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Volumn 501, Issue , 2011, Pages 89-103

Serpins as hormone carriers: Modulation of release

Author keywords

angiotensin; angiotensinogen; CBG; corticosteroid; pre eclampsia; protein thermocouple; renin; S to R change; TBG; thyroxine

Indexed keywords

ANGIOTENSINOGEN; CARRIER PROTEIN; SERINE PROTEINASE INHIBITOR; THYROXINE BINDING GLOBULIN; TRANSCORTIN;

EID: 80955141924     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385950-1.00006-7     Document Type: Chapter
Times cited : (6)

References (50)
  • 1
    • 0032532347 scopus 로고    scopus 로고
    • Antithrombins Wibble and Wobble (T85M/K): Archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation
    • N.J. Beauchamp, R.N. Pike, M. Daly, L. Butler, M. Makris, T.R. Dafforn, A. Zhou, H.L. Fitton, F.E. Preston, I.R. Peake, and R.W. Carrell Antithrombins Wibble and Wobble (T85M/K): Archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation Blood 92 1998 2696 2706 (Pubitemid 28469081)
    • (1998) Blood , vol.92 , Issue.8 , pp. 2696-2706
    • Beauchamp, N.J.1    Pike, R.N.2    Daly, M.3    Butler, L.4    Makris, M.5    Dafforn, T.R.6    Zhou, A.7    Fitton, H.L.8    Preston, F.E.9    Peake, I.R.10    Carrell, R.W.11
  • 2
    • 0025876891 scopus 로고
    • Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec reveals two nucleotide substitutions
    • R. Bertenshaw, K. Takeda, and S. Refetoff Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec reveals two nucleotide substitutions Am. J. Hum. Genet. 48 1991 741 744 (Pubitemid 21891618)
    • (1991) American Journal of Human Genetics , vol.48 , Issue.4 , pp. 741-744
    • Bertenshaw, R.1    Takeda, K.2    Refetoff, S.3
  • 3
    • 4444347073 scopus 로고    scopus 로고
    • Placental oxidative stress: From miscarriage to preeclampsia
    • DOI 10.1016/j.jsgi.2004.03.003, PII S1071557604001388
    • G.J. Burton, and E. Jauniaux Placental oxidative stress: From miscarriage to preeclampsia J. Soc. Gynecol. Invest. 11 2004 342 352 (Pubitemid 39185874)
    • (2004) Journal of the Society for Gynecologic Investigation , vol.11 , Issue.6 , pp. 342-352
    • Burton, G.J.1    Jauniaux, E.2
  • 5
    • 0022395406 scopus 로고
    • 1 -antitrypsin, antithrombin and the mechanism of inflammatory thrombosis
    • DOI 10.1038/317730a0
    • R.W. Carrell, and M.C. Owen Plakalbumin, alpha 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis Nature 317 1985 730 732 (Pubitemid 16223640)
    • (1985) Nature , vol.317 , Issue.6039 , pp. 730-732
    • Carrell, R.W.1    Owen, M.C.2
  • 6
    • 0018629827 scopus 로고
    • Carboxy terminal fragment of human -1-antitrypsin from hydroxylamine cleavage: Homology with antithrombin III
    • R. Carrell, M. Owen, S. Brennan, and L. Vaughan Carboxy terminal fragment of human α-1-antitrypsin from hydroxylamine cleavage: Homology with antithrombin III Biochem. Biophys. Res. Commun. 91 1979 1032 1037 (Pubitemid 10145376)
    • (1979) Biochemical and Biophysical Research Communications , vol.91 , Issue.3 , pp. 1032-1037
    • Carrell, R.1    Owen, M.2    Brennan, S.3    Vaughan, L.4
  • 7
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • R.W. Carrell, D.L. Evans, and P.E. Stein Mobile reactive centre of serpins and the control of thrombosis Nature 353 1991 576 578 (Pubitemid 21912561)
    • (1991) Nature , vol.353 , Issue.6344 , pp. 576-578
    • Carrell, R.W.1    Evans, D.Ll.2    Stein, P.E.3
  • 8
    • 0028773279 scopus 로고
    • Biological implications of a 3 structure of dimeric antithrombin
    • R.W. Carrell, P.E. Stein, G. Fermi, and M.R. Wardell Biological implications of a 3 structure of dimeric antithrombin Structure 2 1994 257 270
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 9
    • 0029855362 scopus 로고    scopus 로고
    • The renin-angiotensin system and the heart: A historical review
    • S.J. Cleland, and J.L. Reid The renin-angiotensin system and the heart: A historical review Heart 76 1996 7 12 (Pubitemid 26395749)
    • (1996) Heart , vol.76 , Issue.SUPPL. 3 , pp. 7-12
    • Cleland, S.J.1    Reid, J.L.2
  • 10
    • 34250736356 scopus 로고    scopus 로고
    • Balancing reactivity against selectivity: The evolution of protein S-nitrosylation as an effector of cell signaling by nitric oxide
    • DOI 10.1016/j.cardiores.2007.04.023, PII S0008636307002106
    • B. Derakhshan, G. Hao, and S.S. Gross Balancing reactivity against selectivity: The evolution of protein S-nitrosylation as an effector of cell signaling by nitric oxide Cardiovasc. Res. 75 2007 210 219 (Pubitemid 46961931)
    • (2007) Cardiovascular Research , vol.75 , Issue.2 , pp. 210-219
    • Derakhshan, B.1    Hao, G.2    Gross, S.S.3
  • 11
    • 33745994900 scopus 로고    scopus 로고
    • Genetic basis of hypertension: Revisiting angiotensinogen
    • DOI 10.1161/01.HYP.0000227932.13687.60, PII 0000426820060700000003
    • M.E. Dickson, and C.D. Sigmund Genetic basis of hypertension: Revisiting angiotensinogen Hypertension 48 2006 14 20 (Pubitemid 44297514)
    • (2006) Hypertension , vol.48 , Issue.1 , pp. 14-20
    • Dickson, M.E.1    Sigmund, C.D.2
  • 12
    • 0020545825 scopus 로고
    • Angiotensinogen is related to the antitrypsin-antithrombin-ovalbumin family
    • R.F. Doolittle Angiotensinogen is related to the antitrypsin- antithrombin-ovalbumin family Science 222 1983 417 419 (Pubitemid 13012680)
    • (1983) Science , vol.222 , Issue.4622 , pp. 417-419
    • Doolittle, R.F.1
  • 13
    • 0006583903 scopus 로고
    • Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: Close homology to the serine antiproteases
    • DOI 10.1073/pnas.83.20.7708
    • I.L. Flink, T.J. Bailey, T.A. Gustafson, B.E. Markham, and E. Morkin Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: Close homology to the serine antiproteases Proc. Natl. Acad. Sci. USA 83 1986 7708 7712 (Pubitemid 17183916)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.20 , pp. 7708-7712
    • Flink, I.L.1    Bailey, T.J.2    Gustafson, T.A.3
  • 14
    • 0032545490 scopus 로고    scopus 로고
    • Role of cysteine residues in human angiotensinogen. Cys232 is required for angiotensinogen-pro major basic protein complex formation
    • A.P. Gimenez-Roqueplo, J. Celerier, G. Schmid, P. Corvol, and X. Jeunemaitre Role of cysteine residues in human angiotensinogen. Cys232 is required for angiotensinogen-pro major basic protein complex formation J. Biol. Chem. 273 1998 34480 34487
    • (1998) J. Biol. Chem. , vol.273 , pp. 34480-34487
    • Gimenez-Roqueplo, A.P.1    Celerier, J.2    Schmid, G.3    Corvol, P.4    Jeunemaitre, X.5
  • 15
    • 0036645673 scopus 로고    scopus 로고
    • Loop variants of the serpin thyroxine-binding globulin: Implications for hormone release upon limited proteolysis
    • DOI 10.1042/BJ20020014
    • H. Grasberger, H.M. Golcher, A. Fingerhut, and O.E. Janssen Loop variants of the serpin thyroxine-binding globulin: Implications for hormone release upon limited proteolysis Biochem. J. 365 2002 311 316 (Pubitemid 34756166)
    • (2002) Biochemical Journal , vol.365 , Issue.1 , pp. 311-316
    • Grasberger, H.1    Golcher, H.M.B.2    Fingerhut, A.3    Janssen, O.E.4
  • 16
    • 0344435262 scopus 로고
    • Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors
    • G.L. Hammond, C.L. Smith, I.S. Goping, D.A. Underhill, M.J. Harley, J. Reventos, N.A. Musto, G.L. Gunsalus, and C.W. Bardin Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors Proc. Natl. Acad. Sci. USA 84 1987 5153 5157 (Pubitemid 17119119)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.15 , pp. 5153-5157
    • Hammond, G.L.1    Smith, C.L.2    Goping, I.S.3
  • 17
    • 0025368906 scopus 로고
    • A role for corticosteroid-binding globulin in delivery of cortisol to activated neutrophils
    • G.L. Hammond, C.L. Smith, N.A. Paterson, and W.J. Sibbald A role for corticosteroid-binding globulin in delivery of cortisol to activated neutrophils J. Clin. Endocrinol. Metab. 71 1990 34 39
    • (1990) J. Clin. Endocrinol. Metab. , vol.71 , pp. 34-39
    • Hammond, G.L.1    Smith, C.L.2    Paterson, N.A.3    Sibbald, W.J.4
  • 19
    • 0024423930 scopus 로고
    • 1 - antitrypsin for structure and function of serpins
    • 1 -antitrypsin for structure and function of serpins Biochemistry 28 1989 8951 8966 (Pubitemid 19283457)
    • (1989) Biochemistry , vol.28 , Issue.23 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 20
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • J.A. Huntington, R.J. Read, and R.W. Carrell Structure of a serpin-protease complex shows inhibition by deformation Nature 407 2000 923 926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 24
    • 0041846670 scopus 로고    scopus 로고
    • Crystal structure of antithrombin in a heparin-bound intermediate state
    • DOI 10.1021/bi034524y
    • D.J. Johnson, and J.A. Huntington Crystal structure of antithrombin in a heparin-bound intermediate state Biochemistry 42 2003 8712 8719 (Pubitemid 36899814)
    • (2003) Biochemistry , vol.42 , Issue.29 , pp. 8712-8719
    • Johnson, D.J.D.1    Huntington, J.A.2
  • 26
    • 35748946026 scopus 로고    scopus 로고
    • Corticosteroid-binding Globulin, a Structural Basis for Steroid Transport and Proteinase-triggered Release
    • DOI 10.1074/jbc.M705014200
    • M.A. Klieber, C. Underhill, G.L. Hammond, and Y.A. Muller Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release J. Biol. Chem. 282 2007 29594 29603 (Pubitemid 350043346)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29594-29603
    • Klieber, M.A.1    Underhill, C.2    Hammond, G.L.3    Muller, Y.A.4
  • 27
    • 34748859681 scopus 로고    scopus 로고
    • The intrarenal renin-angiotensin system: From physiology to the pathobiology of hypertension and kidney disease
    • DOI 10.1124/pr.59.3.3
    • H. Kobori, M. Nangaku, L.G. Navar, and A. Nishiyama The intrarenal renin-angiotensin system: From physiology to the pathobiology of hypertension and kidney disease Pharmacol. Rev. 59 2007 251 287 (Pubitemid 47481436)
    • (2007) Pharmacological Reviews , vol.59 , Issue.3 , pp. 251-287
    • Kobori, H.1    Nangaku, M.2    Navar, L.G.3    Nishiyama, A.4
  • 28
    • 0021747157 scopus 로고
    • 1 -proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • DOI 10.1016/0022-2836(84)90298-5
    • 1 -proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function J. Mol. Biol. 177 1984 531 556 (Pubitemid 15244823)
    • (1984) Journal of Molecular Biology , vol.177 , Issue.3 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 30
    • 55949083365 scopus 로고    scopus 로고
    • Reduced selenium concentrations and glutathione peroxidase activity in preeclamptic pregnancies
    • H.D. Mistry, V. Wilson, M.M. Ramsay, M.E. Symonds, and F. Broughton Pipkin Reduced selenium concentrations and glutathione peroxidase activity in preeclamptic pregnancies Hypertension 52 2008 881 888
    • (2008) Hypertension , vol.52 , pp. 881-888
    • Mistry, H.D.1    Wilson, V.2    Ramsay, M.M.3    Symonds, M.E.4    Broughton Pipkin, F.5
  • 32
    • 76749110706 scopus 로고    scopus 로고
    • Review: Reactive oxygen and nitrogen species and functional adaptation of the placenta
    • L. Myatt Review: Reactive oxygen and nitrogen species and functional adaptation of the placenta Placenta 31 Suppl 2010 S66 S69
    • (2010) Placenta , vol.31 , Issue.SUPPL.
    • Myatt, L.1
  • 33
    • 70450180160 scopus 로고    scopus 로고
    • Protein cysteine modifications: (1) Medical chemistry for proteomics
    • N. Nagahara, T. Matsumura, R. Okamoto, and Y. Kajihara Protein cysteine modifications: (1) Medical chemistry for proteomics Curr. Med. Chem. 16 2009 4419 4444
    • (2009) Curr. Med. Chem. , vol.16 , pp. 4419-4444
    • Nagahara, N.1    Matsumura, T.2    Okamoto, R.3    Kajihara, Y.4
  • 34
    • 0036266596 scopus 로고    scopus 로고
    • Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin
    • DOI 10.1172/JCI200214276
    • G. Nguyen, F. Delarue, C. Burckle, L. Bouzhir, T. Giller, and J.D. Sraer Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin J. Clin. Invest. 109 2002 1417 1427 (Pubitemid 34596167)
    • (2002) Journal of Clinical Investigation , vol.109 , Issue.11 , pp. 1417-1427
    • Nguyen, G.1    Delarue, F.2    Burckle, C.3    Bouzhir, L.4    Giller, T.5    Sraer, J.-D.6
  • 35
    • 0023761757 scopus 로고
    • Hormone binding globulins undergo serpin conformational change in inflammation
    • DOI 10.1038/336257a0
    • P.A. Pemberton, P.E. Stein, M.B. Pepys, J.M. Potter, and R.W. Carrell Hormone binding globulins undergo serpin conformational change in inflammation Nature 336 1988 257 258 (Pubitemid 18264407)
    • (1988) Nature , vol.336 , Issue.6196 , pp. 257-258
    • Pemberton, P.A.1    Stein, P.E.2    Pepys, M.B.3    Potter, J.M.4    Carrell, R.W.5
  • 39
    • 0036801304 scopus 로고    scopus 로고
    • The evolutionary and integrative roles of transthyrein in thyroid hormone homeostasis
    • DOI 10.1677/joe.0.1750061
    • G. Schreiber The evolutionary and integrative roles of transthyretin in thyroid hormone homeostasis J. Endocrinol. 175 2002 61 73 (Pubitemid 35276587)
    • (2002) Journal of Endocrinology , vol.175 , Issue.1 , pp. 61-73
    • Schreiber, G.1
  • 41
    • 0025226070 scopus 로고
    • Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A
    • A.J. Schulze, U. Baumann, S. Knof, E. Jaeger, R. Huber, and C.B. Laurell Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A Eur. J. Biochem. 194 1990 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
  • 42
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • DOI 10.1016/S0092-8674(01)00495-0
    • J.S. Stamler, S. Lamas, and F.C. Fang Nitrosylation. The prototypic redox-based signaling mechanism Cell 106 2001 675 683 (Pubitemid 32900659)
    • (2001) Cell , vol.106 , Issue.6 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 43
    • 0024430428 scopus 로고
    • Ovalbumin and angiotensinogen lack serpin S-R conformational change
    • P.E. Stein, D.A. Tewkesbury, and R.W. Carrell Ovalbumin and angiotensinogen lack serpin S-R conformational change Biochem. J. 262 1989 103 107 (Pubitemid 19220937)
    • (1989) Biochemical Journal , vol.262 , Issue.1 , pp. 103-107
    • Stein, P.E.1    Tewkesbury, D.A.2    Carrell, R.W.3
  • 45
    • 0032475898 scopus 로고    scopus 로고
    • Angiotensinogen cleavage by renin: Importance of a structurally constrained N-terminus
    • DOI 10.1016/S0014-5793(98)01145-4, PII S0014579398011454
    • R.M. Streatfeild-James, D. Williamson, R.N. Pike, D. Tewksbury, R.W. Carrell, and P.B. Coughlin Angiotensinogen cleavage by renin: Importance of a structurally constrained N-terminus FEBS Lett. 436 1998 267 270 (Pubitemid 28468570)
    • (1998) FEBS Letters , vol.436 , Issue.2 , pp. 267-270
    • Streatfeild-James, R.M.A.1    Williamson, D.2    Pike, R.N.3    Tewksbury, D.4    Carrell, R.W.5    Coughlin, P.B.6
  • 46
    • 0034547908 scopus 로고    scopus 로고
    • Linkage between the hormone binding site and the reactive center loop of thyroxine binding globulin
    • S.A. Suda, P.G. Gettins, and P.A. Patston Linkage between the hormone binding site and the reactive center loop of thyroxine binding globulin Arch. Biochem. Biophys. 384 2000 31 36
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 31-36
    • Suda, S.A.1    Gettins, P.G.2    Patston, P.A.3
  • 47
    • 0034681281 scopus 로고    scopus 로고
    • Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin
    • J.C. Whisstock, R. Skinner, R.W. Carrell, and A.M. Lesk Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin J. Mol. Biol. 296 2000 685 699
    • (2000) J. Mol. Biol. , vol.296 , pp. 685-699
    • Whisstock, J.C.1    Skinner, R.2    Carrell, R.W.3    Lesk, A.M.4
  • 49
    • 44649163815 scopus 로고    scopus 로고
    • The S-to-R transition of corticosteroid-binding globulin and the mechanism of hormone release
    • A. Zhou, Z. Wei, P.L. Stanley, R.J. Read, P.E. Stein, and R.W. Carrell The S-to-R transition of corticosteroid-binding globulin and the mechanism of hormone release J. Mol. Biol. 380 2008 244 251
    • (2008) J. Mol. Biol. , vol.380 , pp. 244-251
    • Zhou, A.1    Wei, Z.2    Stanley, P.L.3    Read, R.J.4    Stein, P.E.5    Carrell, R.W.6


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