메뉴 건너뛰기




Volumn 151, Issue 1-3, 2008, Pages 135-138

Angiotensin processing is partially carried out by carboxypeptidases in the rat mesenteric arterial bed perfusate

Author keywords

ACE 2; Carboxypeptidase A; Renin angiotensin system; Vasopeptidase

Indexed keywords

ANGIOTENSIN; ANGIOTENSIN I; ANGIOTENSIN II; ANGIOTENSIN[1-7]; ANGIOTENSIN[1-9]; CARBOXYPEPTIDASE A; CARBOXYPEPTIDASE C; DIPEPTIDYL CARBOXYPEPTIDASE; PROLINE CARBOXYPEPTIDASE; UNCLASSIFIED DRUG;

EID: 56249137597     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2008.09.003     Document Type: Article
Times cited : (7)

References (28)
  • 1
    • 0026409556 scopus 로고    scopus 로고
    • Differential regulation of angiotensin peptide levels in plasma and kidney of the rat
    • Campbell D.J., Lawrence A.C., Towrie A., Kladis A., and Valentijn A.J. Differential regulation of angiotensin peptide levels in plasma and kidney of the rat. Hypertension 18 (1999) 763-773
    • (1999) Hypertension , vol.18 , pp. 763-773
    • Campbell, D.J.1    Lawrence, A.C.2    Towrie, A.3    Kladis, A.4    Valentijn, A.J.5
  • 3
    • 0038163054 scopus 로고
    • The preparation and function of the hypertensin-converting enzyme
    • Skeggs L.T., Kahn J.R., and Shumway N.P. The preparation and function of the hypertensin-converting enzyme. J Exp Med 103 (1956) 295-299
    • (1956) J Exp Med , vol.103 , pp. 295-299
    • Skeggs, L.T.1    Kahn, J.R.2    Shumway, N.P.3
  • 4
    • 0025598309 scopus 로고
    • Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart
    • Urata H., Kinoshita A., Misono K.S., Bumpus F.M., and Husain A. Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart. J Biol Chem 265 (1990) 22348-22357
    • (1990) J Biol Chem , vol.265 , pp. 22348-22357
    • Urata, H.1    Kinoshita, A.2    Misono, K.S.3    Bumpus, F.M.4    Husain, A.5
  • 5
    • 6344246036 scopus 로고    scopus 로고
    • Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism
    • Rice G.I., Thomas D.A., Grant P.J., Turner A.J., and Hooper N.M. Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism. Biochem J 383 (2004) 45-51
    • (2004) Biochem J , vol.383 , pp. 45-51
    • Rice, G.I.1    Thomas, D.A.2    Grant, P.J.3    Turner, A.J.4    Hooper, N.M.5
  • 7
    • 0030971415 scopus 로고    scopus 로고
    • Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid. Inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin-converting enzyme by Ang-(1-9) formed by heart carboxypeptidase A-like activity
    • Kokkonen J.O., Saarinen J., and Kovanen P.T. Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid. Inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin-converting enzyme by Ang-(1-9) formed by heart carboxypeptidase A-like activity. Circulation 95 (1997) 1455-1463
    • (1997) Circulation , vol.95 , pp. 1455-1463
    • Kokkonen, J.O.1    Saarinen, J.2    Kovanen, P.T.3
  • 8
    • 0023749006 scopus 로고
    • Conversion of angiotensin I to angiotensin II by cathepsin A isoenzymes of porcine kidney
    • Miller J.J., Changaris D.G., and Levy R.S. Conversion of angiotensin I to angiotensin II by cathepsin A isoenzymes of porcine kidney. Biochem Biophys Res Commun 154 (1988) 122-129
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 122-129
    • Miller, J.J.1    Changaris, D.G.2    Levy, R.S.3
  • 10
    • 0034721906 scopus 로고    scopus 로고
    • A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase
    • Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., and Turner A.J. A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem 275 (2000) 33238-33243
    • (2000) J Biol Chem , vol.275 , pp. 33238-33243
    • Tipnis, S.R.1    Hooper, N.M.2    Hyde, R.3    Karran, E.4    Christie, G.5    Turner, A.J.6
  • 11
    • 0022480041 scopus 로고
    • Inhibition of angiotensin-converting enzyme by des-Leu10-angiotensin I: a potential mechanism of endogenous angiotensin-converting enzyme inhibition
    • Snyder R.A., and Wintroub B.U. Inhibition of angiotensin-converting enzyme by des-Leu10-angiotensin I: a potential mechanism of endogenous angiotensin-converting enzyme inhibition. Biochim Biophys Acta 871 (1986) 1-5
    • (1986) Biochim Biophys Acta , vol.871 , pp. 1-5
    • Snyder, R.A.1    Wintroub, B.U.2
  • 12
    • 28144445338 scopus 로고    scopus 로고
    • Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1-7) in regulation of cardiovascular function
    • Ferrario C.M., Trask A.J., and Jessup J.A. Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1-7) in regulation of cardiovascular function. Am J Physiol Heart Circ Physiol 289 (2005) H2281-2290
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Ferrario, C.M.1    Trask, A.J.2    Jessup, J.A.3
  • 13
    • 0026041902 scopus 로고
    • A survey of vasoactive peptide metabolizing enzymes in the rat mesenteric arterial bed perfusate
    • Oliveira E.B., Salgado M.C., and Turner A.J. A survey of vasoactive peptide metabolizing enzymes in the rat mesenteric arterial bed perfusate. Biochem Pharmacol 42 (1991) 1897-1904
    • (1991) Biochem Pharmacol , vol.42 , pp. 1897-1904
    • Oliveira, E.B.1    Salgado, M.C.2    Turner, A.J.3
  • 14
    • 17644434645 scopus 로고    scopus 로고
    • Purification and substrate specificity of an angiotensin converting elastase-2 from the rat mesenteric arterial bed perfusate
    • Paula C.A., Sousa M.V., Salgado M.C., and Oliveira E.B. Purification and substrate specificity of an angiotensin converting elastase-2 from the rat mesenteric arterial bed perfusate. Biochim Biophys Acta 1388 (1998) 227-238
    • (1998) Biochim Biophys Acta , vol.1388 , pp. 227-238
    • Paula, C.A.1    Sousa, M.V.2    Salgado, M.C.3    Oliveira, E.B.4
  • 17
    • 13544265463 scopus 로고    scopus 로고
    • Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2
    • Santos C.F., Greene A.S., Salgado M.C., and Oliveira E.B. Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2. Can J Physiol Pharmacol 82 (2004) 1000-1005
    • (2004) Can J Physiol Pharmacol , vol.82 , pp. 1000-1005
    • Santos, C.F.1    Greene, A.S.2    Salgado, M.C.3    Oliveira, E.B.4
  • 19
    • 0037439537 scopus 로고    scopus 로고
    • Development of intramolecularly quenched fluorescent peptides as substrates of angiotensin-converting enzyme 2
    • Yan Z.H., Ren K.J., Wang Y., Chen S., Brock T.A., and Rege A.A. Development of intramolecularly quenched fluorescent peptides as substrates of angiotensin-converting enzyme 2. Anal Biochem 312 (2003) 141-147
    • (2003) Anal Biochem , vol.312 , pp. 141-147
    • Yan, Z.H.1    Ren, K.J.2    Wang, Y.3    Chen, S.4    Brock, T.A.5    Rege, A.A.6
  • 20
    • 31944445995 scopus 로고    scopus 로고
    • Hydrolysis of angiotensin peptides by human angiotensin I-converting enzyme and resensitization of B2 kinin receptors
    • Chen Z., Tan F., Erdös E.G., and Deddish P.A. Hydrolysis of angiotensin peptides by human angiotensin I-converting enzyme and resensitization of B2 kinin receptors. Hypertension 46 (2005) 1368-1373
    • (2005) Hypertension , vol.46 , pp. 1368-1373
    • Chen, Z.1    Tan, F.2    Erdös, E.G.3    Deddish, P.A.4
  • 21
    • 0242569193 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence
    • Guy J.L., Jackson R.M., Acharya K.R., Sturrock E.D., Hooper N.M., and Turner A.J. Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence. Biochemistry 42 (2003) 13185-13192
    • (2003) Biochemistry , vol.42 , pp. 13185-13192
    • Guy, J.L.1    Jackson, R.M.2    Acharya, K.R.3    Sturrock, E.D.4    Hooper, N.M.5    Turner, A.J.6
  • 22
    • 0141988865 scopus 로고    scopus 로고
    • Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2
    • Zisman L.S., Keller R.S., Weaver B., Lin Q., Speth R., Bristow M.R., and Canver C.C. Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2. Circulation 108 (2003) 1707-1712
    • (2003) Circulation , vol.108 , pp. 1707-1712
    • Zisman, L.S.1    Keller, R.S.2    Weaver, B.3    Lin, Q.4    Speth, R.5    Bristow, M.R.6    Canver, C.C.7
  • 23
    • 0028786552 scopus 로고
    • Lysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation
    • Bonten E.J., Galjart N.J., Willemsen R., Usmany M., Vlak J.M., and d'Azzo A. Lysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation. J Biol Chem 270 (1995) 26441-26445
    • (1995) J Biol Chem , vol.270 , pp. 26441-26445
    • Bonten, E.J.1    Galjart, N.J.2    Willemsen, R.3    Usmany, M.4    Vlak, J.M.5    d'Azzo, A.6
  • 24
    • 0018126802 scopus 로고
    • Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney
    • Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., and Erdös E.G. Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney. J Biol Chem 253 (1978) 5927-5931
    • (1978) J Biol Chem , vol.253 , pp. 5927-5931
    • Odya, C.E.1    Marinkovic, D.V.2    Hammon, K.J.3    Stewart, T.A.4    Erdös, E.G.5
  • 25
    • 0019515695 scopus 로고
    • Prolylcarboxypeptidase (angiotensinase C) in human lung and cultured cells
    • Kumamoto K., Stewart T.A., Johnson A.R., and Erdös E.G. Prolylcarboxypeptidase (angiotensinase C) in human lung and cultured cells. J Clin Invest 67 (1981) 210-215
    • (1981) J Clin Invest , vol.67 , pp. 210-215
    • Kumamoto, K.1    Stewart, T.A.2    Johnson, A.R.3    Erdös, E.G.4
  • 26
  • 27
    • 3543030410 scopus 로고    scopus 로고
    • Cooperation between mast cell carboxypeptidase A and the chymase mouse mast cell protease 4 in the formation and degradation of angiotensin II
    • Lundequist A., Tchougounova E., Åbrink M., and Pejler G. Cooperation between mast cell carboxypeptidase A and the chymase mouse mast cell protease 4 in the formation and degradation of angiotensin II. J Biol Chem 279 (2004) 32339-32344
    • (2004) J Biol Chem , vol.279 , pp. 32339-32344
    • Lundequist, A.1    Tchougounova, E.2    Åbrink, M.3    Pejler, G.4
  • 28
    • 43749123507 scopus 로고    scopus 로고
    • Characterization of carboxypeptidase A6, an extracellular matrix peptidase
    • Lyons P.J., Callaway M.B., and Fricker L.D. Characterization of carboxypeptidase A6, an extracellular matrix peptidase. J Biol Chem 283 (2008) 7054-7063
    • (2008) J Biol Chem , vol.283 , pp. 7054-7063
    • Lyons, P.J.1    Callaway, M.B.2    Fricker, L.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.