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Volumn 2, Issue 13-14, 2002, Pages 1741-1746

The kinin system: Suggestions to broaden some prevailing concepts

Author keywords

ACE; Bradykinin; Kinin system

Indexed keywords

ANGIOTENSIN; BRADYKININ; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; KALLIDIN; KALLIDIN[1-9]; KALLIKREIN; KININ; KININASE; KININOGEN; NITRIC OXIDE; PREKALLIKREIN; PROSTAGLANDIN; RECEPTOR PROTEIN; BRADYKININ RECEPTOR;

EID: 0036892440     PISSN: 15675769     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-5769(02)00166-2     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 0026556434 scopus 로고
    • Bioregulation of kinins: Kallikreins, kininogens, and kininases
    • Bhoola K.D., Figueroa C.D., Worthy K. Bioregulation of kinins: kallikreins, kininogens, and kininases. Pharmacol. Rev. 44:1992;1-80.
    • (1992) Pharmacol. Rev. , vol.44 , pp. 1-80
    • Bhoola, K.D.1    Figueroa, C.D.2    Worthy, K.3
  • 2
    • 0036174408 scopus 로고    scopus 로고
    • Pathways for bradykinin formation and inflammatory disease
    • Kaplan A.P., Joseph K., Silverberg M. Pathways for bradykinin formation and inflammatory disease. J. Allergy Clin. Immunol. 109(2):2002;195-209.
    • (2002) J. Allergy Clin. Immunol. , vol.109 , Issue.2 , pp. 195-209
    • Kaplan, A.P.1    Joseph, K.2    Silverberg, M.3
  • 3
    • 0019939372 scopus 로고
    • Kallikrein and prekallikrein of the isolated basolateral membrane of rat kidney
    • Yamada K., Erdös E.G. Kallikrein and prekallikrein of the isolated basolateral membrane of rat kidney. Kidney Int. 22:1982;331-337.
    • (1982) Kidney Int. , vol.22 , pp. 331-337
    • Yamada, K.1    Erdös, E.G.2
  • 4
    • 0001559181 scopus 로고
    • Structure-activity relationships of kinins
    • Erdös E.G. Berlin: Springer
    • Schröder E. Structure-activity relationships of kinins. Erdös E.G. Handbook of experimental pharmacology. vol. XXV:1970;324-350 Springer, Berlin.
    • (1970) Handbook of experimental pharmacology , vol.25 , pp. 324-350
    • Schröder, E.1
  • 7
    • 0017801959 scopus 로고
    • SQ14,225 (D-3-mercapto-2-methylpropanoyl-L-proline), a novel orally active inhibitor of angiotensin I-converting enzyme
    • Rubin B., Laffan R.J., Kotler D.G., O'Keefe E.H., Demaio D.A., Goldberg M.E. SQ14,225 (D-3-mercapto-2-methylpropanoyl-L-proline), a novel orally active inhibitor of angiotensin I-converting enzyme. J. Pharmacol. Exp. Ther. 204:1978;271-280.
    • (1978) J. Pharmacol. Exp. Ther. , vol.204 , pp. 271-280
    • Rubin, B.1    Laffan, R.J.2    Kotler, D.G.3    O'Keefe, E.H.4    Demaio, D.A.5    Goldberg, M.E.6
  • 8
    • 0033785734 scopus 로고    scopus 로고
    • Potentiation of the effects of bradykinin on its receptor in the isolated guinea pig ileum
    • Minshall R.D., Nedumgottil S.J., Igic R., Erdös E.G., Rabito S.F. Potentiation of the effects of bradykinin on its receptor in the isolated guinea pig ileum. Peptides. 24:2000;1257-1264.
    • (2000) Peptides , vol.24 , pp. 1257-1264
    • Minshall, R.D.1    Nedumgottil, S.J.2    Igic, R.3    Erdös, E.G.4    Rabito, S.F.5
  • 9
    • 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., Fleck E. ACE inhibitors are endothelium dependent vasodilators of coronary arteries during submaximal stimulation with bradykinin. Cardiovasc. Res. 27:1993;312-317.
    • (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
  • 10
    • 0002389184 scopus 로고    scopus 로고
    • Perspectives on the early history of angiotensin-converting enzyme - Recent follow-ups
    • T.D. Giles. Fort Lee: Health Care Communications
    • Erdös E.G. Perspectives on the early history of angiotensin-converting enzyme - recent follow-ups. Giles T.D. Angiotensin-converting enzyme (ACE): clinical and experimental insights. 2001;3-16 Health Care Communications, Fort Lee.
    • (2001) Angiotensin-converting enzyme (ACE): Clinical and experimental insights , pp. 3-16
    • Erdös, E.G.1
  • 14
    • 0011735134 scopus 로고
    • Chap. 4 Enzyme kinetics
    • New York: Academic Press
    • Dixon M., Webb E.C. Chap. 4 Enzyme kinetics. Enzymes. 1964;69 Academic Press, New York.
    • (1964) Enzymes , pp. 69
    • Dixon, M.1    Webb, E.C.2
  • 15
    • 0021175531 scopus 로고
    • Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
    • Skidgel R.A., Engelbrecht S., Johnson A.R., Erdös E.G. Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase. Peptides. 5(4):1984;769-776.
    • (1984) Peptides , vol.5 , Issue.4 , pp. 769-776
    • Skidgel, R.A.1    Engelbrecht, S.2    Johnson, A.R.3    Erdös, E.G.4
  • 16
    • 0036267811 scopus 로고    scopus 로고
    • Kinins, the long march - A personal view
    • Erdös E.G. Kinins, the long march - a personal view. Cardiovasc. Res. 54(3):2002;485-491.
    • (2002) Cardiovasc. Res. , vol.54 , Issue.3 , pp. 485-491
    • Erdös, E.G.1
  • 17
    • 0027312101 scopus 로고
    • Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene
    • Soubrier F., Hubert C., Testus P., Nadaud S., Alhenc-Gelas F., Corvol P. Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene. J. Hypertension. 11:1993;471-476.
    • (1993) J. Hypertension , vol.11 , pp. 471-476
    • Soubrier, F.1    Hubert, C.2    Testus, P.3    Nadaud, S.4    Alhenc-Gelas, F.5    Corvol, P.6
  • 18
    • 0024379270 scopus 로고
    • Mouse angiotensin-converting enzyme is a protein composed of two homologous domains
    • Bernstein K.E., Martin B.M., Edwards A.S., Bernstein E.A. Mouse angiotensin-converting enzyme is a protein composed of two homologous domains. J. Biol. Chem. 264:1989;11945-11951.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11945-11951
    • Bernstein, K.E.1    Martin, B.M.2    Edwards, A.S.3    Bernstein, E.A.4
  • 20
    • 0027087022 scopus 로고
    • A comparison of the zinc contents and substrate specificities of the endothelial and testicular forms of porcine angiotensin converting enzyme and the preparation of isoenzyme-specific antisera
    • Williams T.A., Barnes K., Kenny A.J., Turner A.J., Hooper N.M. A comparison of the zinc contents and substrate specificities of the endothelial and testicular forms of porcine angiotensin converting enzyme and the preparation of isoenzyme-specific antisera. Biochem. J. 288(Pt 3):1992;875-881.
    • (1992) Biochem. J. , vol.288 , Issue.PART 3 , pp. 875-881
    • Williams, T.A.1    Barnes, K.2    Kenny, A.J.3    Turner, A.J.4    Hooper, N.M.5
  • 23
    • 0003876684 scopus 로고
    • Cardiovascular physiology
    • St. Louis: C.V. Mosby
    • Berne R.M., Levy M.N. Cardiovascular physiology. 2nd ed. 1972;C.V. Mosby, St. Louis.
    • (1972) 2nd ed.
    • Berne, R.M.1    Levy, M.N.2
  • 24
    • 4244064327 scopus 로고
    • Interaction of Hageman-factor-dependent systems with the complement sequence
    • J.J. Pisano, & K.F. Austen. St. Louis: U.S. Dept. of Health, Education and Welfare
    • Wooldridge D., Spragg J., Austen K.F. Interaction of Hageman-factor-dependent systems with the complement sequence. Pisano J.J., Austen K.F. Chemistry and biology of the kallikrein-kinin system in health and disease. 1976;221 U.S. Dept. of Health, Education and Welfare, St. Louis.
    • (1976) Chemistry and biology of the kallikrein-kinin system in health and disease , pp. 221
    • Wooldridge, D.1    Spragg, J.2    Austen, K.F.3
  • 25
    • 0028327659 scopus 로고
    • Potentiation by ACE inhibitors of the dilator response to bradykinin in the coronary microcirculation: Interaction at the receptor level
    • Hecker M., Pörsti K., Bara A.T., Busse R. Potentiation by ACE inhibitors of the dilator response to bradykinin in the coronary microcirculation: interaction at the receptor level. Br. J. Pharmacol. 111:1994;238-244.
    • (1994) Br. J. Pharmacol. , vol.111 , pp. 238-244
    • Hecker, M.1    Pörsti, K.2    Bara, A.T.3    Busse, R.4
  • 28
    • 0035569034 scopus 로고    scopus 로고
    • Potentiation of kinin analogues by ramiprilat is exclusively related to their degradation
    • Dendorfer A., Reibetamann S., Wolfrum S., Raasch W., Dominiak P. Potentiation of kinin analogues by ramiprilat is exclusively related to their degradation. Hypertension. 38(1):2001;142-146.
    • (2001) Hypertension , vol.38 , Issue.1 , pp. 142-146
    • Dendorfer, A.1    Reibetamann, S.2    Wolfrum, S.3    Raasch, W.4    Dominiak, P.5
  • 29
    • 0036188885 scopus 로고    scopus 로고
    • Kininase-independent potentiation of endothelium-dependent relaxations to kinins by converting enzyme inhibitor perindoprilat
    • Mombouli J.V., Ballard K.D., Vanhoutte P.M. Kininase-independent potentiation of endothelium-dependent relaxations to kinins by converting enzyme inhibitor perindoprilat. Acta Pharmacol. Sin. 23(3):2002;203-207.
    • (2002) Acta Pharmacol. Sin. , vol.23 , Issue.3 , pp. 203-207
    • Mombouli, J.V.1    Ballard, K.D.2    Vanhoutte, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.