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Volumn 126, Issue 12, 1996, Pages 3063-3068

Antihypertensive peptides are present in aorta after oral administration of sour milk containing these peptides to spontaneously hypertensive rats

Author keywords

angiotensin I converting enzyme; antihypertensive peptide; fermented milk; intestinal absorption; spontaneously hypertensive rats

Indexed keywords

AMINO ACID; CALPIS; DIPEPTIDYL CARBOXYPEPTIDASE; ISOLEUCYLPROLYLPROLINE; UNCLASSIFIED DRUG; VALYLPROLYLPROLINE;

EID: 0030469762     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/126.12.3063     Document Type: Article
Times cited : (262)

References (34)
  • 1
    • 0017632634 scopus 로고
    • Clearance of dipeptide from plasma: Role of kidney and intestine peptide transport hydrolysis
    • Adibi, S. A. (1977) Clearance of dipeptide from plasma: role of kidney and intestine peptide transport hydrolysis. CIBA Found. Symp. 50: 265-285.
    • (1977) CIBA Found. Symp. , vol.50 , pp. 265-285
    • Adibi, S.A.1
  • 2
    • 0023860850 scopus 로고
    • Differential effects of oral trondolapril and enalapril on rat tissue angiotensin-converting enzyme
    • Chevillard, C., Brown, N. L., Mathieu, M., Laliberte, F. & Worcel, M. (1988) Differential effects of oral trondolapril and enalapril on rat tissue angiotensin-converting enzyme. Eur. J. Pharmacol. 147: 23-28.
    • (1988) Eur. J. Pharmacol. , vol.147 , pp. 23-28
    • Chevillard, C.1    Brown, N.L.2    Mathieu, M.3    Laliberte, F.4    Worcel, M.5
  • 3
    • 0020656945 scopus 로고
    • Effect of acute oral administration of Captopril and MK-421 on vascular angiotensin converting enzyme activity in the spontaneously hypertensive rat
    • Cohen, M. L., Wiley, K. S. & Kurz, K. K. (1983) Effect of acute oral administration of Captopril and MK-421 on vascular angiotensin converting enzyme activity in the spontaneously hypertensive rat. Life Sci. 32: 565-569.
    • (1983) Life Sci. , vol.32 , pp. 565-569
    • Cohen, M.L.1    Wiley, K.S.2    Kurz, K.K.3
  • 4
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
    • Cushman, D. W. & Cheung, H. S. (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
  • 5
    • 0016817422 scopus 로고
    • Pulmonary angiotensin-converting enzyme
    • Das, M. & Soffers, R. S. (1975) Pulmonary angiotensin-converting enzyme. J. Biol. Chem. 250: 6762-6768.
    • (1975) J. Biol. Chem. , vol.250 , pp. 6762-6768
    • Das, M.1    Soffers, R.S.2
  • 6
    • 0016608047 scopus 로고
    • Angiotensin I converting enzyme
    • Erdos, E. G. (1975) Angiotensin I converting enzyme. Circ. Res. 36: 247-255.
    • (1975) Circ. Res. , vol.36 , pp. 247-255
    • Erdos, E.G.1
  • 7
    • 0017319492 scopus 로고
    • Iso-renin of extrarenal origin: The tissue angiotensiogenase systems
    • Ganten, D., Schelling, P., Vecsei, P. & Ganten, U. (1976) Iso-renin of extrarenal origin: the tissue angiotensiogenase systems. Am. J. Med. 60: 760-772.
    • (1976) Am. J. Med. , vol.60 , pp. 760-772
    • Ganten, D.1    Schelling, P.2    Vecsei, P.3    Ganten, U.4
  • 9
    • 0021271917 scopus 로고
    • Portal absorption of small peptides in rats under unrestrained conditions
    • Hara, H., Funabiki, R., Iwata, M. & Yamazaki, K. (1984) Portal absorption of small peptides in rats under unrestrained conditions. J. Nutr. 114: 1122-1129.
    • (1984) J. Nutr. , vol.114 , pp. 1122-1129
    • Hara, H.1    Funabiki, R.2    Iwata, M.3    Yamazaki, K.4
  • 11
    • 0019987626 scopus 로고
    • Pharmacokinetic properties of captopril after acute and chronic administration to hypertensive subjects
    • Jarrott, B., Drummer, O., Hooper, R., Anderson, A. I., Miach, P. J. & Louis, W. J. (1982) Pharmacokinetic properties of captopril after acute and chronic administration to hypertensive subjects. Am. J. Cardiol. 49: 1547-1549.
    • (1982) Am. J. Cardiol. , vol.49 , pp. 1547-1549
    • Jarrott, B.1    Drummer, O.2    Hooper, R.3    Anderson, A.I.4    Miach, P.J.5    Louis, W.J.6
  • 12
    • 0015350951 scopus 로고
    • Peptide hydrolyses in the brush border and soluble fractions of small intestinal mucosa of rat and man
    • Kim, S. Y., Bertwhistle, W. & Kim, Y. W. (1972) Peptide hydrolyses in the brush border and soluble fractions of small intestinal mucosa of rat and man. J. Clin. Invest. 51: 1419-1430.
    • (1972) J. Clin. Invest. , vol.51 , pp. 1419-1430
    • Kim, S.Y.1    Bertwhistle, W.2    Kim, Y.W.3
  • 15
    • 0000798388 scopus 로고
    • Angiotensin I-converting enzyme activities of synthetic peptides related to the tandem repeated sequence of a maize endosperm protein
    • Maruyama, S., Miyoshi, S., Kaneko, T. & Tanaka, H. (1989) Angiotensin I-converting enzyme activities of synthetic peptides related to the tandem repeated sequence of a maize endosperm protein. Agric. Biol. Chem. 53: 1077-1081.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 1077-1081
    • Maruyama, S.1    Miyoshi, S.2    Kaneko, T.3    Tanaka, H.4
  • 16
    • 0021888747 scopus 로고
    • Angiotensin-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and ileum of rats
    • Maruyama, S., Nakagomi, K., Tomizuka, N. & Suzuki, H. (1985) Angiotensin-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and ileum of rats. Agric. Biol. Chem. 49: 1405-1409.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 1405-1409
    • Maruyama, S.1    Nakagomi, K.2    Tomizuka, N.3    Suzuki, H.4
  • 17
    • 0027619613 scopus 로고
    • Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle
    • Matsui, T., Matsufuji, H., Seki, E., Osajima, K., Nakashima, M. & Osajima, Y. (1993) Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle. Biosci. Biotech. Biochem. 57: 922-925.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 922-925
    • Matsui, T.1    Matsufuji, H.2    Seki, E.3    Osajima, K.4    Nakashima, M.5    Osajima, Y.6
  • 19
    • 0021338073 scopus 로고
    • Vascular angiotensin-converting enzyme activity in man and other species
    • Lond.
    • Miyazaki, M., Okunishi, H., Nishimura, K. & Toda, N. (1984) Vascular angiotensin-converting enzyme activity in man and other species. Clin. Sci. (Lond.) 66: 39-45.
    • (1984) Clin. Sci. , vol.66 , pp. 39-45
    • Miyazaki, M.1    Okunishi, H.2    Nishimura, K.3    Toda, N.4
  • 20
    • 0025243440 scopus 로고
    • Specificity and pH dependence for acylproline cleavage by prolidase
    • Mock, L. W., Green, P. C. & Boyer, K. D. (1990) Specificity and pH dependence for acylproline cleavage by prolidase. J. Biol. Chem. 265: 19600-19605.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19600-19605
    • Mock, L.W.1    Green, P.C.2    Boyer, K.D.3
  • 21
    • 0030093369 scopus 로고    scopus 로고
    • Decrease of tissue angiotensin I-converting enzyme activity upon feeding sour milk spontaneously to hypertensive rats
    • Nakamura, Y., Masuda, O. & Takano, T. (1996) Decrease of tissue angiotensin I-converting enzyme activity upon feeding sour milk spontaneously to hypertensive rats. Biosci. Biotech. Biochem. 60: 488-489.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 488-489
    • Nakamura, Y.1    Masuda, O.2    Takano, T.3
  • 22
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk
    • Nakamura, Y., Yamamoto, N., Sakai, K., Okubo, A., Yamazaki, S. & Takano, T. (1995a) Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk. J. Dairy Sci. 78: 777-783.
    • (1995) J. Dairy Sci. , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 23
    • 0029319296 scopus 로고
    • Antihypertensive effects of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme
    • Nakamura, Y., Yamamoto, N., Sakai, K. & Takano, T. (1995b) Antihypertensive effects of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. J. Dairy Sci. 78: 253-257.
    • (1995) J. Dairy Sci. , vol.78 , pp. 253-257
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Takano, T.4
  • 24
    • 0025936891 scopus 로고
    • Pathogenetic role of vascular angiotensin-converting enzyme in the spontaneously hypertensive rat
    • Okunishi, H., Kawamoto, T., Kurobe, Y., Oka, Y., Ishi, K., Tanaka, T. & Miyazaki, M. (1991) Pathogenetic role of vascular angiotensin-converting enzyme in the spontaneously hypertensive rat. Chin. Exp. Pharmacol. 18: 649-659.
    • (1991) Chin. Exp. Pharmacol. , vol.18 , pp. 649-659
    • Okunishi, H.1    Kawamoto, T.2    Kurobe, Y.3    Oka, Y.4    Ishi, K.5    Tanaka, T.6    Miyazaki, M.7
  • 25
    • 0020072975 scopus 로고
    • Renin synthesis by canine aortic smooth muscle cells in culture
    • Re, R., Fallon, J. T., Drau, U., Quay, S. C. & Haber, E. (1982) Renin synthesis by canine aortic smooth muscle cells in culture. Life Sci. 30: 99-106.
    • (1982) Life Sci. , vol.30 , pp. 99-106
    • Re, R.1    Fallon, J.T.2    Drau, U.3    Quay, S.C.4    Haber, E.5
  • 27
    • 0038163054 scopus 로고
    • The preparation and function of the angiotensin-converting enzyme
    • Skeggs, L. T., Kahn, J. K. & Shumway, N. P. (1956) The preparation and function of the angiotensin-converting enzyme. J. Exp. Med. 103: 295-299.
    • (1956) J. Exp. Med. , vol.103 , pp. 295-299
    • Skeggs, L.T.1    Kahn, J.K.2    Shumway, N.P.3
  • 29
    • 0021178758 scopus 로고
    • Is tissue converting enzyme inhibition a determinant of the antihypertensive efficacy of converting enzyme inhibitor? Studies with the two different compounds, Hoe498 and MK421
    • Unger, T. H., Ganten, D., Lang, R. E. & Schölkens, B. (1984) Is tissue converting enzyme inhibition a determinant of the antihypertensive efficacy of converting enzyme inhibitor? Studies with the two different compounds, Hoe498 and MK421. J. Cardiovasc. Pharmacol. 6: 872-880.
    • (1984) J. Cardiovasc. Pharmacol. , vol.6 , pp. 872-880
    • Unger, T.H.1    Ganten, D.2    Lang, R.E.3    Schölkens, B.4
  • 30
    • 0021956044 scopus 로고
    • Persistent tissue converting enzyme inhibition following chronic treatment with Hoe498 and MK421 in spontaneously hypertensive rats
    • Unger, T. H., Ganten, D., Lang, R. E. & Schölkens, B. (1985) Persistent tissue converting enzyme inhibition following chronic treatment with Hoe498 and MK421 in spontaneously hypertensive rats. J. Cardiovasc. Pharmacol. 7: 36-41.
    • (1985) J. Cardiovasc. Pharmacol. , vol.7 , pp. 36-41
    • Unger, T.H.1    Ganten, D.2    Lang, R.E.3    Schölkens, B.4
  • 31
    • 0019515656 scopus 로고
    • Brain converting enzyme inhibition: A possible mechanism for the antihypertensive action of Captopril in spontaneously hypertensive rats
    • Unger, T. H., Kaufmann-Bühler, Schölkens, B. & Ganten, D. (1981) Brain converting enzyme inhibition: a possible mechanism for the antihypertensive action of Captopril in spontaneously hypertensive rats. Eur. J. Pharmacol. 70: 467-478.
    • (1981) Eur. J. Pharmacol. , vol.70 , pp. 467-478
    • Unger, T.H.1    Kaufmann-Bühler2    Schölkens, B.3    Ganten, D.4
  • 32
    • 0020035149 scopus 로고
    • The effects of Captopril on rat aortic angiotensin-converting enzyme
    • Velletri, P. & Bean, B. L. (1982) The effects of Captopril on rat aortic angiotensin-converting enzyme. J. Cardiovasc. Pharmacol. 4: 315-325.
    • (1982) J. Cardiovasc. Pharmacol. , vol.4 , pp. 315-325
    • Velletri, P.1    Bean, B.L.2
  • 33
    • 0026936217 scopus 로고
    • Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito
    • Yokokawa, K., Chiba, H. & Yoshikawa, M. (1992) Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotech. Biochem. 56: 1541-1545.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 1541-1545
    • Yokokawa, K.1    Chiba, H.2    Yoshikawa, M.3
  • 34
    • 0017893194 scopus 로고
    • Post-proline cleaving enzyme and post-proline dipeptidyl aminopeptidase comparison of two peptidases with high specificity for proline residues
    • Yoshimoto, T., Fischl, M., Orlowski, R. C. & Walter, R. (1978) Post-proline cleaving enzyme and post-proline dipeptidyl aminopeptidase comparison of two peptidases with high specificity for proline residues. J. Biol. Chem. 253: 3708-3716.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3708-3716
    • Yoshimoto, T.1    Fischl, M.2    Orlowski, R.C.3    Walter, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.