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Volumn 93, Issue 2, 2003, Pages 148-154

Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin insights from selective inhibitors

Author keywords

Angiotensin; Angiotensin converting enzyme; Bradykinin; Phosphinic peptide inhibitors

Indexed keywords

ANGIOTENSIN; ANGIOTENSIN I; BRADYKININ; DIPEPTIDYL CARBOXYPEPTIDASE; RXP 407; RXP A380; UNCLASSIFIED DRUG;

EID: 0042490795     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.0000081593.33848.FC     Document Type: Article
Times cited : (152)

References (33)
  • 1
    • 0025039169 scopus 로고
    • Angiotensin I converting enzyme and the changes in our concepts through the years: Lewis K Dahl memorial lecture
    • Erdos EG. Angiotensin I converting enzyme and the changes in our concepts through the years: Lewis K. Dahl memorial lecture. Hypertension. 1990;16:363-370.
    • (1990) Hypertension , vol.16 , pp. 363-370
    • Erdos, E.G.1
  • 2
    • 0026556434 scopus 로고
    • Bioregulation of kinins: Kallikreins, kininogens, and kininases
    • Bhoola KD, Figueroa CD, Worthy K. Bioregulation of kinins: kallikreins, kininogens, and kininases. Pharmacol Rev. 1992;44:1-80.
    • (1992) Pharmacol Rev , vol.44 , pp. 1-80
    • Bhoola, K.D.1    Figueroa, C.D.2    Worthy, K.3
  • 3
    • 0028453483 scopus 로고
    • Corcoran lecture: Angiotensin-converting enzyme inhibition and the heart
    • Gavras H. Corcoran lecture: angiotensin-converting enzyme inhibition and the heart. Hypertension. 1994;23:813-818.
    • (1994) Hypertension , vol.23 , pp. 813-818
    • Gavras, H.1
  • 4
    • 0029010357 scopus 로고
    • Contribution of kinins to the cardiovascular actions of angiotensin-converting enzyme inhibitors
    • Linz W, Wiemer G, Gohlke P, Unger T, Scholkens BA. Contribution of kinins to the cardiovascular actions of angiotensin-converting enzyme inhibitors. Pharmacol Rev. 1995;47:25-49.
    • (1995) Pharmacol Rev , vol.47 , pp. 25-49
    • Linz, W.1    Wiemer, G.2    Gohlke, P.3    Unger, T.4    Scholkens, B.A.5
  • 5
    • 0035048905 scopus 로고    scopus 로고
    • Theodore Cooper lecture: Tissue angiotensin and pathobiology of vascular disease: A unifying hypothesis
    • Dzau VJ. Theodore Cooper lecture: tissue angiotensin and pathobiology of vascular disease: a unifying hypothesis. Hypertension. 2001;37:1047-1052.
    • (2001) Hypertension , vol.37 , pp. 1047-1052
    • Dzau, V.J.1
  • 6
    • 0036120563 scopus 로고    scopus 로고
    • The plasma kallikrein-kinin system counterbalances the renin-angiotensin system
    • Schmaier AH. The plasma kallikrein-kinin system counterbalances the renin-angiotensin system. J Clin Invest. 2002;109:1007-1009.
    • (2002) J Clin Invest , vol.109 , pp. 1007-1009
    • Schmaier, A.H.1
  • 8
    • 0025739667 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme are both catalytically active
    • Wei L, Alhenc-Gelas F, Corvol P, Clauser E. The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J Biol Chem. 1991;266:9002-9008.
    • (1991) J Biol Chem , vol.266 , pp. 9002-9008
    • Wei, L.1    Alhenc-Gelas, F.2    Corvol, P.3    Clauser, E.4
  • 9
    • 0026643458 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
    • Wei L, Clauser E, Alhenc-Gelas F, Corvol P. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J Biol Chem. 1992;267:13398-133405.
    • (1992) J Biol Chem , vol.267 , pp. 13398-133405
    • Wei, L.1    Clauser, E.2    Alhenc-Gelas, F.3    Corvol, P.4
  • 10
    • 0027175193 scopus 로고
    • Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II): Studies with bradykinin and other natural peptides
    • Jaspard E, Wei L, Alhenc-Gelas F. Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II): studies with bradykinin and other natural peptides. J Biol Chem. 1993;268:9496-9503.
    • (1993) J Biol Chem , vol.268 , pp. 9496-9503
    • Jaspard, E.1    Wei, L.2    Alhenc-Gelas, F.3
  • 12
    • 0030981239 scopus 로고    scopus 로고
    • Substrate dependence of angiotensin I-converting enzyme inhibition: Captopril displays a partial selectivity for inhibition of N-acetyl-seryl-aspartyl-lysyl-proline hydrolysis compared with that of angiotensin I
    • Michaud A, Williams TA, Chauvet MT, Corvol P. Substrate dependence of angiotensin I-converting enzyme inhibition: captopril displays a partial selectivity for inhibition of N-acetyl-seryl-aspartyl-lysyl-proline hydrolysis compared with that of angiotensin I. Mol Pharmacol. 1997;51:1070-1076.
    • (1997) Mol Pharmacol , vol.51 , pp. 1070-1076
    • Michaud, A.1    Williams, T.A.2    Chauvet, M.T.3    Corvol, P.4
  • 13
    • 0031954590 scopus 로고    scopus 로고
    • N-domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: Angiotensin-(1-7) and keto-ACE
    • Deddish PA, Marcic B, Jackman HL, Wang HZ, Skidgel RA, Erdos EG. N-domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: angiotensin-(1-7) and keto-ACE. Hypertension. 1998;31:912-917.
    • (1998) Hypertension , vol.31 , pp. 912-917
    • Deddish, P.A.1    Marcic, B.2    Jackman, H.L.3    Wang, H.Z.4    Skidgel, R.A.5    Erdos, E.G.6
  • 14
    • 0028967315 scopus 로고
    • The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme
    • Rousseau A, Michaud A, Chauvet MT, Lenfant M, Corvol P. The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J Biol Chem. 1995;270:3656-3661.
    • (1995) J Biol Chem , vol.270 , pp. 3656-3661
    • Rousseau, A.1    Michaud, A.2    Chauvet, M.T.3    Lenfant, M.4    Corvol, P.5
  • 15
    • 0028180926 scopus 로고
    • Structural constraints of inhibitors for binding at two active sites on somatic angiotensin converting enzyme
    • Perich RB, Jackson B, Johnston CI. Structural constraints of inhibitors for binding at two active sites on somatic angiotensin converting enzyme. Eur J Pharmacol. 1994;266:201-211.
    • (1994) Eur J Pharmacol , vol.266 , pp. 201-211
    • Perich, R.B.1    Jackson, B.2    Johnston, C.I.3
  • 17
    • 0035042245 scopus 로고    scopus 로고
    • RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis
    • Junot C, Gonzales MF, Ezan E, Cotton J, Vazeux G, Michaud A, Azizi M, Vassiliou S, Yiotakis A, Corvol P, Dive V. RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis. J Pharmacol Exp Ther. 2001;297:606-611.
    • (2001) J Pharmacol Exp Ther , vol.297 , pp. 606-611
    • Junot, C.1    Gonzales, M.F.2    Ezan, E.3    Cotton, J.4    Vazeux, G.5    Michaud, A.6    Azizi, M.7    Vassiliou, S.8    Yiotakis, A.9    Corvol, P.10    Dive, V.11
  • 18
    • 0030027331 scopus 로고    scopus 로고
    • Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline
    • Azizi M, Rousseau A, Ezan E, Guyene TT, Michelet S, Grognet JM, Lenfant M, Corvol P, Menard J. Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline. J Clin Invest. 1996;97:839-844.
    • (1996) J Clin Invest , vol.97 , pp. 839-844
    • Azizi, M.1    Rousseau, A.2    Ezan, E.3    Guyene, T.T.4    Michelet, S.5    Grognet, J.M.6    Lenfant, M.7    Corvol, P.8    Menard, J.9
  • 19
    • 0035313232 scopus 로고    scopus 로고
    • Potency and selectivity of RXP407 on human, rat, and mouse angiotensin-converting enzyme
    • Vazeux G, Cotton J, Cuniasse P, Dive V. Potency and selectivity of RXP407 on human, rat, and mouse angiotensin-converting enzyme. Biochem Pharmacol. 2001;61:835-841.
    • (2001) Biochem Pharmacol , vol.61 , pp. 835-841
    • Vazeux, G.1    Cotton, J.2    Cuniasse, P.3    Dive, V.4
  • 20
    • 0037076516 scopus 로고    scopus 로고
    • Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides
    • Cotton J, Hayashi MA, Cuniasse P, Vazeux G, Ianzer D, De Camargo AC, Dive V. Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides. Biochemistry. 2002;41:6065-6071.
    • (2002) Biochemistry , vol.41 , pp. 6065-6071
    • Cotton, J.1    Hayashi, M.A.2    Cuniasse, P.3    Vazeux, G.4    Ianzer, D.5    De Camargo, A.C.6    Dive, V.7
  • 21
    • 0034620609 scopus 로고    scopus 로고
    • Potent and selective inhibition of zinc aminopeptidase A (EC 3.4.11.7, APA) by glutamyl aminophosphinic peptides: Importance of glutamyl aminophosphinic residue in the P1 position
    • Georgiadis D, Vazeux G, Llorens-Cortes C, Yiotakis A, Dive V. Potent and selective inhibition of zinc aminopeptidase A (EC 3.4.11.7, APA) by glutamyl aminophosphinic peptides: importance of glutamyl aminophosphinic residue in the P1 position. Biochemistry. 2000;39:1152-1155.
    • (2000) Biochemistry , vol.39 , pp. 1152-1155
    • Georgiadis, D.1    Vazeux, G.2    Llorens-Cortes, C.3    Yiotakis, A.4    Dive, V.5
  • 22
    • 0028274151 scopus 로고
    • Effects of converting enzyme inhibitors on angiotensin and bradykinin peptides
    • Campbell DJ, Kladis A, Duncan AM. Effects of converting enzyme inhibitors on angiotensin and bradykinin peptides. Hypertension. 1994;23:439-449.
    • (1994) Hypertension , vol.23 , pp. 439-449
    • Campbell, D.J.1    Kladis, A.2    Duncan, A.M.3
  • 23
    • 0026481029 scopus 로고
    • Effect of inhibition of endopeptidase 24.11 on responses to angiotensin II in human volunteers
    • Richards AM, Wittert GA, Espiner EA, Yandle TG, Ikram H, Frampton C. Effect of inhibition of endopeptidase 24.11 on responses to angiotensin II in human volunteers. Circ Res. 1992;71:1501-1507.
    • (1992) Circ Res , vol.71 , pp. 1501-1507
    • Richards, A.M.1    Wittert, G.A.2    Espiner, E.A.3    Yandle, T.G.4    Ikram, H.5    Frampton, C.6
  • 24
    • 0026605307 scopus 로고
    • In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats
    • Yamamoto K, Chappell MC, Brosnihan KB, Ferrario CM. In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats. Hypertension. 1992;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
  • 25
    • 0025788169 scopus 로고
    • Angiotensin-converting enzyme: Zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes
    • Ehlers MR, Riordan JF. Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry. 1991;30:7118-7126.
    • (1991) Biochemistry , vol.30 , pp. 7118-7126
    • Ehlers, M.R.1    Riordan, J.F.2
  • 26
    • 0032493428 scopus 로고    scopus 로고
    • Angiotensin production by the heart: A quantitative study in pigs with the use of radiolabeled angiotensin infusions
    • van Kats JP, Danser AH, van Meegen JR, Sassen LM, Verdouw PD, Schalekamp MA. Angiotensin production by the heart: a quantitative study in pigs with the use of radiolabeled angiotensin infusions. Circulation. 1998;98:73-81.
    • (1998) Circulation , vol.98 , pp. 73-81
    • Van Kats, J.P.1    Danser, A.H.2    Van Meegen, J.R.3    Sassen, L.M.4    Verdouw, P.D.5    Schalekamp, M.A.6
  • 27
    • 0032456219 scopus 로고    scopus 로고
    • Effects of neutral endopeptidase inhibition and combined angiotensin converting enzyme and neutral endopeptidase inhibition on angiotensin and bradykinin peptides in rats
    • Campbell DJ, Anastasopoulos F, Duncan AM, James GM, Kladis A, Briscoe TA. Effects of neutral endopeptidase inhibition and combined angiotensin converting enzyme and neutral endopeptidase inhibition on angiotensin and bradykinin peptides in rats. J Pharmacol Exp Ther. 1998;287:567-577.
    • (1998) J Pharmacol Exp Ther , vol.287 , pp. 567-577
    • Campbell, D.J.1    Anastasopoulos, F.2    Duncan, A.M.3    James, G.M.4    Kladis, A.5    Briscoe, T.A.6
  • 28
    • 0014217361 scopus 로고
    • Conversion of angiotensin I to angiotensin II
    • Ng KK, Vane JR. Conversion of angiotensin I to angiotensin II. Nature. 1967;216:762-766.
    • (1967) Nature , vol.216 , pp. 762-766
    • Ng, K.K.1    Vane, J.R.2
  • 29
    • 0014412538 scopus 로고
    • Fate of angiotensin I in the circulation
    • Ng KK, Vane JR. Fate of angiotensin I in the circulation. Nature. 1968;218:144-150.
    • (1968) Nature , vol.218 , pp. 144-150
    • Ng, K.K.1    Vane, J.R.2
  • 31
    • 0037040222 scopus 로고    scopus 로고
    • The germinal isozyme of angiotensin-converting enzyme can substitute for the somatic isozyme in maintaining normal renal structure and functions
    • Kessler SP, Gomos JB, Scheidemantel TS, Rowe TM, Smith HL, Sen GC. The germinal isozyme of angiotensin-converting enzyme can substitute for the somatic isozyme in maintaining normal renal structure and functions. J Biol Chem. 2002;277:4271-4276.
    • (2002) J Biol Chem , vol.277 , pp. 4271-4276
    • Kessler, S.P.1    Gomos, J.B.2    Scheidemantel, T.S.3    Rowe, T.M.4    Smith, H.L.5    Sen, G.C.6
  • 33
    • 0032515917 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitors
    • Brown NJ, Vaughan DE. Angiotensin-converting enzyme inhibitors. Circulation. 1998;97:1411-1420.
    • (1998) Circulation , vol.97 , pp. 1411-1420
    • Brown, N.J.1    Vaughan, D.E.2


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