메뉴 건너뛰기




Volumn 51, Issue 8, 1996, Pages 1051-1060

Inhibition of angiotensin converting enzyme and potentiation of bradykinin by retro-inverse analogues of short peptides and sequences related to angiotensin I and bradykinin

Author keywords

Angiotensin converting enzyme inhibitors; Bradykinin potentiation; Peptide synthesis; Retro inverso peptide

Indexed keywords

ANGIOTENSIN I DERIVATIVE; BRADYKININ; BRADYKININ DERIVATIVE; DIPEPTIDE; DIPEPTIDYL CARBOXYPEPTIDASE; PEPTIDE DERIVATIVE; SNAKE VENOM; TRIPEPTIDE;

EID: 0029868276     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(96)00047-0     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 0019422994 scopus 로고
    • Antihypertensive activity of N-[(S)]-1-(ethoxycarbonyl)-3-phenylpropyl-L-Ala-L-Pro (MK 421), an orally active converting enzyme inhibitor
    • Sweet CS, Gross DM, Arbegast PT, Gaul SL, Britt PM, Ludden CT, Weitz D and Stone CA, Antihypertensive activity of N-[(S)]-1-(ethoxycarbonyl)-3-phenylpropyl]-L-Ala-L-Pro (MK 421), an orally active converting enzyme inhibitor. J Pharmacol Exp Ther 216: 558-566, 1981.
    • (1981) J Pharmacol Exp Ther , vol.216 , pp. 558-566
    • Sweet, C.S.1    Gross, D.M.2    Arbegast, P.T.3    Gaul, S.L.4    Britt, P.M.5    Ludden, C.T.6    Weitz, D.7    Stone, C.A.8
  • 2
    • 0019152870 scopus 로고
    • Vasodepressor property of the converting enzyme inhibitor captopril (SQ 14225): The role of factors other than renin-angiotensin blockade in the rat
    • Marks ES, Bing RF, Thurston H and Swales JD, Vasodepressor property of the converting enzyme inhibitor captopril (SQ 14225): The role of factors other than renin-angiotensin blockade in the rat. Clin Sci 58: 1-6, 1980.
    • (1980) Clin Sci , vol.58 , pp. 1-6
    • Marks, E.S.1    Bing, R.F.2    Thurston, H.3    Swales, J.D.4
  • 3
    • 0018600836 scopus 로고
    • The effects of captopril, propranolol, and indomethacin on blood pressure and plasma renin activity in spontaneously hypertensive and normotensive rats
    • Antonaccio MJ, Harris D, Goldenberg H, High JP and Rubin B, The effects of captopril, propranolol, and indomethacin on blood pressure and plasma renin activity in spontaneously hypertensive and normotensive rats. Proc Soc Exp Biol Med 162: 429-433, 1979.
    • (1979) Proc Soc Exp Biol Med , vol.162 , pp. 429-433
    • Antonaccio, M.J.1    Harris, D.2    Goldenberg, H.3    High, J.P.4    Rubin, B.5
  • 4
    • 0017650885 scopus 로고
    • Inhibition of angiotensin converting enzyme by SQ 14225 in conscious rabbits
    • Murthy VS, Waldron TL, Goldenberg ME and Vollmer RR, Inhibition of angiotensin converting enzyme by SQ 14225 in conscious rabbits. Eur J Pharmacol 46: 207-212, 1977.
    • (1977) Eur J Pharmacol , vol.46 , pp. 207-212
    • Murthy, V.S.1    Waldron, T.L.2    Goldenberg, M.E.3    Vollmer, R.R.4
  • 5
    • 0025110014 scopus 로고
    • Protective effects of sulfhydryl-containing angiotensin converting enzyme inhibitors against free radical injury in endothelial cells
    • Mak IT, Freedman AM, Dickens BF and Weglicki WB, Protective effects of sulfhydryl-containing angiotensin converting enzyme inhibitors against free radical injury in endothelial cells. Biochem Pharmacol 40: 2169-2175, 1990.
    • (1990) Biochem Pharmacol , vol.40 , pp. 2169-2175
    • Mak, I.T.1    Freedman, A.M.2    Dickens, B.F.3    Weglicki, W.B.4
  • 6
    • 0018288260 scopus 로고
    • Mechanism of angiotensin I converting enzyme inhibition by SQ 20881 (
    • Oparil S, Koerner T and O'Donoghue JK, Mechanism of angiotensin I converting enzyme inhibition by SQ 20881 (
    • (1979) Hypertension , vol.1 , pp. 13-22
    • Oparil, S.1    Koerner, T.2    O'Donoghue, J.K.3
  • 7
    • 0019311085 scopus 로고
    • Discrepancy between antihypertensive effect and angiotensin converting enzyme inhibition by captopril
    • Waeber B, Brunner HR, Brunner DB, Curtet AL, Turini GA and Gavras H, Discrepancy between antihypertensive effect and angiotensin converting enzyme inhibition by captopril. Hypertension 2: 236-242, 1980.
    • (1980) Hypertension , vol.2 , pp. 236-242
    • Waeber, B.1    Brunner, H.R.2    Brunner, D.B.3    Curtet, A.L.4    Turini, G.A.5    Gavras, H.6
  • 8
    • 0021079005 scopus 로고
    • Protracted effect of converting enzyme inhibition on the rat's response to intraarterial bradykinin
    • Lindsey CJ, De Paula UM and Paiva ACM, Protracted effect of converting enzyme inhibition on the rat's response to intraarterial bradykinin. Hypertension 5 (Suppl V): V134-V137, 1983.
    • (1983) Hypertension , vol.5 , Issue.SUPPL. V
    • Lindsey, C.J.1    De Paula, U.M.2    Paiva, A.C.M.3
  • 9
    • 0022481001 scopus 로고
    • Converting enzyme inhibitors decrease kininase but not converting activity in the rat mesenteric vascular bed
    • Bendhack LM, Lindsey CJ and Paiva ACM, Converting enzyme inhibitors decrease kininase but not converting activity in the rat mesenteric vascular bed. Hypertension 8 (Suppl I): I,90-I-94, 1986.
    • (1986) Hypertension , vol.8 , Issue.SUPPL. I
    • Bendhack, L.M.1    Lindsey, C.J.2    Paiva, A.C.M.3
  • 10
    • 0017664337 scopus 로고
    • Bradykinin potentiating and sensitizing activities of new synthetic analogues of snake venom peptides
    • Sabia EB, Tominaga M, Paiva ACM and Piazza TB, Bradykinin potentiating and sensitizing activities of new synthetic analogues of snake venom peptides. J Med Chem 20: 1679-1681, 1977.
    • (1977) J Med Chem , vol.20 , pp. 1679-1681
    • Sabia, E.B.1    Tominaga, M.2    Paiva, A.C.M.3    Piazza, T.B.4
  • 11
    • 0026043502 scopus 로고
    • Potentiation of bradykinin effects and inhibition of kininase activity in isolated smooth muscle
    • Schaffel R, Rodrigues MS and Assreuy J, Potentiation of bradykinin effects and inhibition of kininase activity in isolated smooth muscle. Can J Physiol Pharmacol 69: 904-908, 1990.
    • (1990) Can J Physiol Pharmacol , vol.69 , pp. 904-908
    • Schaffel, R.1    Rodrigues, M.S.2    Assreuy, J.3
  • 12
    • 0028274151 scopus 로고
    • Effects of converting enzyme inhibitors on angiotensin and bradykinin peptides
    • Campbell DJ, Kladis A and Ducan AM, Effects of converting enzyme inhibitors on angiotensin and bradykinin peptides. Hypertension 23: 439-449, 1994.
    • (1994) Hypertension , vol.23 , pp. 439-449
    • Campbell, D.J.1    Kladis, A.2    Ducan, A.M.3
  • 14
    • 0015080491 scopus 로고
    • Action of bradykinin potentiating factor (BFP) and dimercaprol (BAL) on the responses to bradykinin of isolated preparations of rat intestines
    • Camargo ACM and Ferreira SH, Action of bradykinin potentiating factor (BFP) and dimercaprol (BAL) on the responses to bradykinin of isolated preparations of rat intestines. Br J Pharmacol 42: 305-307, 1971.
    • (1971) Br J Pharmacol , vol.42 , pp. 305-307
    • Camargo, A.C.M.1    Ferreira, S.H.2
  • 15
    • 17544388906 scopus 로고
    • Inhibition of the conversion of angiotensin I to II and potentiation of bradykinin by small peptides present in Bothrops jararaca venom
    • Greene LJ, Camargo ACM, Krieger EM, Stewart JM and Ferreira SH, Inhibition of the conversion of angiotensin I to II and potentiation of bradykinin by small peptides present in Bothrops jararaca venom. Circ Res 30/31 (Suppl II): II-62-II-71, 1972.
    • (1972) Circ Res , vol.30-31 , Issue.SUPPL. II
    • Greene, L.J.1    Camargo, A.C.M.2    Krieger, E.M.3    Stewart, J.M.4    Ferreira, S.H.5
  • 16
    • 0028327659 scopus 로고
    • Potentiation by ACE inhibitors of the dilator response to bradykinin in the coronary microcirculation: Interaction at the receptor level
    • Hecker M, Porsti I, Bara AT and Bussi R, Potentiation by ACE inhibitors of the dilator response to bradykinin in the coronary microcirculation: Interaction at the receptor level. Br J Pharmacol 111: 238-244, 1994.
    • (1994) Br J Pharmacol , vol.111 , pp. 238-244
    • Hecker, M.1    Porsti, I.2    Bara, A.T.3    Bussi, R.4
  • 17
    • 85047678379 scopus 로고
    • ACE inhibitors are endothelium dependent vasodilators of coronary arteries during submaximal stimulation with bradykinin
    • Auch-Schwelk W, Bossaller C, Claus M, Graf K, Gräfe M and Fleck E, ACE inhibitors are endothelium dependent vasodilators of coronary arteries during submaximal stimulation with bradykinin. Cardiovasc Res 27: 312-317, 1993.
    • (1993) Cardiovasc Res , vol.27 , pp. 312-317
    • Auch-Schwelk, W.1    Bossaller, C.2    Claus, M.3    Graf, K.4    Gräfe, M.5    Fleck, E.6
  • 18
    • 37049106674 scopus 로고
    • Synthesis, resolution, and assignment of configuration of potent hypotensive retro-inverso bradykinin potentiating peptide 5a (BPP 5a) analogues
    • Verdini AS and Viscome GC, Synthesis, resolution, and assignment of configuration of potent hypotensive retro-inverso bradykinin potentiating peptide 5a (BPP 5a) analogues. J Chem Soc Perkin Trans I: 697-701, 1985.
    • (1985) J Chem Soc Perkin Trans , vol.1 , pp. 697-701
    • Verdini, A.S.1    Viscome, G.C.2
  • 19
    • 0021744465 scopus 로고
    • Solid phase synthesis of retro-inverso peptide analogues
    • Bonelly F, Pessi A and Verdini AS, Solid phase synthesis of retro-inverso peptide analogues. Int J Pept Protein Res 24: 553-556, 1984.
    • (1984) Int J Pept Protein Res , vol.24 , pp. 553-556
    • Bonelly, F.1    Pessi, A.2    Verdini, A.S.3
  • 20
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I and Berger A, On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27: 157-162, 1967.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 21
    • 33845560283 scopus 로고
    • On the concept of linear modified retro-peptide structures
    • Goodman M and Chorev M, On the concept of linear modified retro-peptide structures. Acc Chem Res 12: 1-7, 1979.
    • (1979) Acc Chem Res , vol.12 , pp. 1-7
    • Goodman, M.1    Chorev, M.2
  • 22
    • 0000845126 scopus 로고
    • A dozen years of retro-inverso peptidomimetics
    • Chorev M and Goodman M, A dozen years of retro-inverso peptidomimetics. Acc Chem Res 26: 266-273, 1993.
    • (1993) Acc Chem Res , vol.26 , pp. 266-273
    • Chorev, M.1    Goodman, M.2
  • 23
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of COOH-terminal dipeptide sequence
    • Cheung H-S, Wang F-L, Ondetti MA, Sabo EF and Cushman DW, Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of COOH-terminal dipeptide sequence. J Biol Chem 255: 401-407, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 401-407
    • Cheung, H.-S.1    Wang, F.-L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 24
    • 0019981669 scopus 로고
    • Inhibition of renin by conformationally restricted analogues of angiotensinogen
    • Nakaie CR, Oliveira MCF, Juliano L and Paiva ACM, Inhibition of renin by conformationally restricted analogues of angiotensinogen. Biochem J 205: 43-47, 1982.
    • (1982) Biochem J , vol.205 , pp. 43-47
    • Nakaie, C.R.1    Oliveira, M.C.F.2    Juliano, L.3    Paiva, A.C.M.4
  • 25
    • 0014959663 scopus 로고
    • Isolation of bradykinin potentiating peptides from Bothrops jararaca venom
    • Ferreira SH, Bartelt DC and Greene LJ, Isolation of bradykinin potentiating peptides from Bothrops jararaca venom. Biochemistry 9: 2583-2593, 1970.
    • (1970) Biochemistry , vol.9 , pp. 2583-2593
    • Ferreira, S.H.1    Bartelt, D.C.2    Greene, L.J.3
  • 26
    • 0015228658 scopus 로고
    • Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffii. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C
    • Kato H and Suzuki T, Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffii. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C. Biochemistry 10: 972-980, 1971.
    • (1971) Biochemistry , vol.10 , pp. 972-980
    • Kato, H.1    Suzuki, T.2
  • 28
    • 0022177236 scopus 로고
    • Synthesis and kinetic parameters of hydrolysis by trypsin of some acyl-arginyl-p-nitroanilides and peptides containing arginyl-p-nitroanilide
    • Juliano MA and Juliano L, Synthesis and kinetic parameters of hydrolysis by trypsin of some acyl-arginyl-p-nitroanilides and peptides containing arginyl-p-nitroanilide. Braz J Med Biol Res 18: 435-445, 1985.
    • (1985) Braz J Med Biol Res , vol.18 , pp. 435-445
    • Juliano, M.A.1    Juliano, L.2
  • 30
    • 0026639416 scopus 로고
    • Substrate specificities of tissue kallikrein and T-kininogenase: Their possible role in kininogen processing
    • Chagas JR, Hirata IY, Juliano MA, Xiong W, Wang C, Chao J, Juliano L and Prado ES, Substrate specificities of tissue kallikrein and T-kininogenase: Their possible role in kininogen processing. Biochemistry 31: 4969-4974, 1992.
    • (1992) Biochemistry , vol.31 , pp. 4969-4974
    • Chagas, J.R.1    Hirata, I.Y.2    Juliano, M.A.3    Xiong, W.4    Wang, C.5    Chao, J.6    Juliano, L.7    Prado, E.S.8
  • 31
    • 0040893587 scopus 로고
    • Chemical procedures for the synthesis of peptides
    • John Wiley, New York
    • Greenstein JP and Winitz M, Chemical procedures for the synthesis of peptides. Chemistry of the Amino Acids, Vol. 2, pp. 763-1295. John Wiley, New York, 1961.
    • (1961) Chemistry of the Amino Acids , vol.2 , pp. 763-1295
    • Greenstein, J.P.1    Winitz, M.2
  • 32
    • 0039115555 scopus 로고
    • A method for the stepwise degradation of polypeptides
    • Bergmann M and Zervas L, A method for the stepwise degradation of polypeptides. J Biol Chem 113: 341-357, 1936.
    • (1936) J Biol Chem , vol.113 , pp. 341-357
    • Bergmann, M.1    Zervas, L.2
  • 33
    • 0017131074 scopus 로고
    • Synthesis of biologically active retroenantiomers of angiotensin peptides
    • Goissis G, Nouaihetas VLA and Paiva ACM, Synthesis of biologically active retroenantiomers of angiotensin peptides. J Med Chem 19: 1287-1290, 1976.
    • (1976) J Med Chem , vol.19 , pp. 1287-1290
    • Goissis, G.1    Nouaihetas, V.L.A.2    Paiva, A.C.M.3
  • 34
    • 0018121934 scopus 로고
    • Refinement of the Coomassie blue method of protein quantitation
    • Spector T, Refinement of the Coomassie blue method of protein quantitation. Anal Biochem 86: 142-146, 1978.
    • (1978) Anal Biochem , vol.86 , pp. 142-146
    • Spector, T.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
    • Cushman DW and Cheung HS, Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharmacol 20: 1637-1648, 1971.
    • (1971) Biochem Pharmacol , vol.20 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 37
    • 0017194947 scopus 로고
    • A sensitive fluorimetric assay for serum angiotensin converting enzyme
    • Friedland F and Silverstein F, A sensitive fluorimetric assay for serum angiotensin converting enzyme. Am J Clin Pathol 66: 416-424, 1976.
    • (1976) Am J Clin Pathol , vol.66 , pp. 416-424
    • Friedland, F.1    Silverstein, F.2
  • 38
    • 0015051857 scopus 로고
    • Characterization of a dipeptidyl hydrolase (kinin II; angiotensin I converting enzyme)
    • Yang HYT, Erdös EG and Levin Y, Characterization of a dipeptidyl hydrolase (kinin II; angiotensin I converting enzyme). J Pharmacol Exp Ther 117: 291-300, 1971.
    • (1971) J Pharmacol Exp Ther , vol.117 , pp. 291-300
    • Yang, H.Y.T.1    Erdös, E.G.2    Levin, Y.3
  • 40
    • 0016424451 scopus 로고
    • Synthesis and properties of new bradykinin potentiating peptides
    • Tominaga M, Stewart JM, Paiva TB and Paiva ACM, Synthesis and properties of new bradykinin potentiating peptides. J Med Chem 18: 130-133, 1975.
    • (1975) J Med Chem , vol.18 , pp. 130-133
    • Tominaga, M.1    Stewart, J.M.2    Paiva, T.B.3    Paiva, A.C.M.4
  • 41
    • 0024576412 scopus 로고
    • Kinetic and inhibitory characteristics of serum angiotensin-converting enzyme from nine mammalian species
    • Ibarra-Rubio MH, Pena JC and Pedraza-Chaverri J, Kinetic and inhibitory characteristics of serum angiotensin-converting enzyme from nine mammalian species. Comp Biochem Physiol [B] 92: 339-403, 1989.
    • (1989) Comp Biochem Physiol [b] , vol.92 , pp. 339-403
    • Ibarra-Rubio, M.H.1    Pena, J.C.2    Pedraza-Chaverri, J.3
  • 42
    • 0017065286 scopus 로고
    • Angiotensin I-converting enzyme from guinea pig lung and serum. A comparison of some kinetic and inhibition properties
    • Lanzillo JJ and Fanburg BL, Angiotensin I-converting enzyme from guinea pig lung and serum. A comparison of some kinetic and inhibition properties. Biochim Biophys Acta 445: 161-168, 1976.
    • (1976) Biochim Biophys Acta , vol.445 , pp. 161-168
    • Lanzillo, J.J.1    Fanburg, B.L.2
  • 43
    • 0019546187 scopus 로고
    • Purification of human serum angiotensin I converting enzyme by affinity chromatography
    • Harris RB, Ohlsson JT and Wilson IB, Purification of human serum angiotensin I converting enzyme by affinity chromatography. Anal Biochem 111: 227-234, 1981.
    • (1981) Anal Biochem , vol.111 , pp. 227-234
    • Harris, R.B.1    Ohlsson, J.T.2    Wilson, I.B.3
  • 44
    • 0007663812 scopus 로고
    • Retro-inverso isomerization of peptides: Side reactions in the synthesis of N-N′-diacyl-1,1-diamino-2-phenylethane derivatives
    • Chorev M, MacDonald SA and Goodman M, Retro-inverso isomerization of peptides: Side reactions in the synthesis of N-N′-diacyl-1,1-diamino-2-phenylethane derivatives. J Org Chem 49: 821-827, 1984.
    • (1984) J Org Chem , vol.49 , pp. 821-827
    • Chorev, M.1    MacDonald, S.A.2    Goodman, M.3
  • 45
    • 0019853079 scopus 로고
    • Purification and substrate specificity of bovine angiotensin-converting enzyme
    • Rohrbach MS, Williams EB and Rolstad DA, Purification and substrate specificity of bovine angiotensin-converting enzyme. J Biol Chem 256: 225-230, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 225-230
    • Rohrbach, M.S.1    Williams, E.B.2    Rolstad, D.A.3
  • 46
    • 0021152476 scopus 로고
    • Angiotensin-converting enzyme inhibitors: Biochemical properties and biological actions
    • Ondetti MA and Chusman DW, Angiotensin-converting enzyme inhibitors: Biochemical properties and biological actions. Crit Rev Biochem 16: 381-411, 1984.
    • (1984) Crit Rev Biochem , vol.16 , pp. 381-411
    • Ondetti, M.A.1    Chusman, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.