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Volumn 82, Issue 1, 1999, Pages 72-79

Involvement of Lys 62(217) and lys 63(218) of human anticoagulant protein C in heparin stimulation of inhibition by the protein C inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; ALPHA 1 ANTITRYPSIN; ANTICOAGULANT PROTEIN; HEPARIN; LYSINE; PLASMINOGEN ACTIVATOR INHIBITOR 3; PROTEIN C; SERINE PROTEINASE; SODIUM CHLORIDE;

EID: 0032773568     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1614632     Document Type: Article
Times cited : (32)

References (49)
  • 2
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967; 27: 157-62.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 4
    • 0001976355 scopus 로고
    • The protein C anticoagulant system
    • Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds). Philadelphia, PA, W B Saunders Company
    • Dahlbäck B, Stenflo J. The protein C anticoagulant system. In: The Molecular Basis of Blood Diseases. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H (eds). Philadelphia, PA, W B Saunders Company, 1994; pp 599-627.
    • (1994) The Molecular Basis of Blood Diseases , pp. 599-627
    • Dahlbäck, B.1    Stenflo, J.2
  • 5
    • 0026409651 scopus 로고
    • Treatment of homozygous protein C deficiency and neonatal purpura fulminans with a purified protein C concentrate
    • Dreyfus M, Maghey JF, Bridey F, Schultz HP, Planche C, Dehan M, Tchernia G. Treatment of homozygous protein C deficiency and neonatal purpura fulminans with a purified protein C concentrate. N Engl J Med 1991; 325: 1565-8.
    • (1991) N Engl J Med , vol.325 , pp. 1565-1568
    • Dreyfus, M.1    Maghey, J.F.2    Bridey, F.3    Schultz, H.P.4    Planche, C.5    Dehan, M.6    Tchernia, G.7
  • 6
    • 0031590612 scopus 로고    scopus 로고
    • Use of protein C concentrate, heparin, and haemodiafiltration in meningococcus-induced purpura fulminans
    • Smith OP, White B, Vaughan D, Rafferty M, Claffey L, Lyons B, Casey W. Use of protein C concentrate, heparin, and haemodiafiltration in meningococcus-induced purpura fulminans. Lancet 1997; 350: 1590-3.
    • (1997) Lancet , vol.350 , pp. 1590-1593
    • Smith, O.P.1    White, B.2    Vaughan, D.3    Rafferty, M.4    Claffey, L.5    Lyons, B.6    Casey, W.7
  • 7
    • 0025848885 scopus 로고
    • In vivo and in vitro complexes of activated protein C with two inhibitors in baboon plasma
    • España F, Gruber AG, Heeb MJ, Hanson SR, Harker LA, Griffin JH. In vivo and in vitro complexes of activated protein C with two inhibitors in baboon plasma. Blood 1991; 77: 1754-60.
    • (1991) Blood , vol.77 , pp. 1754-1760
    • España, F.1    Gruber, A.G.2    Heeb, M.J.3    Hanson, S.R.4    Harker, L.A.5    Griffin, J.H.6
  • 8
    • 0023755722 scopus 로고
    • Physiologic inhibition of human activated protein C by alpha1-antitrypsin
    • Heeb MJ, Griffin JH. Physiologic inhibition of human activated protein C by alpha1-antitrypsin. J Biol Chem 1988; 263: 11613-6.
    • (1988) J Biol Chem , vol.263 , pp. 11613-11616
    • Heeb, M.J.1    Griffin, J.H.2
  • 9
    • 0027438386 scopus 로고
    • Interaction of activated protein C with serpins
    • Hermans JM, Stone SR, Interaction of activated protein C with serpins. Biochem J 1993; 295: 239-45.
    • (1993) Biochem J , vol.295 , pp. 239-245
    • Hermans, J.M.1    Stone, S.R.2
  • 10
    • 0009567079 scopus 로고
    • Structural aspects of the serpin reaction coordinate
    • Katz DS, Christianson DW. Structural aspects of the serpin reaction coordinate. Persp Drug Discov Design 1994; 2: 459-74.
    • (1994) Persp Drug Discov Design , vol.2 , pp. 459-474
    • Katz, D.S.1    Christianson, D.W.2
  • 11
    • 0030888853 scopus 로고    scopus 로고
    • The serpin-proteinase complex revealed
    • Lawrence DA. The serpin-proteinase complex revealed. Nat Struct Biol 1997; 4: 339-41.
    • (1997) Nat Struct Biol , vol.4 , pp. 339-341
    • Lawrence, D.A.1
  • 12
    • 0031036673 scopus 로고    scopus 로고
    • Major proteinase movement upon stable serpin-proteinase complex formation
    • Stratikos E, Gettins PGW, Major proteinase movement upon stable serpin-proteinase complex formation. Proc Natl Acad Sci USA 1997; 94: 453-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 453-458
    • Stratikos, E.1    Gettins, P.G.W.2
  • 14
    • 0028332939 scopus 로고
    • Molecular mapping of the heparin-binding exosite of thrombin
    • Sheehan JP, Sadler JE. Molecular mapping of the heparin-binding exosite of thrombin. Proc Natl Acad Sci USA 1994, 91: 5518-22.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5518-5522
    • Sheehan, J.P.1    Sadler, J.E.2
  • 15
    • 0027972583 scopus 로고
    • Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III
    • Gan ZR, Li Y, Chen Z, Lewis SD, Shafer JA. Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III. J Biol Chem 1994; 269: 1301-5.
    • (1994) J Biol Chem , vol.269 , pp. 1301-1305
    • Gan, Z.R.1    Li, Y.2    Chen, Z.3    Lewis, S.D.4    Shafer, J.A.5
  • 16
    • 0028061369 scopus 로고
    • Regulation of thrombin activity by antithrombin and heparin
    • Olson ST, Björk I. Regulation of thrombin activity by antithrombin and heparin. Sem Thromb Hemostas 1994; 20: 373-409.
    • (1994) Sem Thromb Hemostas , vol.20 , pp. 373-409
    • Olson, S.T.1    Björk, I.2
  • 17
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson ST, Bjork I, Sheffer R, Craig PA, Shore JD, Choay J. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J Biol Chem 1992; 267: 12528-38.
    • (1992) J Biol Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 18
    • 0028475334 scopus 로고
    • A mechanism for heparininduced potentiation of antithrombin III
    • van Boeckel CA, Grootenhuis PD, Visser A. A mechanism for heparininduced potentiation of antithrombin III. Nat Struct Biol 1994; 1: 423-5.
    • (1994) Nat Struct Biol , vol.1 , pp. 423-425
    • Van Boeckel, C.A.1    Grootenhuis, P.D.2    Visser, A.3
  • 19
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • Olson ST, Bjork I. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects. J Biol Chem 1991; 266: 6353-64.
    • (1991) J Biol Chem , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Bjork, I.2
  • 20
    • 0030469373 scopus 로고    scopus 로고
    • Heparin stimulation of the inhibition of activated protein C and other enzymes by human protein C inhibitor -influence of the molecular weight of heparin and ionic strength
    • Aznar J, España F, Estellés A, Royo M. Heparin stimulation of the inhibition of activated protein C and other enzymes by human protein C inhibitor -influence of the molecular weight of heparin and ionic strength. Thromb Haemost 1996; 76: 983-8.
    • (1996) Thromb Haemost , vol.76 , pp. 983-988
    • Aznar, J.1    España, F.2    Estellés, A.3    Royo, M.4
  • 21
    • 0026598679 scopus 로고
    • Modulation of protein C inhibitor activity by histidine-rich glycoprotein and platelet factor 4: Role of zinc and calcium ions in the heparin-neutralizing ability of histidine-rich glycoprotein
    • Kazama Y, Koide T. Modulation of protein C inhibitor activity by histidine-rich glycoprotein and platelet factor 4: role of zinc and calcium ions in the heparin-neutralizing ability of histidine-rich glycoprotein. Thromb Haemost 1992; 67: 50-5.
    • (1992) Thromb Haemost , vol.67 , pp. 50-55
    • Kazama, Y.1    Koide, T.2
  • 22
    • 0345176222 scopus 로고    scopus 로고
    • Anticoagulant synergism of heparin and activated protein C in vitro
    • Petäjä J, Fernández JA, Gruber A, Griffin JH. Anticoagulant synergism of heparin and activated protein C in vitro. J Clin Invest 1997; 99: 2655-63.
    • (1997) J Clin Invest , vol.99 , pp. 2655-2663
    • Petäjä, J.1    Fernández, J.A.2    Gruber, A.3    Griffin, J.H.4
  • 23
    • 0029983596 scopus 로고    scopus 로고
    • Structural investigation of the alpha-1-antichymotrypsin: Prostate-specific antigen complex by comparative model building
    • Villoutreix BO, Lilja H, Pettersson K, Lövgren T, Teleman O. Structural investigation of the alpha-1-antichymotrypsin: Prostate-specific antigen complex by comparative model building. Protein Sei 1996; 5: 836-51.
    • (1996) Protein Sei , vol.5 , pp. 836-851
    • Villoutreix, B.O.1    Lilja, H.2    Pettersson, K.3    Lövgren, T.4    Teleman, O.5
  • 24
    • 4243373196 scopus 로고    scopus 로고
    • Identification of a heparin binding site in activated protein C (Lys 37-39) and its detrimental intermolecular interaction with Arg 278 of protein C inhibitor
    • Neese LL, Gerlitz B, Cooper ST, Grinnell BW, Church FC. Identification of a heparin binding site in activated protein C (Lys 37-39) and its detrimental intermolecular interaction with Arg 278 of protein C inhibitor. Blood 1997; 90: 146a.
    • (1997) Blood , vol.90
    • Neese, L.L.1    Gerlitz, B.2    Cooper, S.T.3    Grinnell, B.W.4    Church, F.C.5
  • 25
    • 0031424043 scopus 로고    scopus 로고
    • Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: Studies related to proline-10
    • Shen L, Shah A, Dahlbäck B, Nelsestuen GL. Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: studies related to proline-10. Biochemistry 1997; 36: 16025-31.
    • (1997) Biochemistry , vol.36 , pp. 16025-16031
    • Shen, L.1    Shah, A.2    Dahlbäck, B.3    Nelsestuen, G.L.4
  • 26
    • 0028174359 scopus 로고
    • Resistance to inhibition by alpha-1-anti-trypsin and species specificity of a chimeric human/bovine protein C
    • Holly RD, Foster DC. Resistance to inhibition by alpha-1-anti-trypsin and species specificity of a chimeric human/bovine protein C. Biochemistry 1994; 33: 1876-80.
    • (1994) Biochemistry , vol.33 , pp. 1876-1880
    • Holly, R.D.1    Foster, D.C.2
  • 27
    • 0026787415 scopus 로고
    • Heparin binding to protein C inhibitor
    • Pratt CW, Church FC. Heparin binding to protein C inhibitor. J Biol Chem 1992; 267: 8789-94.
    • (1992) J Biol Chem , vol.267 , pp. 8789-8794
    • Pratt, C.W.1    Church, F.C.2
  • 28
    • 0027288125 scopus 로고
    • Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin
    • Ami RK, Padmanabhan K, Padmanabhan KP, Wu T-P, Tulinsky A. Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin. Biochemistry 1993; 32: 4727-37.
    • (1993) Biochemistry , vol.32 , pp. 4727-4737
    • Ami, R.K.1    Padmanabhan, K.2    Padmanabhan, Kp.3    Wu, T.-P.4    Tulinsky, A.5
  • 29
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human α-thrombin: Interactions with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9 Å crystal structure of human α-thrombin: Interactions with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J 1989; 8: 3467-75.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 34
    • 0027164634 scopus 로고
    • NMR and molecular modelling studies of the solution conformation of heparin
    • Mulloy B, Forster MJ. Jones C, Davies DB. NMR and molecular modelling studies of the solution conformation of heparin. Biochem J 1993; 293: 849-58.
    • (1993) Biochem J , vol.293 , pp. 849-858
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Davies, D.B.4
  • 35
    • 0028204534 scopus 로고
    • Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen
    • Fisher CL. Greengard JS, Griffin JH. Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen. Protein Sci 1994; 3: 588-99.
    • (1994) Protein Sci , vol.3 , pp. 588-599
    • Fisher, C.L.1    Greengard, J.S.2    Griffin, J.H.3
  • 36
    • 0028323166 scopus 로고
    • Structural basis for type I and type II deficiencies of antithrombotic plasma protein C: Patterns revealed by three-dimensional molecular modelling of mutations of the protease domain
    • Greengard JS, Fisher CL, Villoutreix B, Griffin JH. Structural basis for type I and type II deficiencies of antithrombotic plasma protein C: patterns revealed by three-dimensional molecular modelling of mutations of the protease domain. Proteins 1994; 18: 367-80.
    • (1994) Proteins , vol.18 , pp. 367-380
    • Greengard, J.S.1    Fisher, C.L.2    Villoutreix, B.3    Griffin, J.H.4
  • 37
    • 0031452272 scopus 로고    scopus 로고
    • Homology modelling of the catalytic domain of early mammalian protein C: Evolution of structural features
    • Wacey AI. Krawczak M, Kemball-Cook G, Cooper DN. Homology modelling of the catalytic domain of early mammalian protein C: evolution of structural features. Hum Genel 1997; 101: 37-42.
    • (1997) Hum Genel , vol.101 , pp. 37-42
    • Wacey, A.I.1    Krawczak, M.2    Kemball-Cook, G.3    Cooper, D.N.4
  • 38
    • 0028882129 scopus 로고
    • Intermolecular interactions between protein C inhibitor and coagulation proteases
    • Cooper ST, Whinna HC. Jackson TP, Boyd JM, Church FC. Intermolecular interactions between protein C inhibitor and coagulation proteases. Biochemistry 1995; 34: 12991-7.
    • (1995) Biochemistry , vol.34 , pp. 12991-12997
    • Cooper, S.T.1    Whinna, H.C.2    Jackson, T.P.3    Boyd, J.M.4    Church, F.C.5
  • 39
    • 0033135017 scopus 로고    scopus 로고
    • Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site directed mutagenesis and computer modeling
    • Knobe KE, Bernsdotter A, Shen L, Morser J, Dahlbäck B, Villoutreix BO. Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site directed mutagenesis and computer modeling. Proteins 1999; 35: 218-34.
    • (1999) Proteins , vol.35 , pp. 218-234
    • Knobe, K.E.1    Bernsdotter, A.2    Shen, L.3    Morser, J.4    Dahlbäck, B.5    Villoutreix, B.O.6
  • 40
    • 0029787653 scopus 로고    scopus 로고
    • Mutation of prolease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin
    • Gerlitz B and Grinnell BW. Mutation of prolease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin. J Biol Chem 1996; 271: 2285-8.
    • (1996) J Biol Chem , vol.271 , pp. 2285-2288
    • Gerlitz, B.1    Grinnell, B.W.2
  • 41
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin lo acidic fibroblast growth factor
    • Fromm JR, Hileman RE, Caldwell EE, Weiler JM, Linhardl RJ. Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin lo acidic fibroblast growth factor. Arch Biochem Biophys 1995; 323: 279-87.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.3    Weiler, J.M.4    Linhardl, R.J.5
  • 43
    • 0027230866 scopus 로고
    • General features of the heparin-binding serpins antithromhin. Heparin cofactor II and protein C inhibitor
    • Pratt CW, Church FC. General features of the heparin-binding serpins antithromhin. heparin cofactor II and protein C inhibitor. Blood Coagul Fibrinolysis 1993; 4: 479-490.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 479-490
    • Pratt, C.W.1    Church, F.C.2
  • 44
    • 0030044548 scopus 로고    scopus 로고
    • A two-allele polymorphism in protein C inhibitor with varying frequencies in different ethnic populations
    • Radtke KP, Greengard JS, Fernandez JA. Villoutreix BO, Griffin JH. A two-allele polymorphism in protein C inhibitor with varying frequencies in different ethnic populations. Thromb Haemost 1996; 75: 62-9.
    • (1996) Thromb Haemost , vol.75 , pp. 62-69
    • Radtke, Kp.1    Greengard, J.S.2    Fernandez, J.A.3    Villoutreix, B.O.4    Griffin, J.H.5
  • 45
    • 0027960551 scopus 로고
    • Role of the H helix in heparin binding to protein C inhibitor
    • Shirk RA, Elisen MG, Meijers JC, Church FC. Role of the H helix in heparin binding to protein C inhibitor. J Biol Chem 1994; 269: 28690-5.
    • (1994) J Biol Chem , vol.269 , pp. 28690-28695
    • Shirk, R.A.1    Elisen, M.G.2    Meijers, J.C.3    Church, F.C.4
  • 47
    • 0028812595 scopus 로고    scopus 로고
    • Characterization of a cDNA for rhesus monkey protein C inhibitor: Evidence for N-terminal involvement in heparin stimulation
    • Radtke KP, Fernandez JA, Villoutreix BO. Greengard JS, Griffin JH. Characterization of a cDNA for rhesus monkey protein C inhibitor: evidence for N-terminal involvement in heparin stimulation. Thromb Haemost 1996; 74: 1079-87.
    • (1996) Thromb Haemost , vol.74 , pp. 1079-1087
    • Radtke, Kp.1    Fernandez, J.A.2    Villoutreix, B.O.3    Greengard, J.S.4    Griffin, J.H.5
  • 48
    • 0030853308 scopus 로고    scopus 로고
    • Identification of the antithrombin III heparin binding site
    • Ersdal-Badju E, Lu A, Zuo Y, Picard V, Bock SC. Identification of the antithrombin III heparin binding site. J Biol Chem 1997; 272: 19393-400.
    • (1997) J Biol Chem , vol.272 , pp. 19393-19400
    • Ersdal-Badju, E.1    Lu, A.2    Zuo, Y.3    Picard, V.4    Bock, S.C.5


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