메뉴 건너뛰기




Volumn 119, Issue 2, 1996, Pages 365-373

Role of bradykinin receptors in the renal effects of inhibition of angiotensin converting enzyme and endopeptidases 24.11 and 24.15 in conscious rabbits

Author keywords

Angiotensin converting enzyme; Bradykinin; Conscious rabbit; Hoe 140; Metalloendopeptidase 24.11; Metalloendopeptidase 24.15; Renal function

Indexed keywords

4 AMINOBENZOIC ACID DERIVATIVE; BRADYKININ; BRADYKININ B2 RECEPTOR; CAPTOPRIL; DIPEPTIDYL CARBOXYPEPTIDASE; ICATIBANT; MEMBRANE METALLOENDOPEPTIDASE; N (1 CARBOXY 3 PHENYLPROPYL)ALANYLALANYLTYROSYL 4 AMINOBENZOATE; N (1 CARBOXY 3 PHENYLPROPYL)PHENYLALANYLISOSERINE; PROTEINASE; SODIUM ION; UNCLASSIFIED DRUG;

EID: 0029793682     PISSN: 00071188     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1476-5381.1996.tb15995.x     Document Type: Article
Times cited : (15)

References (46)
  • 2
  • 4
    • 0028224966 scopus 로고
    • Role of endopeptidase 3.4.24.16 in the catabolism of neurotensin, in vivo, in the vascularly perfused dog ileum
    • BARELLI, H., FOX-THRELKELD, J.E.T., DIVE, V., DANIEL, E.E., VINCENT, J.P. & CHECLER, F. (1994). Role of endopeptidase 3.4.24.16 in the catabolism of neurotensin, in vivo, in the vascularly perfused dog ileum. Br. J. Pharmacol., 112, 127-132.
    • (1994) Br. J. Pharmacol. , vol.112 , pp. 127-132
    • Barelli, H.1    Fox-Threlkeld, J.E.T.2    Dive, V.3    Daniel, E.E.4    Vincent, J.P.5    Checler, F.6
  • 6
    • 0027452188 scopus 로고
    • Evidence that enzymatic conversion of N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate, a specific inhibitor of endopeptidase 24.15, to N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala is necessary for inhibition of angiotensin converting enzyme
    • CARDOZO, C. & ORLOWSKI, M. (1993). Evidence that enzymatic conversion of N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate, a specific inhibitor of endopeptidase 24.15, to N-[1(R,S)-carboxy-3-phenylpropyl]-Ala-Ala is necessary for inhibition of angiotensin converting enzyme. Peptides, 14, 1259-1262.
    • (1993) Peptides , vol.14 , pp. 1259-1262
    • Cardozo, C.1    Orlowski, M.2
  • 7
    • 0026451940 scopus 로고
    • Inhibition of angiotensin converting enzyme by the metalloendopeptidase 3.4.24.15 inhibitor c-phenylpropyl-alanyl-alanyl-phenylalanyl-p-aminobenzoate
    • CHAPPELL, M.C., WELCHES, W.R., BROSNIHAN, K.B. & FERRARI, C.M. (1992). Inhibition of angiotensin converting enzyme by the metalloendopeptidase 3.4.24.15 inhibitor c-phenylpropyl-alanyl-alanyl-phenylalanyl-p-aminobenzoate. Peptides, 13, 943-946.
    • (1992) Peptides , vol.13 , pp. 943-946
    • Chappell, M.C.1    Welches, W.R.2    Brosnihan, K.B.3    Ferrari, C.M.4
  • 8
    • 0028037677 scopus 로고
    • Comparison of renal hemodynamic effect of ramiprilat to captopril; possible role of kinins
    • CHEN, K. & ZIMMERMAN, B.G. (1994). Comparison of renal hemodynamic effect of ramiprilat to captopril; possible role of kinins. J. Pharmacol. Exp. Ther., 270, 491-497.
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 491-497
    • Chen, K.1    Zimmerman, B.G.2
  • 9
    • 0021285834 scopus 로고
    • Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain
    • CHU, T.G. & ORLOWSKI, M. (1984). Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain. Biochemistry, 23, 3598-3603.
    • (1984) Biochemistry , vol.23 , pp. 3598-3603
    • Chu, T.G.1    Orlowski, M.2
  • 10
    • 0021860568 scopus 로고
    • Soluble metalloendopeptidase from rat brain: Action on enkephalin-containing peptides and other bioactive peptides
    • CHU, T.G. & ORLOWSKI, M. (1985). Soluble metalloendopeptidase from rat brain: action on enkephalin-containing peptides and other bioactive peptides. Endocrinology, 116, 1418-1425.
    • (1985) Endocrinology , vol.116 , pp. 1418-1425
    • Chu, T.G.1    Orlowski, M.2
  • 12
    • 0027933436 scopus 로고
    • Interactions of blockade of nitric oxide synthase and angiotensin-converting enzyme on renal function in conscious rabbits
    • EVANS, R.G., RANKIN, A.J. & ANDERSON, W.P. (1994). Interactions of blockade of nitric oxide synthase and angiotensin-converting enzyme on renal function in conscious rabbits. J. Cardiovasc. Pharmacol., 24, 542-551.
    • (1994) J. Cardiovasc. Pharmacol. , vol.24 , pp. 542-551
    • Evans, R.G.1    Rankin, A.J.2    Anderson, W.P.3
  • 15
    • 0028998269 scopus 로고
    • Dual inhibition of angiotensin-converting enzyme and neutral endopeptidase in rats with hypertension
    • FRENCH, J.F., ANDERSON, B.A., DOWNS, T.R. & DAGE, R.C. (1995). Dual inhibition of angiotensin-converting enzyme and neutral endopeptidase in rats with hypertension. J. Cardiovasc. Pharmacol., 26, 107-113.
    • (1995) J. Cardiovasc. Pharmacol. , vol.26 , pp. 107-113
    • French, J.F.1    Anderson, B.A.2    Downs, T.R.3    Dage, R.C.4
  • 16
    • 0027223728 scopus 로고
    • Reduction of myocardial infarct size in rabbits by ramiprilat: Reversal by the bradykinin antagonist Hoe 140
    • HARTMAN, J.C., WALL, T.M., HULLINGER, T.G. & SHEBUSKI, R.J. (1993). Reduction of myocardial infarct size in rabbits by ramiprilat: reversal by the bradykinin antagonist Hoe 140. J. Cardiovasc, Pharmacol., 21, 996-1003.
    • (1993) J. Cardiovasc, Pharmacol. , vol.21 , pp. 996-1003
    • Hartman, J.C.1    Wall, T.M.2    Hullinger, T.G.3    Shebuski, R.J.4
  • 17
    • 0027226183 scopus 로고
    • Bradykinin causes selective efferent arteriolar dilation during angiotensin I converting enzyme inhibition
    • KON, V., FOGO, A. & ICHIKAWA, I. (1993). Bradykinin causes selective efferent arteriolar dilation during angiotensin I converting enzyme inhibition. Kidney Int., 44, 545-550.
    • (1993) Kidney Int. , vol.44 , pp. 545-550
    • Kon, V.1    Fogo, A.2    Ichikawa, I.3
  • 18
    • 0024431281 scopus 로고
    • Evaluation of lithium clearance as a marker of proximal tubule sodium handling
    • KOOMANS, H.A., BOER, W.H. & DORHOUT MEES, E.J. (1989). Evaluation of lithium clearance as a marker of proximal tubule sodium handling. Kidney Int., 36, 2-12.
    • (1989) Kidney Int. , vol.36 , pp. 2-12
    • Koomans, H.A.1    Boer, W.H.2    Dorhout Mees, E.J.3
  • 19
    • 0025287626 scopus 로고
    • Inhibition of endopeptidase 24.15 greatly increases the release of luteinizing hormone and follicle stimulating hormone in response to luteinizing hormone/ releasing hormone
    • LASDUN, A. & ORLOWSKI, M. (1990). Inhibition of endopeptidase 24.15 greatly increases the release of luteinizing hormone and follicle stimulating hormone in response to luteinizing hormone/ releasing hormone. J. Pharmacol. Exp. Ther., 253, 1265-1271.
    • (1990) J. Pharmacol. Exp. Ther. , vol.253 , pp. 1265-1271
    • Lasdun, A.1    Orlowski, M.2
  • 20
    • 0024355965 scopus 로고
    • Inhibition of endopeptidase 24.15 slows the in vivo degradation of luteinizing hormone-releasing hormone
    • LASDUN, A., REZNIK, S., MOLINEAUX, C.J. & ORLOWSKI, M. (1989). Inhibition of endopeptidase 24.15 slows the in vivo degradation of luteinizing hormone-releasing hormone. J. Pharmacol. Exp. Ther., 251, 439-447.
    • (1989) J. Pharmacol. Exp. Ther. , vol.251 , pp. 439-447
    • Lasdun, A.1    Reznik, S.2    Molineaux, C.J.3    Orlowski, M.4
  • 21
    • 0028272080 scopus 로고
    • Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts
    • LEW, R.A., TETAZ, T.J., GLUCKSMAN, M.J., ROBERTS, J.L. & SMITH, A.I. (1994). Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts. J. Biol. Chem., 269, 12626-12632.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12626-12632
    • Lew, R.A.1    Tetaz, T.J.2    Glucksman, M.J.3    Roberts, J.L.4    Smith, A.I.5
  • 22
  • 23
    • 0025861868 scopus 로고
    • On making multiple comparisons in clinical and experimental pharmacology and physiology
    • LUDBROOK, J. (1991). On making multiple comparisons in clinical and experimental pharmacology and physiology. Clin. Exp. Pharmacol. Physiol., 18, 379-392.
    • (1991) Clin. Exp. Pharmacol. Physiol. , vol.18 , pp. 379-392
    • Ludbrook, J.1
  • 24
    • 33746663881 scopus 로고
    • Repeated measurements and multiple comparisons in cardiovascular research
    • LUDBROOK, J. (1994). Repeated measurements and multiple comparisons in cardiovascular research. Cardiovasc. Res., 28, 303-311.
    • (1994) Cardiovasc. Res. , vol.28 , pp. 303-311
    • Ludbrook, J.1
  • 25
    • 0029054967 scopus 로고
    • Approaches to the development of novel antihypertensive drugs: Crucial role of the renal kallikrein-kinin system
    • MAJIMA, M. & KATORI, M. (1995). Approaches to the development of novel antihypertensive drugs: crucial role of the renal kallikrein-kinin system. Trends Pharmacol. Sci., 16, 239-246.
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 239-246
    • Majima, M.1    Katori, M.2
  • 26
    • 0028931280 scopus 로고
    • Natriuretic response to neutral endopeptidase inhibition is blunted by enalapril in healthy men
    • MOTWANI, J.G., LANG, C.C., CRAMB, G. & STRUTHERS, A.D. (1995). Natriuretic response to neutral endopeptidase inhibition is blunted by enalapril in healthy men. Hypertension, 25, 637-642.
    • (1995) Hypertension , vol.25 , pp. 637-642
    • Motwani, J.G.1    Lang, C.C.2    Cramb, G.3    Struthers, A.D.4
  • 27
    • 0020824984 scopus 로고
    • A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides
    • ORLOWSKI, M., MICHAUD, C. & CHU, T.G. (1983). A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur. J. Biochem., 135, 81-88.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 81-88
    • Orlowski, M.1    Michaud, C.2    Chu, T.G.3
  • 28
    • 0023871927 scopus 로고
    • Substrate-related potent inhibitors of brain metallo-endopeptidase
    • ORLOWSKI, M., MICHAUD, C. & MOLINEAUX, C.J. (1988). Substrate-related potent inhibitors of brain metallo-endopeptidase. Biochemistry, 27, 597-602.
    • (1988) Biochemistry , vol.27 , pp. 597-602
    • Orlowski, M.1    Michaud, C.2    Molineaux, C.J.3
  • 29
    • 0024406166 scopus 로고
    • Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides
    • ORLOWSKI, M., REZNIK, S., AYALA, J. & PIEROTTI, A.R. (1989). Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides. Biochem. J., 261, 951-958.
    • (1989) Biochem. J. , vol.261 , pp. 951-958
    • Orlowski, M.1    Reznik, S.2    Ayala, J.3    Pierotti, A.R.4
  • 30
  • 33
    • 0027519535 scopus 로고
    • Systemic hemodynamics, renal function and hormonal levels during inhibition of neutral endopeptidase 3.4.24.11 and angiotensin-converting enzyme in conscious dogs with pacing-induced heart failure
    • SEYMOUR, A.A., ASAAD, M.M., LANOCE, V.M., LANGENBACHER, K.M., FENNELL, S.A. & ROGERS, W.L. (1993). Systemic hemodynamics, renal function and hormonal levels during inhibition of neutral endopeptidase 3.4.24.11 and angiotensin-converting enzyme in conscious dogs with pacing-induced heart failure. J. Pharmacol. Exp. Ther., 266, 872-883.
    • (1993) J. Pharmacol. Exp. Ther. , vol.266 , pp. 872-883
    • Seymour, A.A.1    Asaad, M.M.2    Lanoce, V.M.3    Langenbacher, K.M.4    Fennell, S.A.5    Rogers, W.L.6
  • 34
    • 0028293527 scopus 로고
    • Potentiation of the renal responses to bradykinin by inhibition of neutral endopeptidase 3.4.24.11 and angiotensin-converting enzyme in anaesthetised dogs
    • SEYMOUR, A.A., SHELDON, J.H., SMITH, P.L., ASAAD, M. & ROGERS, W.L. (1994). Potentiation of the renal responses to bradykinin by inhibition of neutral endopeptidase 3.4.24.11 and angiotensin-converting enzyme in anaesthetised dogs. J. Pharmacol. Exp. Ther., 269, 263-270.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 263-270
    • Seymour, A.A.1    Sheldon, J.H.2    Smith, P.L.3    Asaad, M.4    Rogers, W.L.5
  • 35
    • 0001459424 scopus 로고
    • The renal clearance of substituted hippuric acid derivatives and other aromatic acids in dog and man
    • SMITH, H.W., FINKELSTEIN, N., ALIMINOSA, L., CRAWFORD, B. & GRABER, M. (1945). The renal clearance of substituted hippuric acid derivatives and other aromatic acids in dog and man. J. Clin. Invest., 24, 388-404.
    • (1945) J. Clin. Invest. , vol.24 , pp. 388-404
    • Smith, H.W.1    Finkelstein, N.2    Aliminosa, L.3    Crawford, B.4    Graber, M.5
  • 36
    • 0024435563 scopus 로고
    • SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers blood pressure in desoxycorticosterone acetate-sodium hypertensive rats
    • SYBERTZ, E.J., CHIU, P.J.S., VEMULAPALLI, S., PITTS, B., FOSTER, C.J., WATKINS, R.W., BARNETT, A. & HASLANGER, M.F. (1989). SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers blood pressure in desoxycorticosterone acetate-sodium hypertensive rats. J. Pharmacol. Exp. Ther., 250, 624-631.
    • (1989) J. Pharmacol. Exp. Ther. , vol.250 , pp. 624-631
    • Sybertz, E.J.1    Chiu, P.J.S.2    Vemulapalli, S.3    Pitts, B.4    Foster, C.J.5    Watkins, R.W.6    Barnett, A.7    Haslanger, M.F.8
  • 37
    • 0028935197 scopus 로고
    • Role of angiotensin converting enzyme in the vascular effects of an endopeptidase 24.15 inhibitor
    • TELFORD, S.E., SMITH, A.I., LEW, R.A. PERICH, R.B., MADDEN, A.C. & EVANS, R.G. (1995). Role of angiotensin converting enzyme in the vascular effects of an endopeptidase 24.15 inhibitor. Br. J. Pharmacol., 114, 1185-1192.
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 1185-1192
    • Telford, S.E.1    Smith, A.I.2    Lew, R.A.3    Perich, R.B.4    Madden, A.C.5    Evans, R.G.6
  • 38
    • 85035174559 scopus 로고
    • The endopeptidase 24.11 inhibitor SCH 39370 does not prevent conversion of N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate to an angiotensin converting enzyme inhibitor in vivo
    • Abstract
    • TOMODA, F., LEW, R.A., SMITH, A.I. & EVANS, R.G. (1995). The endopeptidase 24.11 inhibitor SCH 39370 does not prevent conversion of N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate to an angiotensin converting enzyme inhibitor in vivo. Proc. Aus. Physiol. Pharmacol. Soc., 26, 75P (Abstract).
    • (1995) Proc. Aus. Physiol. Pharmacol. Soc. , vol.26
    • Tomoda, F.1    Lew, R.A.2    Smith, A.I.3    Evans, R.G.4
  • 39
    • 0028037135 scopus 로고
    • The role of kinins and atrial natriuretic peptide on the renal effects of neutral endopeptidase inhibitor in rats
    • URA, N., SHIMAMOTO, K., KURODA, S., NOMURA, N., IWATA, M., AOYAMA, T. & IIMURA, O. (1994). The role of kinins and atrial natriuretic peptide on the renal effects of neutral endopeptidase inhibitor in rats. Clin. Exp. Hyperten., 16, 799-808.
    • (1994) Clin. Exp. Hyperten. , vol.16 , pp. 799-808
    • Ura, N.1    Shimamoto, K.2    Kuroda, S.3    Nomura, N.4    Iwata, M.5    Aoyama, T.6    Iimura, O.7
  • 40
    • 0028838979 scopus 로고
    • Hypotensive and natriuretic effects of RB 105, a new dual inhibitor of angiotensin converting enzyme and neutral endopeptidase in hypertensive rats
    • VERA, W.O., FOURNIÉ-ZALUSKI, M.-C., PHAM, I., LABOULANDINE, I., ROQUES, B.-P. & MICHEL, J-B. (1995). Hypotensive and natriuretic effects of RB 105, a new dual inhibitor of angiotensin converting enzyme and neutral endopeptidase in hypertensive rats. J. Pharmacol. Exp. Ther., 272, 343-351.
    • (1995) J. Pharmacol. Exp. Ther. , vol.272 , pp. 343-351
    • Vera, W.O.1    Fournié-Zaluski, M.-C.2    Pham, I.3    Laboulandine, I.4    Roques, B.-P.5    Michel, J.-B.6
  • 41
    • 0029119487 scopus 로고
    • Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: Effect on neurotensin degradation in vitro and in vivo
    • VINCENT, B., DIVE, V., YIOTAKIS, A., SMADJA, C., MALDONADO, R., VINCENT, J.-P. & CHECLER, F. (1995). Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: effect on neurotensin degradation in vitro and in vivo. Br. J. Pharmacol., 115, 1053-1063.
    • (1995) Br. J. Pharmacol. , vol.115 , pp. 1053-1063
    • Vincent, B.1    Dive, V.2    Yiotakis, A.3    Smadja, C.4    Maldonado, R.5    Vincent, J.-P.6    Checler, F.7
  • 42
    • 0027359062 scopus 로고
    • Endopeptidase 3.4.24.11 converts N-1-(R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme
    • WILLIAMS, C.H., YAMAMOTO, T., WALSH, D.M. & ALLSOP, D (1993). Endopeptidase 3.4.24.11 converts N-1-(R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme. Biochem. J., 294, 681-684.
    • (1993) Biochem. J. , vol.294 , pp. 681-684
    • Williams, C.H.1    Yamamoto, T.2    Walsh, D.M.3    Allsop, D.4
  • 46
    • 0028152383 scopus 로고
    • Effects of a metalloendopeptidase-24.15 inhibitor on renal hemodynamics and function in rats
    • YANG, X.-P., SAITOH, S., SCICLI, A.G., MASCHA, E., ORLOWSKI, M. & CARRETERO, O.A. (1994). Effects of a metalloendopeptidase-24.15 inhibitor on renal hemodynamics and function in rats. Hypertension, 23 (suppl. 1), I-235-I-239.
    • (1994) Hypertension , vol.23 , Issue.1 SUPPL.
    • Yang, X.-P.1    Saitoh, S.2    Scicli, A.G.3    Mascha, E.4    Orlowski, M.5    Carretero, O.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.