메뉴 건너뛰기




Volumn 363, Issue 2, 2007, Pages 255-262

Determination of angiotensin I-converting enzyme activity in cell culture using fluorescence resonance energy transfer peptides

Author keywords

Angiotensin I converting enzyme; Aorta smooth muscle cells (ASMC); Cell culture; CHO cells; Enzyme activity; Fluorescence resonance energy transfer (FRET) peptides; Fluorimetric assay

Indexed keywords

CELL CULTURE; CELLS; ENERGY TRANSFER; FORSTER RESONANCE ENERGY TRANSFER; HYDROLYSIS; MUSCLE; PEPTIDES; RESONANCE;

EID: 33947278905     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.01.020     Document Type: Article
Times cited : (13)

References (32)
  • 1
    • 0027244532 scopus 로고
    • Zinc metallopeptidases: active site structure and design of selective and mixed inhibitors: new approaches in the search for analgesics and anti-hypertensives
    • Roques B.P. Zinc metallopeptidases: active site structure and design of selective and mixed inhibitors: new approaches in the search for analgesics and anti-hypertensives. Biochem. Soc. Trans. 3 (1993) 678-685
    • (1993) Biochem. Soc. Trans. , vol.3 , pp. 678-685
    • Roques, B.P.1
  • 2
    • 0038163054 scopus 로고
    • Preparation and function of the hypertensin-converting enzyme
    • Skeggs L.T., Kahn J.R., and Shumway N.P. 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
  • 3
    • 0014957830 scopus 로고
    • A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin
    • Yang H.Y.T., Erdos E.G., and Levin Y. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. Biophys. Acta 214 (1970) 374-376
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 374-376
    • Yang, H.Y.T.1    Erdos, E.G.2    Levin, Y.3
  • 6
    • 0025824349 scopus 로고
    • Structure of the angiotensin I-converting enzyme gene. Two alternate promoters correspond to evolutionary steps of a duplicated gene
    • Hubert C., Houot A.M., Corvol P., and Soubrier F. Structure of the angiotensin I-converting enzyme gene. Two alternate promoters correspond to evolutionary steps of a duplicated gene. J. Biol. Chem. 266 (1991) 15377-15383
    • (1991) J. Biol. Chem. , vol.266 , pp. 15377-15383
    • Hubert, C.1    Houot, A.M.2    Corvol, P.3    Soubrier, F.4
  • 7
    • 0025756812 scopus 로고
    • The mRNAs encoding the two angiotensin-converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initiation sites
    • Kumar R.S., Thekkumkara T.J., and Sen G.C. The mRNAs encoding the two angiotensin-converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initiation sites. J. Biol. Chem. 266 (1991) 3854-3862
    • (1991) J. Biol. Chem. , vol.266 , pp. 3854-3862
    • Kumar, R.S.1    Thekkumkara, T.J.2    Sen, G.C.3
  • 8
    • 0024473131 scopus 로고
    • The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme
    • Lattion A.L., Soubrier F., Allegrini J., Hubert C., Corvol P., and Alhenc-Gelas F. The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett. 252 (1989) 99-104
    • (1989) FEBS Lett. , vol.252 , pp. 99-104
    • Lattion, A.L.1    Soubrier, F.2    Allegrini, J.3    Hubert, C.4    Corvol, P.5    Alhenc-Gelas, F.6
  • 9
    • 0042908657 scopus 로고
    • Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme
    • Ehlers M.R.W., Fox E.A., Strydom D.J., and Riordan J.F. Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. USA 86 (1989) 7741-7745
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7741-7745
    • Ehlers, M.R.W.1    Fox, E.A.2    Strydom, D.J.3    Riordan, J.F.4
  • 10
    • 0015139369 scopus 로고
    • Concentrations of angiotensin-converting enzyme in tissues of the rat
    • Cushman D.W., and Cheung H.S. Concentrations of angiotensin-converting enzyme in tissues of the rat. Biochim. Biophys. Acta 250 (1971) 261-265
    • (1971) Biochim. Biophys. Acta , vol.250 , pp. 261-265
    • Cushman, D.W.1    Cheung, H.S.2
  • 12
    • 0035122434 scopus 로고    scopus 로고
    • Angiotensin converting enzymes from human urine of mild hypertensive untreated patients resemble the N-terminal fragment of human angiotensin I-converting enzyme
    • Casarini D.E., Plavinik F.L., Zanella M.T., Marson O., Krieger J.E., Hirata I.Y., and Stella R.C. Angiotensin converting enzymes from human urine of mild hypertensive untreated patients resemble the N-terminal fragment of human angiotensin I-converting enzyme. Int. J. Biochem. Cell Biol. 33 (2001) 75-85
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 75-85
    • Casarini, D.E.1    Plavinik, F.L.2    Zanella, M.T.3    Marson, O.4    Krieger, J.E.5    Hirata, I.Y.6    Stella, R.C.7
  • 15
    • 0034713884 scopus 로고    scopus 로고
    • Peptidase specificity characterization of C- and N- terminal catalytic sites of angiotensin I-converting enzyme
    • Araújo M.C., Melo R.L., Cesari M.H., Juliano M.A., Juliano L., and Carmona A.K. Peptidase specificity characterization of C- and N- terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry 39 (2000) 8519-8525
    • (2000) Biochemistry , vol.39 , pp. 8519-8525
    • Araújo, M.C.1    Melo, R.L.2    Cesari, M.H.3    Juliano, M.A.4    Juliano, L.5    Carmona, A.K.6
  • 16
    • 10844240710 scopus 로고    scopus 로고
    • Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides for defining substrate specificity of the angiotensin I-converting enzyme and development of selective C-domain substrates
    • Bersanetti P.A., Andrade M.C., Casarini D.E., Juliano M.A., Nchinda A.T., Sturrock E.D., Juliano L., and Carmona A.K. Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides for defining substrate specificity of the angiotensin I-converting enzyme and development of selective C-domain substrates. Biochemistry 43 (2004) 15729-15736
    • (2004) Biochemistry , vol.43 , pp. 15729-15736
    • Bersanetti, P.A.1    Andrade, M.C.2    Casarini, D.E.3    Juliano, M.A.4    Nchinda, A.T.5    Sturrock, E.D.6    Juliano, L.7    Carmona, A.K.8
  • 18
  • 20
    • 33947229426 scopus 로고    scopus 로고
    • R.J. Leatherbarrow, Grafit, version 5.0, Erithacus Software Ltd., Staines, U.K. (1992).
  • 22
    • 0025788169 scopus 로고
    • Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes
    • Ehlers M.R.W., and Riordan J.F. Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry 30 (1991) 7118-7126
    • (1991) Biochemistry , vol.30 , pp. 7118-7126
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 23
    • 0025739667 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme are both catalytically active
    • Wei L., Alhenc-Gelas F., Corvol P., and Clauser E. The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266 (1991) 9002-9008
    • (1991) J. Biol. Chem. , vol.266 , pp. 9002-9008
    • Wei, L.1    Alhenc-Gelas, F.2    Corvol, P.3    Clauser, E.4
  • 24
    • 0027247370 scopus 로고
    • Characterization of a secretase activity which releases angiotensin-converting enzyme from the membrane
    • Oppong S.Y., and Hooper N.M. Characterization of a secretase activity which releases angiotensin-converting enzyme from the membrane. Biochem. J. 292 (1993) 597-603
    • (1993) Biochem. J. , vol.292 , pp. 597-603
    • Oppong, S.Y.1    Hooper, N.M.2
  • 25
    • 0030790474 scopus 로고    scopus 로고
    • Differences in the hydrolysis of enkephalin congeners by the two domains of angiotensin converting enzyme
    • Deddish P.A., Jackman H.L., Skidgel R.A., and Erdos E.G. Differences in the hydrolysis of enkephalin congeners by the two domains of angiotensin converting enzyme. Biochem. Pharmacol. 53 (1997) 1459-1463
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1459-1463
    • Deddish, P.A.1    Jackman, H.L.2    Skidgel, R.A.3    Erdos, E.G.4
  • 26
    • 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., and Corvol P. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267 (1992) 13398-13405
    • (1992) J. Biol. Chem. , vol.267 , pp. 13398-13405
    • Wei, L.1    Clauser, E.2    Alhenc-Gelas, F.3    Corvol, P.4
  • 27
    • 0037014664 scopus 로고    scopus 로고
    • Temperature induced selective death of the C-domain within angiotensin-converting enzyme molecule
    • Voronov S., Zueva N., Orlov V., Arutyunyan A., and Kost O. Temperature induced selective death of the C-domain within angiotensin-converting enzyme molecule. FEBS Lett. 522 (2002) 77-82
    • (2002) FEBS Lett. , vol.522 , pp. 77-82
    • Voronov, S.1    Zueva, N.2    Orlov, V.3    Arutyunyan, A.4    Kost, O.5
  • 28
    • 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., and 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. 268 (1993) 9496-9503
    • (1993) J. Biol. Chem. , vol.268 , pp. 9496-9503
    • Jaspard, E.1    Wei, L.2    Alhenc-Gelas, F.3
  • 29
    • 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 M.T., Lenfant M., and 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. 270 (1995) 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
  • 30
    • 0031954590 scopus 로고    scopus 로고
    • N-Domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: angiotensin-( 1-7) and keto-ACE
    • Deddish P.A., Marcic B., Jackman H.L., Wang H.Z., Sikgel R.A., and Erdos E.G. N-Domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: angiotensin-( 1-7) and keto-ACE. Hypertension 31 (1998) 912-917
    • (1998) Hypertension , vol.31 , pp. 912-917
    • Deddish, P.A.1    Marcic, B.2    Jackman, H.L.3    Wang, H.Z.4    Sikgel, R.A.5    Erdos, E.G.6
  • 31
    • 23644435174 scopus 로고    scopus 로고
    • The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity
    • Woodman Z.L., Schwager S.L., Redelinghuys P., Carmona A.K., Ehlers M.R., and Sturrock E.D. The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity. Biochem. J. 389 (2005) 739-744
    • (2005) Biochem. J. , vol.389 , pp. 739-744
    • Woodman, Z.L.1    Schwager, S.L.2    Redelinghuys, P.3    Carmona, A.K.4    Ehlers, M.R.5    Sturrock, E.D.6
  • 32
    • 27144540407 scopus 로고    scopus 로고
    • Continuous real-time measurement of tumor necrosis factor-alpha converting enzyme activity on live cells
    • Alvarez-Iglesias M., Wayne G., O'Dea K.P., Amour A., and Takata M. Continuous real-time measurement of tumor necrosis factor-alpha converting enzyme activity on live cells. Lab. Invest. 85 (2005) 1440-1448
    • (2005) Lab. Invest. , vol.85 , pp. 1440-1448
    • Alvarez-Iglesias, M.1    Wayne, G.2    O'Dea, K.P.3    Amour, A.4    Takata, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.