33645743686 scopus 로고    scopus 로고
    • 2+/calmodulin-stimulated phosphodiesterase 1A in vascular smooth muscle cell growth and survival
    • 2+/calmodulin-stimulated phosphodiesterase 1A in vascular smooth muscle cell growth and survival. Circ Res 98: 777-784.
    • (2006) Circ Res , vol.98 , pp. 777-784
    • Nagel, D.J.1    Aizawa, T.2    Jeon, K.I.3    Liu, W.4    Mohan, A.5    Wei, H.6
  • 12
    • 0035818615 scopus 로고    scopus 로고
    • Upregulation of phosphodiesterase 1A1 expression is associated with the development of nitrate tolerance
    • Kim D, Rybalkin SD, Pi X, Wang Y, Zhang C, Munzel T, Beavo JA, Berk BC, Yan C (2001) Upregulation of phosphodiesterase 1A1 expression is associated with the development of nitrate tolerance. Circulation 104: 2338-2343.
    • (2001) Circulation , vol.104 , pp. 2338-2343
    • Kim, D.1    Rybalkin, S.D.2    Pi, X.3    Wang, Y.4    Zhang, C.5    Munzel, T.6    Beavo, J.A.7    Berk, B.C.8    Yan, C.9
  • 13
    • 34247586182 scopus 로고    scopus 로고
    • Phosphodiesterase 1 upregulation in pulmonary arterial hypertension. Target for reverse-remodeling therapy
    • Schermuly RT, Pullamsetti SS, Kwapiszewska G, Dumitrascu R, Tian X, Weissmann N, Ghofrani HA, Kaulen C, Dunkern T, Schudt C, Voswinckel R, Zhou J, Samidurai A, Klepetko W, Paddenberg R, Kummer W, Seeger W, Grimminger F (2007) Phosphodiesterase 1 upregulation in pulmonary arterial hypertension. Target for reverse-remodeling therapy. Circulation 115: 2331-2339.
    • (2007) Circulation , vol.115 , pp. 2331-2339
    • Schermuly, R.T.1    Pullamsetti, S.S.2    Kwapiszewska, G.3    Dumitrascu, R.4    Tian, X.5    Weissmann, N.6
  • 14
    • 12244313740 scopus 로고    scopus 로고
    • Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation
    • Bender AT, Ostenson CL, Wang EH, Beavo JA (2005) Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation. Proc Natl Acad Sci USA 102: 497-502.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 497-502
    • Bender, A.T.1    Ostenson, C.L.2    Wang, E.H.3    Beavo, J.A.4
  • 15
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices
    • O'Neil KT, DeGrado WF (1990) How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helices. Trends Biochem Sci 15: 59-64.
    • (1990) Trends Biochem Sci , vol.15 , pp. 59-64
    • O'Neil, K.T.1    Degrado, W.F.2
  • 16
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: Production, processing and potential health benefits
    • Udenigwe CC, Aluko RE (2011) Food protein-derived bioactive peptides: Production, processing and potential health benefits. J Food Sci 77: R11-R24.
    • (2011) J Food Sci , vol.77
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 17
    • 0036980820 scopus 로고    scopus 로고
    • Antihypertensive medication and quality of life- silent treatment of a silent killer?
    • Bremmer AD (2003) Antihypertensive medication and quality of life- silent treatment of a silent killer?Cardiovasc Drugs Ther 16: 353-364.
    • (2003) Cardiovasc Drugs Ther , vol.16 , pp. 353-364
    • Bremmer, A.D.1
  • 18
    • 0034814575 scopus 로고    scopus 로고
    • Effects of an ace-inhibitory agent, katsuobushi oligopeptide, in spontaneously hypertensive rat and in borderline and mildly hypertensive subjects
    • Fujita H, Yamagani T, Ohshima K (2001) Effects of an ace-inhibitory agent, katsuobushi oligopeptide, in spontaneously hypertensive rat and in borderline and mildly hypertensive subjects. Nutr Res 21: 1149-1158.
    • (2001) Nutr Res , vol.21 , pp. 1149-1158
    • Fujita, H.1    Yamagani, T.2    Ohshima, K.3
  • 19
    • 77950123764 scopus 로고    scopus 로고
    • The impact of lactotripeptides on blood pressure response in stage 1 and stage 2 hypertensives
    • Germino FW, Neutel J, Nonaka M, Hendler SS (2010) The impact of lactotripeptides on blood pressure response in stage 1 and stage 2 hypertensives. J Clin Hypertens 12: 153-159.
    • (2010) J Clin Hypertens , vol.12 , pp. 153-159
    • Germino, F.W.1    Neutel, J.2    Nonaka, M.3    Hendler, S.S.4
  • 20
    • 78049479104 scopus 로고    scopus 로고
    • IPP-rich milk protein hydrolysate lowers blood pressure in subjects with stage 1 hypertension, a randomized controlled trial
    • Boelsma E, Kloek J (2010) IPP-rich milk protein hydrolysate lowers blood pressure in subjects with stage 1 hypertension, a randomized controlled trial. Nutr J 9: 52.
    • (2010) Nutr J , vol.9 , pp. 52
    • Boelsma, E.1    Kloek, J.2
  • 21
    • 57249089073 scopus 로고    scopus 로고
    • An in vitro investigation of selected biological activities of hydrolyzed flaxseed (Linum usitatissimum L.) proteins
    • Marambe PWMLHK, Shand PJ, Wanasundara JPD (2008) An in vitro investigation of selected biological activities of hydrolyzed flaxseed (Linum usitatissimum L.) proteins. J Am Oil Chem Soc 85: 1155-1164.
    • (2008) J Am Oil Chem Soc , vol.85 , pp. 1155-1164
    • Marambe, P.W.M.L.H.K.1    Shand, P.J.2    Wanasundara, J.P.D.3
  • 22
    • 80052581797 scopus 로고    scopus 로고
    • Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion
    • Marambe HK, Shand PJ, Wanasundara JPD (2011) Release of angiotensin I-converting enzyme inhibitory peptides from flaxseed (Linum usitatissimum L.) protein under simulated gastrointestinal digestion. J Agric Food Chem 59: 9596-9604.
    • (2011) J Agric Food Chem , vol.59 , pp. 9596-9604
    • Marambe, H.K.1    Shand, P.J.2    Wanasundara, J.P.D.3
  • 23
    • 64549083283 scopus 로고    scopus 로고
    • Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions
    • Udenigwe CC, Lin Y-S, Hou W-C, Aluko RE (2009) Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions. J Funct Foods 1: 199-207.
    • (2009) J Funct Foods , vol.1 , pp. 199-207
    • Udenigwe, C.C.1    Lin, Y.-S.2    Hou, W.-C.3    Aluko, R.E.4
  • 24
    • 64549113397 scopus 로고    scopus 로고
    • Flaxseed protein-derived peptide fractions: antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages
    • Udenigwe CC, Lu Y-L, Han C-H, Hou W-C, Aluko RE (2009) Flaxseed protein-derived peptide fractions: Antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages. Food Chem 116: 277-284.
    • (2009) Food Chem , vol.116 , pp. 277-284
    • Udenigwe, C.C.1    Lu, Y.-L.2    Han, C.-H.3    Hou, W.-C.4    Aluko, R.E.5
  • 25
    • 77951275186 scopus 로고    scopus 로고
    • Antioxidant and angiotensin converting enzyme-inhibitory properties of a flaxseed protein-derived high Fischer ratio peptide mixture
    • Udenigwe CC, Aluko RE (2010) Antioxidant and angiotensin converting enzyme-inhibitory properties of a flaxseed protein-derived high Fischer ratio peptide mixture. J Agric Food Chem 58: 4762-4768.
    • (2010) J Agric Food Chem , vol.58 , pp. 4762-4768
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 27
    • 83055188018 scopus 로고    scopus 로고
    • Kinetics of the inhibition of renin and angiotensin-I converting enzyme by polar and non-polar polyphenolic extracts of Vernonia amygdalina and Gongronema latifolium leaves
    • Ajibola CF, Eleyinmi AF, Aluko RE (2011) Kinetics of the inhibition of renin and angiotensin-I converting enzyme by polar and non-polar polyphenolic extracts of Vernonia amygdalina and Gongronema latifolium leaves. Plant Foods Hum Nutr 66: 320-327.
    • (2011) Plant Foods Hum Nutr , vol.66 , pp. 320-327
    • Ajibola, C.F.1    Eleyinmi, A.F.2    Aluko, R.E.3
  • 28
    • 33750350429 scopus 로고    scopus 로고
    • Effect of cationic flaxseed protein hydrolysate fractions on the in vitro structure and activity of calmodulin-dependent endothelial nitric oxide synthase
    • Omoni AO, Aluko RE (2006) Effect of cationic flaxseed protein hydrolysate fractions on the in vitro structure and activity of calmodulin-dependent endothelial nitric oxide synthase. Mol Nutr Food Res 50: 958-966.
    • (2006) Mol Nutr Food Res , vol.50 , pp. 958-966
    • Omoni, A.O.1    Aluko, R.E.2
  • 29
    • 33744460253 scopus 로고    scopus 로고
    • Mechanism of the inhibition of calmodulin-dependent neuronal nitric oxide synthase by flaxseed protein hydrolysates
    • Omoni AO, Aluko RE (2006) Mechanism of the inhibition of calmodulin-dependent neuronal nitric oxide synthase by flaxseed protein hydrolysates. J Am Oil Chem Soc 83: 335-340.
    • (2006) J Am Oil Chem Soc , vol.83 , pp. 335-340
    • Omoni, A.O.1    Aluko, R.E.2
  • 30
    • 60049093575 scopus 로고    scopus 로고
    • Concentration and selective separation of bioactive peptides from alfalfa white protein hydrolysate by electrodialysis with ultrafiltration membranes
    • Firdaous L, Dhulster P, Amiot J, Gaudreau A, Lecouturier D, Kapel R, Lutin F, Vézina L-P, Bazinet L (2009) Concentration and selective separation of bioactive peptides from alfalfa white protein hydrolysate by electrodialysis with ultrafiltration membranes. J Membr Sci 329: 60-67.
    • (2009) J Membr Sci , vol.329 , pp. 60-67
    • Firdaous, L.1    Dhulster, P.2    Amiot, J.3    Gaudreau, A.4    Lecouturier, D.5    Kapel, R.6    Lutin, F.7    Vézina, L.-P.8    Bazinet, L.9
  • 31
    • 76349107121 scopus 로고    scopus 로고
    • Multifunctional peptides from egg white lysozyme
    • You SJ, Udenigwe CC, Aluko RE, Wu J (2010) Multifunctional peptides from egg white lysozyme. Food Res Int 43: 848-855.
    • (2010) Food Res Int , vol.43 , pp. 848-855
    • You, S.J.1    Udenigwe, C.C.2    Aluko, R.E.3    Wu, J.4
  • 32
    • 27444437848 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship modelling peptides and proteins as a tool in food science
    • Pripp AH, Isaksson T, Stepaniak L, Sørhaug T, Ardö Y (2004) Quantitative structure-activity relationship modelling peptides and proteins as a tool in food science. Trends Food Sci Technol 16: 484-494.
    • (2004) Trends Food Sci Technol , vol.16 , pp. 484-494
    • Pripp, A.H.1    Isaksson, T.2    Stepaniak, L.3    Sørhaug, T.4    Ardö, Y.5
  • 33
    • 0029395013 scopus 로고
    • Calmodulin-binding peptides isolated from α-casein peptone
    • Kizawa K, Naganuma K, Murakami U (1995) Calmodulin-binding peptides isolated from α-casein peptone. J Dairy Res 62: 587-592.
    • (1995) J Dairy Res , vol.62 , pp. 587-592
    • Kizawa, K.1    Naganuma, K.2    Murakami, U.3
  • 34
    • 0020635354 scopus 로고
    • Inhibition of calmodulin activity by insect venom peptides
    • Barnette MS, Daly R, Weiss B (1983) Inhibition of calmodulin activity by insect venom peptides. Biochem Pharmacol 32: 2929-2933.
    • (1983) Biochem Pharmacol , vol.32 , pp. 2929-2933
    • Barnette, M.S.1    Daly, R.2    Weiss, B.3
  • 35
    • 26844440677 scopus 로고    scopus 로고
    • Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides
    • Li H, Aluko RE (2005) Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides. J Nutr Biochem 16: 656-662.
    • (2005) J Nutr Biochem , vol.16 , pp. 656-662
    • Li, H.1    Aluko, R.E.2
  • 36
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
    • Cushman DW, Cheung HS (1971) Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharmacol 20: 1637-1648.
    • (1971) Biochem Pharmacol , vol.20 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2


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