메뉴 건너뛰기




Volumn 118, Issue 5, 1996, Pages 1269-1277

Synthetic inhibitors of endopeptidase EC 3.4.24.15: Potency and stability in vitro and in vivo

Author keywords

Angiotensin; Angiotensin converting enzyme; Bradykinin; Metalloendopeptidase 24.15; Neutral endopeptidase; Pharmacokinetics; Phosphoramidon

Indexed keywords

ANGIOTENSIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; IODINE 125; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE INHIBITOR; N (1 CARBOXY 3 PHENYLPROPYL)PHENYLALANYLISOSERINE; PHOSPHORAMIDON;

EID: 0030018193     PISSN: 00071188     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1476-5381.1996.tb15533.x     Document Type: Article
Times cited : (15)

References (31)
  • 1
    • 8944244233 scopus 로고
    • Canberra, Australia: Australian Government Publishing Service
    • AUSTRALIAN CODE OF PRACTICE FOR THE CARE AND USE OF ANIMALS FOR SCIENTIFIC PURPOSES. (1990). Canberra, Australia: Australian Government Publishing Service.
    • (1990)
  • 3
    • 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
  • 4
    • 0029043724 scopus 로고
    • Endopeptidase inhibition in angiotensin-induced hypertension. Effect of SCH 39370 in sheep
    • CHARLES, C.J., ESPINER, E.A., RICHARDS, A.M. & SYBERTZ, E.J. (1995). Endopeptidase inhibition in angiotensin-induced hypertension. Effect of SCH 39370 in sheep. Hypertension, 26, 89-94.
    • (1995) Hypertension , vol.26 , pp. 89-94
    • Charles, C.J.1    Espiner, E.A.2    Richards, A.M.3    Sybertz, E.J.4
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0025783911 scopus 로고
    • Inhibition of endopeptidase-24.15 decreases blood pressure in normotensive rats
    • GENDEN, E.M. & MOLINEAUX, C.J. (1991). Inhibition of endopeptidase-24.15 decreases blood pressure in normotensive rats. Hypertension, 18, 360-365.
    • (1991) Hypertension , vol.18 , pp. 360-365
    • Genden, E.M.1    Molineaux, C.J.2
  • 8
    • 0023038641 scopus 로고
    • Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin
    • HERSH, L.B. & MORIHARA, K. (1986). Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin. J. Biol. Chem., 261, 6433-6437.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6433-6437
    • Hersh, L.B.1    Morihara, K.2
  • 9
    • 0029155961 scopus 로고
    • Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24.15 using combinatorial chemistry
    • JIRACEK, J., YIOTAKIS, A., VINCENT, B., LECOQ. A., NICOLAOU, A., CHECLER, F. & DIVE, V. (1995). Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24.15 using combinatorial chemistry. J. Biol. Chem., 270, 21701-21706.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21701-21706
    • Jiracek, J.1    Yiotakis, A.2    Vincent, B.3    Lecoq, A.4    Nicolaou, A.5    Checler, F.6    Dive, V.7
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0029048092 scopus 로고
    • Substrate specificity differences between recombinant rat testes endopeptidase EC 3.4.24.15 and the native brain enzyme
    • LEW, R.A., HEY, N.J., TETAZ, T.J., GLUCKSMAN, M.J., ROBERTS, J.L. & SMITH, A.I. (1995). Substrate specificity differences between recombinant rat testes endopeptidase EC 3.4.24.15 and the native brain enzyme. Biochem. Biophys. Res. Commun., 209, 788-795.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 788-795
    • Lew, R.A.1    Hey, N.J.2    Tetaz, T.J.3    Glucksman, M.J.4    Roberts, J.L.5    Smith, A.I.6
  • 13
    • 0028272080 scopus 로고
    • Evidence for a two-step mechanism of gonadotropin-releasing hormone (GnRH) metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.24.24.15
    • LEW, R.A. TETAZ, T., GLUCKSMAN, M.J., ROBERTS, J.L. & SMITH, A.I. (1994). Evidence for a two-step mechanism of gonadotropin-releasing hormone (GnRH) metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.24.24.15. J. Biol. Chem., 269, 12626-12632.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12626-12632
    • Lew, R.A.1    Tetaz, T.2    Glucksman, M.J.3    Roberts, J.L.4    Smith, A.I.5
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0023721848 scopus 로고
    • Endopeptidase-24.15 is the primary enzyme that degrades luteinizing hormone releasing hormone both in vitro and in vivo
    • MOLINEAUX, C.J., LASDUN, A., MICHAUD, C. & ORLOWSKI, M. (1988). Endopeptidase-24.15 is the primary enzyme that degrades luteinizing hormone releasing hormone both in vitro and in vivo. J. Neurochem., 51, 624-633.
    • (1988) J. Neurochem. , vol.51 , pp. 624-633
    • Molineaux, C.J.1    Lasdun, A.2    Michaud, C.3    Orlowski, M.4
  • 17
    • 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
  • 18
    • 0023871927 scopus 로고
    • Substrate-related potent inhibitors of brain metalloendopeptidase
    • ORLOWSKI, M., MICHAUD, C. & MOLINEAUX, C.J. (1988). Substrate-related potent inhibitors of brain metalloendopeptidase. Biochemistry, 27, 597-602.
    • (1988) Biochemistry , vol.27 , pp. 597-602
    • Orlowski, M.1    Michaud, C.2    Molineaux, C.J.3
  • 19
    • 0022551217 scopus 로고
    • Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions. Comparison with bacterial thermolysin
    • POZSGAY, M., MICHAUD, C., LIEBMAN, M & ORLOWSKI, M. (1986). Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions. Comparison with bacterial thermolysin. Biochemistry, 25, 1292 1299.
    • (1986) Biochemistry , vol.25 , pp. 1292-1299
    • Pozsgay, M.1    Michaud, C.2    Liebman, M.3    Orlowski, M.4
  • 20
    • 0019817187 scopus 로고
    • Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1, 3, 4, 6-tetrachloro-3α, 6α-diphenyl glycoluril (Iodogen)
    • SALACINSKI, P.R.P., MCLEAN, C., SKYES, J.E.C., CLEMENT-JONES. V.V. & LOWRY, P.J. (1981). Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1, 3, 4, 6-tetrachloro-3α, 6α-diphenyl glycoluril (Iodogen). Anal. Biochem., 117, 136-146.
    • (1981) Anal. Biochem. , vol.117 , pp. 136-146
    • Salacinski, P.R.P.1    Mclean, C.2    Skyes, J.E.C.3    Clement-Jones, V.V.4    Lowry, P.J.5
  • 21
    • 0025009278 scopus 로고
    • Enkephalinase (EC 3.4.24.11) inhibitors: Protection of endogenous ANF against inactivation and potential therapeutic applications
    • SCHWARTZ, J.-C., GROS, C., LECOMTE, J.-M. & BRALET, J. (1990). Enkephalinase (EC 3.4.24.11) inhibitors: protection of endogenous ANF against inactivation and potential therapeutic applications. Life Sci., 47, 1279-1297.
    • (1990) Life Sci. , vol.47 , pp. 1279-1297
    • Schwartz, J.-C.1    Gros, C.2    Lecomte, J.-M.3    Bralet, J.4
  • 22
    • 0011118368 scopus 로고
    • 2-and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone
    • 2-and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc. Natl. Acad. Sci. U.S.A., 82, 1025-1029.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1025-1029
    • Skidgel, R.A.1    Erdos, E.G.2
  • 23
    • 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., 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    Barnett, A.6    Haslanger, M.F.7
  • 24
    • 0025641384 scopus 로고
    • Neutral metalloendopeptidase inhibition: A novel means of circulatory modulation
    • SYBERTZ, E.J., JR., CHIU, P.J.S., WATKINS, R.W. & VEMULAPALLI, S. (1990). Neutral metalloendopeptidase inhibition: a novel means of circulatory modulation. J. Hypertens., 8(Suppl. 7). S161-S167.
    • (1990) J. Hypertens. , vol.8 , Issue.7 SUPPL.
    • Sybertz Jr., E.J.1    Chiu, P.J.S.2    Watkins, R.W.3    Vemulapalli, S.4
  • 25
    • 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
  • 26
    • 0002321492 scopus 로고
    • Inhibition of zinc peptidases that hydrolyse neuropeptides
    • ed. Turner, A.J. Chichester, UK: Ellis Horwood Ltd.
    • THORSETT, E.D. & WYVRATT, M.J. (1987). Inhibition of zinc peptidases that hydrolyse neuropeptides. In Neuropeptides and Their Peptidases. ed. Turner, A.J. pp. 229-292. Chichester, UK: Ellis Horwood Ltd.
    • (1987) Neuropeptides and Their Peptidases. , pp. 229-292
    • Thorsett, E.D.1    Wyvratt, M.J.2
  • 27
    • 0025363494 scopus 로고
    • An alternative quenched fluoresence substrate for Pz-peptidase
    • TISLJAR, U., KNIGHT, C.G. & BARRETT, A.J. (1990). An alternative quenched fluoresence substrate for Pz-peptidase. Anal. Biochem., 186, 112-115.
    • (1990) Anal. Biochem. , vol.186 , pp. 112-115
    • Tisljar, U.1    Knight, C.G.2    Barrett, A.J.3
  • 29
    • 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
  • 30
    • 0026605307 scopus 로고
    • In vivo metabolism of angiotensin 1 by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats
    • YAMAMOTO, K., CHAPPELL, M.C, BROSNIHAN, K.B. & FERRARIO, C.M. (1992). In vivo metabolism of angiotensin 1 by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats. Hypertension, 19, 692-696.
    • (1992) Hypertension , vol.19 , pp. 692-696
    • Yamamoto, K.1    Chappell, M.C.2    Brosnihan, K.B.3    Ferrario, C.M.4
  • 31
    • 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. I), 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.