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Volumn 400, Issue 1, 2006, Pages 169-178

Polymerization of human angiotensinogen: Insights into its structural mechanism and functional significance

Author keywords

Angiotensinogen; Hypertension; Non inhibitory; Polymers; Renin; Serpin

Indexed keywords

BLOOD; ELECTRON MICROSCOPY; MOLECULAR STRUCTURE; MOLECULAR WEIGHT; PLASMAS; POLYMERIZATION;

EID: 33751087751     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060444     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 0020545825 scopus 로고
    • Angiotensinogen is related to the antitrypsin-antithrombin-ovalbumin family
    • Doolittle, R. F. (1983) Angiotensinogen is related to the antitrypsin-antithrombin-ovalbumin family. Science 222, 417-419
    • (1983) Science , vol.222 , pp. 417-419
    • Doolittle, R.F.1
  • 2
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • Irving, J. A., Pike, R. N., Lesk, A. M. and Whisstock, J. C. (2000) Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res. 10, 1845-1864
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 3
    • 0024430428 scopus 로고
    • Ovalbumin and angiotensinogen lack serpin S → R conformational change
    • Stein, P. E., Tewksbury, D. A. and Carrell, R. W. (1989) Ovalbumin and angiotensinogen lack serpin S → R conformational change. Biochem. J. 262, 103-107
    • (1989) Biochem. J. , vol.262 , pp. 103-107
    • Stein, P.E.1    Tewksbury, D.A.2    Carrell, R.W.3
  • 4
    • 0028803776 scopus 로고
    • Pigment epithelium-derived factor behaves like a noninhibitory serpin. Neurotrophic activity does not require the serpin reactive loop
    • Becerra, S. P., Sagasti, A., Spinella, P. and Notario, V. (1995) Pigment epithelium-derived factor behaves like a noninhibitory serpin. Neurotrophic activity does not require the serpin reactive loop. J. Biol. Chem. 270, 25992-25999
    • (1995) J. Biol. Chem. , vol.270 , pp. 25992-25999
    • Becerra, S.P.1    Sagasti, A.2    Spinella, P.3    Notario, V.4
  • 5
    • 0029058971 scopus 로고
    • The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin
    • Pemberton, P. A., Wong, D. T., Gibson, H. L., Kiefer, M. C., Fitzpatrick, P. A., Sager, R. and Barr, P. J. (1995) The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin. J. Biol Chem. 270, 15832-15837
    • (1995) J. Biol Chem. , vol.270 , pp. 15832-15837
    • Pemberton, P.A.1    Wong, D.T.2    Gibson, H.L.3    Kiefer, M.C.4    Fitzpatrick, P.A.5    Sager, R.6    Barr, P.J.7
  • 6
    • 85047676452 scopus 로고
    • Kinetics of the human renin and human substrate reaction
    • Gould, A. B. and Green, D. (1971) Kinetics of the human renin and human substrate reaction. Cardiovasc. Res. 5, 86-89
    • (1971) Cardiovasc. Res. , vol.5 , pp. 86-89
    • Gould, A.B.1    Green, D.2
  • 7
    • 0017319491 scopus 로고
    • The biochemistry of the renin-angiotensin system and its role in hypertension
    • Skeggs, L. T., Dorer, F. E., Kahn, J. R., Lentz, K. E. and Levine, M. (1976) The biochemistry of the renin-angiotensin system and its role in hypertension. Am. J. Med. 60, 737-748
    • (1976) Am. J. Med. , vol.60 , pp. 737-748
    • Skeggs, L.T.1    Dorer, F.E.2    Kahn, J.R.3    Lentz, K.E.4    Levine, M.5
  • 9
    • 0017864751 scopus 로고
    • Characterization of human angiotensinogen
    • Tewksbury, D. A., Frome, W. L. and Dumas, M. L. (1978) Characterization of human angiotensinogen. J. Biol. Chem. 253, 3817-3820
    • (1978) J. Biol. Chem. , vol.253 , pp. 3817-3820
    • Tewksbury, D.A.1    Frome, W.L.2    Dumas, M.L.3
  • 10
    • 0023102985 scopus 로고
    • The rapid purification and partial characterization of human serum angiotensinogen
    • Campbell, C. J., Charlton, P. A., Grinham, C. J., Mooney, C. J. and Pendlebury, J. E. (1987) The rapid purification and partial characterization of human serum angiotensinogen. Biochem. J. 243, 121-126
    • (1987) Biochem. J. , vol.243 , pp. 121-126
    • Campbell, C.J.1    Charlton, P.A.2    Grinham, C.J.3    Mooney, C.J.4    Pendlebury, J.E.5
  • 11
    • 0017586140 scopus 로고
    • Chromatographic separation of multiple renin substrates in women: Effect of pregnancy and oral contraceptives
    • Gordon, D. B. and Sachin, I. N. (1977) Chromatographic separation of multiple renin substrates in women: effect of pregnancy and oral contraceptives. Proc. Soc. Exp. Biol. Med. 156, 461-464
    • (1977) Proc. Soc. Exp. Biol. Med. , vol.156 , pp. 461-464
    • Gordon, D.B.1    Sachin, I.N.2
  • 12
    • 0020411938 scopus 로고
    • High molecular weight angiotensinogen levels in hypertensive pregnant women
    • Tewksbury, D. A. and Dart, R. A. (1982) High molecular weight angiotensinogen levels in hypertensive pregnant women. Hypertension 4, 729-734
    • (1982) Hypertension , vol.4 , pp. 729-734
    • Tewksbury, D.A.1    Dart, R.A.2
  • 13
    • 0022457626 scopus 로고
    • Changing renin substrates in human pregnancy
    • Tetlow, H. J. and Broughton-Pipkin, F. (1986) Changing renin substrates in human pregnancy. J. Endocrinol. 109, 257-262
    • (1986) J. Endocrinol. , vol.109 , pp. 257-262
    • Tetlow, H.J.1    Broughton-Pipkin, F.2
  • 14
    • 0027771406 scopus 로고
    • Regional distribution of the angiotensinogens in human placentae
    • Lenz, T., Sealey, J. E. and Tewksbury, D. A. (1993) Regional distribution of the angiotensinogens in human placentae. Placenta 14, 695-699
    • (1993) Placenta , vol.14 , pp. 695-699
    • Lenz, T.1    Sealey, J.E.2    Tewksbury, D.A.3
  • 15
    • 0033870896 scopus 로고    scopus 로고
    • Quantification and characterization of pregnancy-associated complexes of angiotensinogen and the proform of eosinophil major basic protein in serum and amniotic fluid
    • Christiansen, M., Jaliashvili, I., Overgaard, M. T., Ensinger, C., Obrist, P. and Oxvig, C. (2000) Quantification and characterization of pregnancy-associated complexes of angiotensinogen and the proform of eosinophil major basic protein in serum and amniotic fluid. Clin. Chem. 46, 1099-1105
    • (2000) Clin. Chem. , vol.46 , pp. 1099-1105
    • Christiansen, M.1    Jaliashvili, I.2    Overgaard, M.T.3    Ensinger, C.4    Obrist, P.5    Oxvig, C.6
  • 16
    • 0024521689 scopus 로고
    • Immunochemical comparison of high molecular weight angiotensinogen from amniotic fluid, plasma of men, and plasma of pregnant women
    • Tewksbury, D. A. and Tryon, E. S. (1989) Immunochemical comparison of high molecular weight angiotensinogen from amniotic fluid, plasma of men, and plasma of pregnant women. Am. J. Hypertens. 2, 411-413
    • (1989) Am. J. Hypertens. , vol.2 , pp. 411-413
    • Tewksbury, D.A.1    Tryon, E.S.2
  • 17
    • 0029907068 scopus 로고    scopus 로고
    • Quantitation of five forms of high molecular weight angiotensinogen from human placenta
    • Tewksbury, D. A. (1996) Quantitation of five forms of high molecular weight angiotensinogen from human placenta. Am. J. Hypertens. 9, 1029-1034
    • (1996) Am. J. Hypertens. , vol.9 , pp. 1029-1034
    • Tewksbury, D.A.1
  • 18
    • 0037528713 scopus 로고    scopus 로고
    • Characterization of different high molecular weight angiotensinogen forms
    • Ramaha, A., Celerier, J. and Patston, P. A. (2003) Characterization of different high molecular weight angiotensinogen forms. Am. J. Hypertens. 16, 478-483
    • (2003) Am. J. Hypertens. , vol.16 , pp. 478-483
    • Ramaha, A.1    Celerier, J.2    Patston, P.A.3
  • 20
    • 0034112580 scopus 로고    scopus 로고
    • Quantitation of the five forms of plasma high molecular weight angiotensinogen in women with pregnancy-induced hypertension
    • Tewksbury, D. A., Goodman, J. R., Kaiser, S. J., Burrill, R. E. and Brown, H. L. (2000) Quantitation of the five forms of plasma high molecular weight angiotensinogen in women with pregnancy-induced hypertension. Am. J. Hypertens. 13, 221-225
    • (2000) Am. J. Hypertens. , vol.13 , pp. 221-225
    • Tewksbury, D.A.1    Goodman, J.R.2    Kaiser, S.J.3    Burrill, R.E.4    Brown, H.L.5
  • 21
    • 17044445816 scopus 로고    scopus 로고
    • Characterization of a human angiotensinogen cleaved in its reactive center loop by a proteolytic activity from Chinese hamster ovary cells
    • Celerier, J., Schmid, G., Le Caer, J. P., Gimenez-Roqueplo, A. P., Bur, D., Friedlein, A., Langen, H., Corvol, P. and Jeunemaitre, X. (2000) Characterization of a human angiotensinogen cleaved in its reactive center loop by a proteolytic activity from Chinese hamster ovary cells. J. Biol. Chem. 275, 10648-10654
    • (2000) J. Biol. Chem. , vol.275 , pp. 10648-10654
    • Celerier, J.1    Schmid, G.2    Le Caer, J.P.3    Gimenez-Roqueplo, A.P.4    Bur, D.5    Friedlein, A.6    Langen, H.7    Corvol, P.8    Jeunemaitre, X.9
  • 22
    • 0021045008 scopus 로고
    • Differences in the kinetic rate constants of normal and high molecular weight renin substrate from term pregnancy human plasma
    • Shionoiri, H., Gotoh, E., Kaneko, Y., Eggena, P. and Sambhi, M. P. (1983) Differences in the kinetic rate constants of normal and high molecular weight renin substrate from term pregnancy human plasma. Endocrinol. Jpn. 30, 731-736
    • (1983) Endocrinol. Jpn. , vol.30 , pp. 731-736
    • Shionoiri, H.1    Gotoh, E.2    Kaneko, Y.3    Eggena, P.4    Sambhi, M.P.5
  • 23
    • 0028829397 scopus 로고
    • Kinetic analysis of the reaction of human renin with human high and low molecular weight angiotensinogen
    • Tryon, E. S. and Tewksbury, D. A. (1995) Kinetic analysis of the reaction of human renin with human high and low molecular weight angiotensinogen. Hypertens. Preg. 14, 327-338
    • (1995) Hypertens. Preg. , vol.14 , pp. 327-338
    • Tryon, E.S.1    Tewksbury, D.A.2
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 0023700976 scopus 로고
    • Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites
    • Bruch, M., Weiss, V. and Engel, J. (1988) Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites. J. Biol. Chem. 263, 16626-16630
    • (1988) J. Biol. Chem. , vol.263 , pp. 16626-16630
    • Bruch, M.1    Weiss, V.2    Engel, J.3
  • 30
    • 0027295822 scopus 로고
    • α1-antitrypsin Siiyama (Ser53→Phe). Further evidence for intracellular loop-sheet polymerization
    • Lomas, D. A., Finch, J. T., Seyama, K., Nukiwa, T. and Carrell, R. W. (1993) α1-antitrypsin Siiyama (Ser53→Phe). Further evidence for intracellular loop-sheet polymerization. J. Biol. Chem. 268, 15333-15335
    • (1993) J. Biol. Chem. , vol.268 , pp. 15333-15335
    • Lomas, D.A.1    Finch, J.T.2    Seyama, K.3    Nukiwa, T.4    Carrell, R.W.5
  • 32
    • 0026755363 scopus 로고
    • The mechanism of Z α1-antitrypsin accumulation in the liver
    • Lomas, D. A., Evans, D. L., Finch, J. T. and Carrell, R. W. (1992) The mechanism of Z α1-antitrypsin accumulation in the liver. Nature 357, 605-607
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 36
    • 0034721790 scopus 로고    scopus 로고
    • Pathogenic α1-antitrypsin polymers are formed by reactive loop-β-sheet a linkage
    • Sivasothy, P., Dafforn, T. R., Gettins, P. G. and Lomas, D. A. (2000) Pathogenic α1-antitrypsin polymers are formed by reactive loop-β-sheet A linkage. J. Biol. Chem. 275, 33663-33668
    • (2000) J. Biol. Chem. , vol.275 , pp. 33663-33668
    • Sivasothy, P.1    Dafforn, T.R.2    Gettins, P.G.3    Lomas, D.A.4
  • 37
    • 0025742788 scopus 로고
    • Serpin tertiary structure transformation
    • Stein, P. and Chothia, C. (1991) Serpin tertiary structure transformation. J. Mol. Biol. 221, 615-621
    • (1991) J. Mol. Biol. , vol.221 , pp. 615-621
    • Stein, P.1    Chothia, C.2
  • 40
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn→Asp)
    • Bruce, D., Perry, D. J., Borg, J. Y., Carrell, R. W. and Wardell, M. R. (1994) Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn→Asp) J. Clin. Invest. 94, 2265-2274
    • (1994) J. Clin. Invest. , vol.94 , pp. 2265-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 41
    • 0028773279 scopus 로고
    • Biological implications of a 3A structure of dimeric antithrombin
    • Carrell, R. W., Stein, P. E., Fermi, G. and Wardell, M. R. (1994) Biological implications of a 3A structure of dimeric antithrombin. Structure 2, 257-270
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 42
    • 0029012309 scopus 로고
    • α1-Antitrypsin Mmalton (Phe52Δ) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization
    • Lomas, D. A., Elliott, P. R., Sidhar, S. K., Foreman, R. C., Finch, J. T., Cox, D. W., Whisstock, J. C. and Carrell, R. W. (1995) α1-Antitrypsin Mmalton (Phe52Δ) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization. J. Biol. Chem. 270, 16864-16870
    • (1995) J. Biol. Chem. , vol.270 , pp. 16864-16870
    • Lomas, D.A.1    Elliott, P.R.2    Sidhar, S.K.3    Foreman, R.C.4    Finch, J.T.5    Cox, D.W.6    Whisstock, J.C.7    Carrell, R.W.8
  • 43
    • 0033081498 scopus 로고    scopus 로고
    • The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion
    • Sharp, A. M., Stein, P. E., Pannu, N. S., Carrell, R. W., Berkenpas, M. B., Ginsburg, D., Lawrence, D. A. and Read, R. J. (1999) The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure 7, 111-118
    • (1999) Structure , vol.7 , pp. 111-118
    • Sharp, A.M.1    Stein, P.E.2    Pannu, N.S.3    Carrell, R.W.4    Berkenpas, M.B.5    Ginsburg, D.6    Lawrence, D.A.7    Read, R.J.8
  • 44
    • 0025226070 scopus 로고
    • Structural transition of α1-antitrypsin by a peptide sequentially similar to β-strand s4A
    • Schulze, A. J., Baumann, U., Knof, S., Jaeger, E., Huber, R. and Laurell, C. B. (1990) Structural transition of α1-antitrypsin by a peptide sequentially similar to β-strand s4A. Eur. J. Biochem. 194, 51-56
    • (1990) Eur. J. Biochem. , vol.194 , pp. 51-56
    • Schulze, A.J.1    Baumann, U.2    Knof, S.3    Jaeger, E.4    Huber, R.5    Laurell, C.B.6
  • 45
    • 0036324175 scopus 로고    scopus 로고
    • Release and degradation of angiotensin I and angiotensin II from angiotensinogen by neutrophil serine proteinases
    • Ramaha, A. and Patston, P. A. (2002) Release and degradation of angiotensin I and angiotensin II from angiotensinogen by neutrophil serine proteinases. Arch. Biochem. Biophys. 397, 77-83
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 77-83
    • Ramaha, A.1    Patston, P.A.2
  • 46
    • 0037235357 scopus 로고    scopus 로고
    • Detection of a receptor for angiotensinogen on placental cells
    • Tewksbury, D. A., Pan, N. and Kaiser, S. J. (2003) Detection of a receptor for angiotensinogen on placental cells. Am. J. Hypertens. 16, 59-62
    • (2003) Am. J. Hypertens. , vol.16 , pp. 59-62
    • Tewksbury, D.A.1    Pan, N.2    Kaiser, S.J.3
  • 47
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: Critical function of sheet opening mechanism
    • Carrell, R. W. and Stein, P. E. (1996) The biostructural pathology of the serpins: critical function of sheet opening mechanism. Biol. Chem. Hoppe-Seyler 377, 1-17
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 1-17
    • Carrell, R.W.1    Stein, P.E.2
  • 48
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas, D. A. and Carrell, R. W. (2002) Serpinopathies and the conformational dementias. Nat. Rev. Genet. 3, 759-768
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 49
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein, P. E. and Carrell, R. W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2, 96-113
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2


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