메뉴 건너뛰기




Volumn 270, Issue 2 14-2, 1996, Pages

Impact of angiotensin-converting enzyme substrate conformation on fractional hydrolysis in lung

Author keywords

cyclophilin; cyclosporin A

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE;

EID: 0029918454     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1996.270.2.l251     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0001585104 scopus 로고
    • Effects of prolyl cis,trans isomerase on peptide hormone metabolism
    • Chung, A. Y. K., J. W. Ryan, and F. Valido. Effects of prolyl cis,trans isomerase on peptide hormone metabolism (Abstract). FASEB J. 5: A1579, 1991.
    • (1991) FASEB J. , vol.5
    • Chung, A.Y.K.1    Ryan, J.W.2    Valido, F.3
  • 2
    • 0001541596 scopus 로고
    • Comparison of the hydrolyses of two synthetic ACE substrates by rabbit lung in vivo
    • Cziraki, A., J. W. Ryan, I. Horvath, L. E. Fisher, J. Parkerson, and J. D. Catravas. Comparison of the hydrolyses of two synthetic ACE substrates by rabbit lung in vivo (Abstract). FASEB J. 9: A719, 1995.
    • (1995) FASEB J. , vol.9
    • Cziraki, A.1    Ryan, J.W.2    Horvath, I.3    Fisher, L.E.4    Parkerson, J.5    Catravas, J.D.6
  • 3
    • 0024313666 scopus 로고
    • Effect of transit time on metabolism of a pulmonary endothelial enzyme substrate
    • Heart Cire. Physiol. 26
    • Dawson, C. A., R. D. Bongard, D. A. Rickaby, J. H. Linehan, and D. L. Roerig. Effect of transit time on metabolism of a pulmonary endothelial enzyme substrate. Am. J. Physiol. 257 (Heart Cire. Physiol. 26): H853-H965, 1989.
    • (1989) Am. J. Physiol. , vol.257
    • Dawson, C.A.1    Bongard, R.D.2    Rickaby, D.A.3    Linehan, J.H.4    Roerig, D.L.5
  • 4
    • 0026719285 scopus 로고
    • Pulmonary angiotensin-converting enzyme substrate hydrolysis during exercise
    • Dupuis, J., C. A. Goresky, J. W. Ryan, J. L. Rouleau, and G. G. Bach. Pulmonary angiotensin-converting enzyme substrate hydrolysis during exercise. J. Appl. Physiol. 72: 1868-1886, 1992.
    • (1992) J. Appl. Physiol. , vol.72 , pp. 1868-1886
    • Dupuis, J.1    Goresky, C.A.2    Ryan, J.W.3    Rouleau, J.L.4    Bach, G.G.5
  • 5
    • 0028050923 scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and their effectors
    • Fischer, G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33: 1415-1436, 1994.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 6
    • 0021689983 scopus 로고
    • Conformational specificity of chymotrypsin proline-containing substrates
    • Fischer, G., H. Bang, E. Berger, and A. Schellenberger. Conformational specificity of chymotrypsin proline-containing substrates. Chim. Biophys. Acta 791: 87-97, 1984.
    • (1984) Chim. Biophys. Acta , vol.791 , pp. 87-97
    • Fischer, G.1    Bang, H.2    Berger, E.3    Schellenberger, A.4
  • 7
    • 0022555419 scopus 로고
    • Pharmacological aspects of metabolic processes in the pulmonary microcirculation
    • Gillis, C. N. Pharmacological aspects of metabolic processes in the pulmonary microcirculation. Am. Rev. Pharmacol. Toxicol. 26: 183-200, 1986.
    • (1986) Am. Rev. Pharmacol. Toxicol. , vol.26 , pp. 183-200
    • Gillis, C.N.1
  • 8
    • 13344263717 scopus 로고
    • The effect of left anterior descending (LAD) coronary occlusion on dynamically perfused coronary capillary surface area in dog
    • Horvath, I., A. Cziraki, J. Parkerson, and J. D. Catravas. The effect of left anterior descending (LAD) coronary occlusion on dynamically perfused coronary capillary surface area in dog (Abstract). FASEB J. 9: A847, 1995.
    • (1995) FASEB J. , vol.9
    • Horvath, I.1    Cziraki, A.2    Parkerson, J.3    Catravas, J.D.4
  • 9
    • 0025144288 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase activity of cyclophilin studied by one dimensional 1H nuclear magnetic spectroscopy
    • Hsu, V. L., R. E. Handschumacher, and I. M. Armitage. Peptidyl-prolyl cis-trans isomerase activity of cyclophilin studied by one dimensional 1H nuclear magnetic spectroscopy. J. Am. Chem. Soc. 112: 6745-6747, 1990.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6745-6747
    • Hsu, V.L.1    Handschumacher, R.E.2    Armitage, I.M.3
  • 10
    • 0022586797 scopus 로고
    • Direct NMR evidence that prolidase is specific for the trans isomer of imidopeptide substrates
    • King, G. K., C. R. Middlehurst, and P. W. Kuchel. Direct NMR evidence that prolidase is specific for the trans isomer of imidopeptide substrates. Biochemistry 25: 1054-1062, 1986.
    • (1986) Biochemistry , vol.25 , pp. 1054-1062
    • King, G.K.1    Middlehurst, C.R.2    Kuchel, P.W.3
  • 11
    • 0021102440 scopus 로고
    • Evidence showing that a proline-specific endopeptidase has an absolute requirement for a trans peptide bond immediately preceding the active bond
    • Lin, L.-N., and J. F. Brandts. Evidence showing that a proline-specific endopeptidase has an absolute requirement for a trans peptide bond immediately preceding the active bond. Biochemistry 22: 4480-4485, 1983.
    • (1983) Biochemistry , vol.22 , pp. 4480-4485
    • Lin, L.-N.1    Brandts, J.F.2
  • 12
    • 0018785339 scopus 로고
    • Evidence suggesting that some proteolytic enzymes may cleave only the trans form of the peptide bond
    • Lin, L. N., and J. F. Brandts. Evidence suggesting that some proteolytic enzymes may cleave only the trans form of the peptide bond. Biochemistry 18: 43-47, 1979.
    • (1979) Biochemistry , vol.18 , pp. 43-47
    • Lin, L.N.1    Brandts, J.F.2
  • 13
    • 0018789687 scopus 로고
    • Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyproline
    • Lin, L.-N., and J. F. Brandts. Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyproline. Biochemistry 18: 5037-5042, 1979.
    • (1979) Biochemistry , vol.18 , pp. 5037-5042
    • Lin, L.-N.1    Brandts, J.F.2
  • 14
    • 0024799211 scopus 로고
    • Hydrolysis of a synthetic angiotensin converting enzyme substrate in dog lungs
    • Heart Circ. Physiol. 26
    • . Linehan, J. H., T. A. Bronikowski, D. A. Rickaby, and C. A. Dawson. Hydrolysis of a synthetic angiotensin converting enzyme substrate in dog lungs. Am. J. Physiol. 257 (Heart Circ. Physiol. 26): H2006-H2016, 1989.
    • (1989) Am. J. Physiol. , vol.257
    • Linehan, J.H.1    Bronikowski, T.A.2    Rickaby, D.A.3    Dawson, C.A.4
  • 17
    • 0028904569 scopus 로고
    • In vivo measurements of pulmonary angiotensin-converting enzyme kinetics. I. Theory and error analysis
    • Markham, J., T. J. McCarthy, M. J. Welch, and D. P. Schuster. In vivo measurements of pulmonary angiotensin-converting enzyme kinetics. I. Theory and error analysis. J. Appl. Physiol. 78: 1158-1168, 1995.
    • (1995) J. Appl. Physiol. , vol.78 , pp. 1158-1168
    • Markham, J.1    McCarthy, T.J.2    Welch, M.J.3    Schuster, D.P.4
  • 18
    • 0029549997 scopus 로고
    • Cyclophilin facilitated bradykinin inactivation in the perfused rat lung
    • Merker, M. P., and C. A. Dawson. Cyclophilin facilitated bradykinin inactivation in the perfused rat lung. Biochem. Pharm. 50: 2085-2091, 1995.
    • (1995) Biochem. Pharm. , vol.50 , pp. 2085-2091
    • Merker, M.P.1    Dawson, C.A.2
  • 19
    • 0021276972 scopus 로고
    • Uptake and nature of the intracellular binding of cyclosporin a in a murine thymoma cell line, BW5147
    • Merker, M., and R. E. Handschumacher. Uptake and nature of the intracellular binding of cyclosporin A in a murine thymoma cell line, BW5147. J. Immunology 132: 1-6, 1984.
    • (1984) J. Immunology , vol.132 , pp. 1-6
    • Merker, M.1    Handschumacher, R.E.2
  • 20
    • 0027500781 scopus 로고
    • Angiotensin converting enzyme preferentially hydrolyzes the trans isomer of a proline containing substrate
    • Merker, M. P., C. A. Dawson, R. Bongard, D. Roerig, S. Haworth, and J. Linehan. Angiotensin converting enzyme preferentially hydrolyzes the trans isomer of a proline containing substrate. J. Appl. Physiol. 75: 1519-1524, 1993.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 1519-1524
    • Merker, M.P.1    Dawson, C.A.2    Bongard, R.3    Roerig, D.4    Haworth, S.5    Linehan, J.6
  • 21
    • 0023228946 scopus 로고
    • Effect of flow and surface area on angiotensin converting enzyme activity in rabbit lungs
    • Moalli, R., B. R. Pitt, and C. N. Gillis. Effect of flow and surface area on angiotensin converting enzyme activity in rabbit lungs. J. Appl. Physiol. 62: 2042-2050, 1987.
    • (1987) J. Appl. Physiol. , vol.62 , pp. 2042-2050
    • Moalli, R.1    Pitt, B.R.2    Gillis, C.N.3
  • 22
    • 0023808703 scopus 로고
    • Selective effect of phorbol ester on serotonin removal and ACE activity in rabbit lungs
    • Myers, C. L., and B. R. Pitt. Selective effect of phorbol ester on serotonin removal and ACE activity in rabbit lungs. J. Appl. Physiol. 65: 377-384, 1988.
    • (1988) J. Appl. Physiol. , vol.65 , pp. 377-384
    • Myers, C.L.1    Pitt, B.R.2
  • 24
    • 0023280383 scopus 로고
    • Correlation of pulmonary ACE activity and capillary surface area during postnatal development
    • Pitt, B. R., G. Lister, P. Davies, and L. Reid. Correlation of pulmonary ACE activity and capillary surface area during postnatal development. J. Appl. Physiol. 62: 2031-2041, 1987.
    • (1987) J. Appl. Physiol. , vol.62 , pp. 2031-2041
    • Pitt, B.R.1    Lister, G.2    Davies, P.3    Reid, L.4
  • 25
    • 0020111712 scopus 로고
    • Conformational and acidbase equilibria of captopril in aqueous solution
    • Rabenstein, D. L., and A. A. Isab. Conformational and acidbase equilibria of captopril in aqueous solution. Anal. Chem. 54: 526-529, 1982.
    • (1982) Anal. Chem. , vol.54 , pp. 526-529
    • Rabenstein, D.L.1    Isab, A.A.2
  • 26
    • 0023189776 scopus 로고
    • Effects of gas composition and pH on kinetics of lung angiotensin converting enzyme
    • Rickaby, D. A., R. D. Bongard, M. J. Tristani, J. H. Linehan, and C. A. Dawson. Effects of gas composition and pH on kinetics of lung angiotensin converting enzyme. J. Appl. Physiol. 62: 1216-1221, 1987.
    • (1987) J. Appl. Physiol. , vol.62 , pp. 1216-1221
    • Rickaby, D.A.1    Bongard, R.D.2    Tristani, M.J.3    Linehan, J.H.4    Dawson, C.A.5
  • 27
    • 0027184839 scopus 로고
    • Cyclosporin binding proteins. Identification, distribution, function and relation to FK binding proteins
    • Ryffel, B. Cyclosporin binding proteins. Identification, distribution, function and relation to FK binding proteins. Biochem. Pharm. 46: 1-12, 1993.
    • (1993) Biochem. Pharm. , vol.46 , pp. 1-12
    • Ryffel, B.1
  • 29
    • 0028969060 scopus 로고
    • In vivo measurements of pulmonary angiotensin converting enzyme kinetics. II. Implementation and application
    • Schuster, D. P., T. J. McCarthy, M. J. Welch, S. Holmberg, P. Sandiford, and J. Markham. In vivo measurements of pulmonary angiotensin converting enzyme kinetics. II. Implementation and application. J. Appl. Physiol. 78: 1169-1178, 1995.
    • (1995) J. Appl. Physiol. , vol.78 , pp. 1169-1178
    • Schuster, D.P.1    McCarthy, T.J.2    Welch, M.J.3    Holmberg, S.4    Sandiford, P.5    Markham, J.6
  • 30
    • 0026701332 scopus 로고
    • Membrane-bound aminopeptidase P from bovine lung
    • Simmons, W. H., and A. T. Orawski. Membrane-bound aminopeptidase P from bovine lung. J. Biol. Chem. 267: 4897-4903, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4897-4903
    • Simmons, W.H.1    Orawski, A.T.2
  • 31
    • 0025115970 scopus 로고
    • cis-trans isomerization of an angiotensin converting enzyme inhibitor. An enzyme kinetic and nuclear magnetic resonance study
    • Skoglof, A., I. Nilsson, S. Gustafsson, J. Deinum, and P. Gothe. cis-trans isomerization of an angiotensin converting enzyme inhibitor. An enzyme kinetic and nuclear magnetic resonance study. Biochim Biophys. Acta 1041: 22-30, 1990.
    • (1990) Biochim Biophys. Acta , vol.1041 , pp. 22-30
    • Skoglof, A.1    Nilsson, I.2    Gustafsson, S.3    Deinum, J.4    Gothe, P.5
  • 32
    • 0026355711 scopus 로고
    • Effects of blood flow on lung ACE kinetics: Evidence for microvascular recruitment
    • Toivonen, H. J., and J. D. Catravas. Effects of blood flow on lung ACE kinetics: evidence for microvascular recruitment. J. Appl. Physiol. 71: 2244-2254, 1991.
    • (1991) J. Appl. Physiol. , vol.71 , pp. 2244-2254
    • Toivonen, H.J.1    Catravas, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.