메뉴 건너뛰기




Volumn 35, Issue 6, 2000, Pages 1284-1290

Angiotensin I-converting enzyme isoforms (high and low molecular weight) in urine of premature and full-term infants

Author keywords

Angiotensin converting enzyme; Infants, full term; Infants, premature; Nephrogenesis; Urine

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE;

EID: 0034124227     PISSN: 0194911X     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.HYP.35.6.1284     Document Type: Article
Times cited : (20)

References (45)
  • 1
    • 0014957830 scopus 로고
    • A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin
    • Yang HYY, Erdös EG, Levin V. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochem Biophys Acta. 1970;214:374-376.
    • (1970) Biochem Biophys Acta , vol.214 , pp. 374-376
    • Yang, H.Y.Y.1    Erdös, E.G.2    Levin, V.3
  • 2
    • 0023197647 scopus 로고
    • The broad substrate specificity of human angiotensin I converting enzyme
    • Review
    • Skidgel RA, Erdös EG. The broad substrate specificity of human angiotensin I converting enzyme. Clin Exp Hypertens [A]. 1987;A9:243-259. Review.
    • (1987) Clin Exp Hypertens [A] , vol.A9 , pp. 243-259
    • Skidgel, R.A.1    Erdös, E.G.2
  • 3
    • 0021175531 scopus 로고
    • Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
    • Skidgel RA, Engelbrench S, Johnson AR, Erdös EG. Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase. Peptides. 1984;5:769.
    • (1984) Peptides , vol.5 , pp. 769
    • Skidgel, R.A.1    Engelbrench, S.2    Johnson, A.R.3    Erdös, E.G.4
  • 7
    • 0025039169 scopus 로고
    • Angiotensin I-converting enzyme and the changes in our concepts through the years
    • Erdös EG. Angiotensin I-converting enzyme and the changes in our concepts through the years. Hypertension. 1990;16:363-370.
    • (1990) Hypertension , vol.16 , pp. 363-370
    • Erdös, E.G.1
  • 8
    • 0020678693 scopus 로고
    • Activation of angiotensin converting enzyme by monovalent anions
    • Bünning P, Riordan JF. Activation of angiotensin converting enzyme by monovalent anions. Biochemistry. 1983;22:110-116.
    • (1983) Biochemistry , vol.22 , pp. 110-116
    • Bünning, P.1    Riordan, J.F.2
  • 10
    • 1642442623 scopus 로고
    • Tissue renin-angiotensin system: Physiologic and pharmacologic implications: Introduction
    • Dzau VJ. Tissue renin-angiotensin system: physiologic and pharmacologic implications: introduction. Circulation. 1988;77(pt 2):I1-I3.
    • (1988) Circulation , vol.77 , Issue.2 PART
    • Dzau, V.J.1
  • 11
    • 0023280497 scopus 로고
    • The angiotensin I-converting enzyme
    • Erdös EG, and Skidgel RA. The angiotensin I-converting enzyme. Lab Invest. 1987;56:345-348.
    • (1987) Lab Invest , vol.56 , pp. 345-348
    • Erdös, E.G.1    Skidgel, R.A.2
  • 12
    • 0029142859 scopus 로고
    • Angiotensin as a renal growth promoting factor
    • Wolf G. Angiotensin as a renal growth promoting factor. Adv Exp Med Biol. 1995;377:225-236.
    • (1995) Adv Exp Med Biol , vol.377 , pp. 225-236
    • Wolf, G.1
  • 14
    • 0032408635 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I-converting enzymes from mesangial cells in culture
    • Andrade MC, Quinto BM, Carmona AK, Ribas OS, Boim MA, Schor N, Casarini DE. Purification and characterization of angiotensin I-converting enzymes from mesangial cells in culture. J Hypertens. 1998;16(pt 2):2063-2074.
    • (1998) J Hypertens , vol.16 , Issue.2 PART , pp. 2063-2074
    • Andrade, M.C.1    Quinto, B.M.2    Carmona, A.K.3    Ribas, O.S.4    Boim, M.A.5    Schor, N.6    Casarini, D.E.7
  • 16
    • 0019378697 scopus 로고
    • Angiotensin converting enzyme in cultured endothelial cells and growth medium: Relationship to enzyme from kidney and plasma
    • Ching SF, Hayes LW, Slakey LL. Angiotensin converting enzyme in cultured endothelial cells and growth medium: relationship to enzyme from kidney and plasma. Biochim Biophys Acta. 1981;657:222-231.
    • (1981) Biochim Biophys Acta , vol.657 , pp. 222-231
    • Ching, S.F.1    Hayes, L.W.2    Slakey, L.L.3
  • 17
    • 0019458616 scopus 로고
    • Expression of angiotensin-converting enzyme activity in cultured pulmonary artery endothelial cells
    • Del Vecchio PJ, Smith JR. Expression of angiotensin-converting enzyme activity in cultured pulmonary artery endothelial cells. J Cell Physiol. 1981;108:337-345.
    • (1981) J Cell Physiol , vol.108 , pp. 337-345
    • Del Vecchio, P.J.1    Smith, J.R.2
  • 19
    • 0028231134 scopus 로고
    • Ontogeny of somatic angiotensin-converting enzyme
    • Yosipiv IV, Dipp S, el-Dahr SS. Ontogeny of somatic angiotensin-converting enzyme. Hypertension. 1994;23:369-374.
    • (1994) Hypertension , vol.23 , pp. 369-374
    • Yosipiv, I.V.1    Dipp, S.2    El-Dahr, S.S.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0017194947 scopus 로고
    • A sensitive fluorometric assay for serum angiotensin converting enzyme
    • Friedland J, Silverstein E. A sensitive fluorometric assay for serum angiotensin converting enzyme. Am J Clin Pathol. 1976;66:416-424.
    • (1976) Am J Clin Pathol , vol.66 , pp. 416-424
    • Friedland, J.1    Silverstein, E.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0021955447 scopus 로고
    • Structure and function of human angiotensin converting enzyme (kininase II)
    • Erdös EG. Skidgel RA. Structure and function of human angiotensin converting enzyme (kininase II). Biochem Soc Trans. 1985;13:42-44.
    • (1985) Biochem Soc Trans , vol.13 , pp. 42-44
    • Erdös, E.G.1    Skidgel, R.A.2
  • 27
    • 0343999620 scopus 로고
    • Isolation of two differentially glycosylated forms of peptidyl-dipeptidase A (angiotensin converting enzyme) from pig brain: A re-evaluation of their role in neuropeptide metabolism
    • Hooper NM, Turner AJ. Isolation of two differentially glycosylated forms of peptidyl-dipeptidase A (angiotensin converting enzyme) from pig brain: a re-evaluation of their role in neuropeptide metabolism. Biochem Pharmacol. 1987;51:11-14.
    • (1987) Biochem Pharmacol , vol.51 , pp. 11-14
    • Hooper, N.M.1    Turner, A.J.2
  • 29
    • 0023721888 scopus 로고
    • Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: Effect of chloride and pH
    • Ehlers MRW, Kirsh RE. Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH. Biochemistry 1988;27:188-201.
    • (1988) Biochemistry , vol.27 , pp. 188-201
    • Ehlers, M.R.W.1    Kirsh, R.E.2
  • 30
    • 0002732011 scopus 로고
    • Angiotensin I converting enzyme: Biochemistry and molecular biology
    • Laragh JH, Brenner BM, eds. New York, NY: Raven Press
    • Ehlers MRW, Riordan JF. Angiotensin I converting enzyme: Biochemistry and molecular biology. In: Laragh JH, Brenner BM, eds. Hypertension: Pathophysiology Diagnosis and Management. New York, NY: Raven Press; 1990:1217-1231.
    • (1990) Hypertension: Pathophysiology Diagnosis and Management , pp. 1217-1231
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 31
    • 0020053454 scopus 로고
    • Activation/inactivation of human ACE following chemical modifications of amino groups near the active site
    • Weare JA. Activation/inactivation of human ACE following chemical modifications of amino groups near the active site. Biochem Biophys Res Comm. 1982;104:1319-1326.
    • (1982) Biochem Biophys Res Comm , vol.104 , pp. 1319-1326
    • Weare, J.A.1
  • 32
    • 0017923176 scopus 로고
    • Properties of three different forms of angiotensin I-converting enzyme from human lung
    • Nishimura K, Yoshida N, Hiwada K, Ueda E, Kokubu T. Properties of three different forms of angiotensin I-converting enzyme from human lung. Biochem Biophys Acta. 1978;522:229-237.
    • (1978) Biochem Biophys Acta , vol.522 , pp. 229-237
    • Nishimura, K.1    Yoshida, N.2    Hiwada, K.3    Ueda, E.4    Kokubu, T.5
  • 33
    • 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
  • 37
    • 0027406861 scopus 로고
    • A comparison of the properties and enzymatic activities of three angiotensin processing enzymes; angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11
    • Welches WR, Brosnihan KB, Ferrario CM. A comparison of the properties and enzymatic activities of three angiotensin processing enzymes; angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11. Life Sci. 1993;52:1461-1480.
    • (1993) Life Sci , vol.52 , pp. 1461-1480
    • Welches, W.R.1    Brosnihan, K.B.2    Ferrario, C.M.3
  • 38
    • 0029926375 scopus 로고    scopus 로고
    • Angiotensin-(1-7) dilates canine coronary arteries through kinins and nitric oxide
    • Brosnihan KB, Li P, Ferrario CM. Angiotensin-(1-7) dilates canine coronary arteries through kinins and nitric oxide. Hypertension 1996;27(pt 2):523-528.
    • (1996) Hypertension , vol.27 , Issue.2 PART , pp. 523-528
    • Brosnihan, K.B.1    Li, P.2    Ferrario, C.M.3
  • 40
    • 0030062074 scopus 로고    scopus 로고
    • Renal actions of angiotensin-(1-7): In vivo and in vitro studies
    • Handa FK, Ferrario CM, Strandhoy JW. Renal actions of angiotensin-(1-7): in vivo and in vitro studies. Am J Physiol. 1996;270:F141-F147.
    • (1996) Am J Physiol , vol.270
    • Handa, F.K.1    Ferrario, C.M.2    Strandhoy, J.W.3
  • 41
    • 0031600505 scopus 로고    scopus 로고
    • Metabolism of angiotensin-(1-7) by angiotensin-converting enzyme
    • Chappell MC, Pirro NT, Sykes A, Ferrario CM. Metabolism of angiotensin-(1-7) by angiotensin-converting enzyme. Hypertension. 1998;31(pt 2):362-367.
    • (1998) Hypertension , vol.31 , Issue.2 PART , pp. 362-367
    • Chappell, M.C.1    Pirro, N.T.2    Sykes, A.3    Ferrario, C.M.4
  • 42
    • 0031954590 scopus 로고    scopus 로고
    • N-domain specific substrate and C-domain inhibitors of angiotensin I 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 I 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
  • 43
    • 0028967315 scopus 로고
    • The hemoregulatory peptide N-acetyl-Ser-Asp- Lys-Pro is a natural and specific substrate of N-terminal active site of human ACE
    • Rousseau A, Michaud A, Chauvet MT, Lenfand M, Corvol P. The hemoregulatory peptide N-acetyl-Ser-Asp- Lys-Pro is a natural and specific substrate of N-terminal active site of human ACE. 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    Lenfand, M.4    Corvol, P.5
  • 44
    • 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 T-T, Michelet S, Grognet J-M, Lenfant M, Corvol P, Ménard 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    Ménard, J.9
  • 45
    • 0029316877 scopus 로고
    • Renal physiology part 1: Structure and function
    • Bissinger RL. Renal physiology part 1: structure and function. Neonatal Network. 1995;14:9-20.
    • (1995) Neonatal Network , vol.14 , pp. 9-20
    • Bissinger, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.