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Volumn 44, Issue 37, 2005, Pages 12508-12514

Role of the hexapeptide disulfide loop in the γ-carboxyglutamic acid domain of protein C in Ca2+-mediated structural and functional properties

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD; CARBOXYLIC ACIDS; IMMUNOLOGY; MOLECULAR STRUCTURE; PROTEINS; VITAMINS;

EID: 24944501229     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050974+     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon, C. T. (1993) Molecular events that control the protein C anticoagulant pathway, Thromb. Haemostasis 70, 29-35.
    • (1993) Thromb. Haemostasis , vol.70 , pp. 29-35
    • Esmon, C.T.1
  • 2
    • 0022910521 scopus 로고
    • Mechanism of protein C-dependent clot lysis: Role of plasminogen activator inhibitor
    • Sakata, Y., Loskutoff, D. J., Gladson, C. L., Hekman, C. M., and Griffin, J. H. (1986) Mechanism of protein C-dependent clot lysis: role of plasminogen activator inhibitor, Blood 68, 1218-1223.
    • (1986) Blood , vol.68 , pp. 1218-1223
    • Sakata, Y.1    Loskutoff, D.J.2    Gladson, C.L.3    Hekman, C.M.4    Griffin, J.H.5
  • 3
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar, L., Nesheim, M. E., and Tracy, P. B. (1996) The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent, Blood 88, 2093-2100.
    • (1996) Blood , vol.88 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 4
    • 0035992710 scopus 로고    scopus 로고
    • Activated protein C: Potential therapy for severe sepsis, thrombosis and stroke
    • Griffin, J. H., Zlokovic, B. V., and Fernandez, J. A. (2002) Activated protein C: potential therapy for severe sepsis, thrombosis and stroke, Semin. Hematol. 39, 197-205.
    • (2002) Semin. Hematol. , vol.39 , pp. 197-205
    • Griffin, J.H.1    Zlokovic, B.V.2    Fernandez, J.A.3
  • 5
    • 0035815747 scopus 로고    scopus 로고
    • Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis
    • Joyce, D. E., Gelbert, L., Ciaccia, A., DeHoff, B., and Grinnell, B. W. (2001) Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis, J. Biol. Chem. 276, 11199-11203.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11199-11203
    • Joyce, D.E.1    Gelbert, L.2    Ciaccia, A.3    Dehoff, B.4    Grinnell, B.W.5
  • 7
    • 0021099422 scopus 로고
    • Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C
    • Esmon, N. L., DeBault, L. E., and Esmon, C. T. (1983) Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C, J. Biol. Chem. 258, 5548-5553.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5548-5553
    • Esmon, N.L.1    Debault, L.E.2    Esmon, C.T.3
  • 8
    • 0028267187 scopus 로고
    • Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C
    • Colpitts, T. L., and Castellino, F. J. (1994) Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C, Biochemistry 33, 3501-3508.
    • (1994) Biochemistry , vol.33 , pp. 3501-3508
    • Colpitts, T.L.1    Castellino, F.J.2
  • 9
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann K. G., Nesheim, M. E., Church, W. R., Haley, P., and Krishnaswamy, S. (1990) Surface-dependent reactions of the vitamin K-dependent enzyme complexes, Blood 76, 1-16.
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 10
    • 0028286007 scopus 로고
    • Properties of recombinant chimeric human protein C and activated protein C containing the gamma-carboxyglutamic acid and trailing helical stack domains of protein C replaced by those of human coagulation factor IX
    • Christiansen, W. T., and Castellino, F. J. (1994) Properties of recombinant chimeric human protein C and activated protein C containing the gamma-carboxyglutamic acid and trailing helical stack domains of protein C replaced by those of human coagulation factor IX, Biochemistry 33, 5901-5911.
    • (1994) Biochemistry , vol.33 , pp. 5901-5911
    • Christiansen, W.T.1    Castellino, F.J.2
  • 11
    • 0030988243 scopus 로고    scopus 로고
    • Properties of a recombinant chimeric protein in which the gamma-carboxyglutamic acid and helical stack domains of human anticoagulant protein C are replaced by those of human coagulation factor VII
    • Geng, J. P., and Castellino, F. J. (1997) Properties of a recombinant chimeric protein in which the gamma-carboxyglutamic acid and helical stack domains of human anticoagulant protein C are replaced by those of human coagulation factor VII, Thromb. Haemostasis 77, 926-933.
    • (1997) Thromb. Haemostasis , vol.77 , pp. 926-933
    • Geng, J.P.1    Castellino, F.J.2
  • 12
    • 0032502796 scopus 로고    scopus 로고
    • A chimeric protein C containing the prothrombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity
    • Smirnov, M. D., Safa, O., Regan, L., Mather, T., Stearns-Kurosawa, D. J., Kurosawa, S., Rezaie, A. R., Esmon, N. L., and Esmon, C. T. (1998) A chimeric protein C containing the prothrombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity, J. Biol. Chem. 273, 9031-9040.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9031-9040
    • Smirnov, M.D.1    Safa, O.2    Regan, L.3    Mather, T.4    Stearns-Kurosawa, D.J.5    Kurosawa, S.6    Rezaie, A.R.7    Esmon, N.L.8    Esmon, C.T.9
  • 13
    • 0030666197 scopus 로고    scopus 로고
    • The interaction between the endothelial cell protein C receptor and protein C is dictated by the gamma-carboxyglutamic acid domain of protein C
    • Regan, L. M., Mollica, J. S., Rezaie, A. R., and Esmon, C. T. (1997) The interaction between the endothelial cell protein C receptor and protein C is dictated by the gamma-carboxyglutamic acid domain of protein C, J. Biol. Chem. 272, 26279-26284.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26279-26284
    • Regan, L.M.1    Mollica, J.S.2    Rezaie, A.R.3    Esmon, C.T.4
  • 14
    • 0026687609 scopus 로고
    • Role of individual gamma-carboxyglutamic acid residues of activated human protein C in defining its in vitro anticoagulant activity
    • Zhang, L., Jhingan, A., and Castellino, F. J. (1992) Role of individual gamma-carboxyglutamic acid residues of activated human protein C in defining its in vitro anticoagulant activity, Blood 80, 942-952.
    • (1992) Blood , vol.80 , pp. 942-952
    • Zhang, L.1    Jhingan, A.2    Castellino, F.J.3
  • 15
    • 0027155692 scopus 로고
    • The contributions of individual gamma-carboxyglutamic acid residues in the calcium-dependent binding of recombinant human protein C to acidic phospholipids vesicles
    • Zhang, L., and Castellino, F. J. (1993) The contributions of individual gamma-carboxyglutamic acid residues in the calcium-dependent binding of recombinant human protein C to acidic phospholipids vesicles, J. Biol. Chem. 268, 12040-12045.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12040-12045
    • Zhang, L.1    Castellino, F.J.2
  • 16
    • 0025881214 scopus 로고
    • Role of the hexapeptide disulfide loop present in the y-carboxyglutamic acid domain of human protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C
    • Zhang, L., and Castellino, F. J. (1991) Role of the hexapeptide disulfide loop present in the y-carboxyglutamic acid domain of human protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C, Biochemistry 30, 6696-6704.
    • (1991) Biochemistry , vol.30 , pp. 6696-6704
    • Zhang, L.1    Castellino, F.J.2
  • 17
    • 0027943163 scopus 로고
    • Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor
    • Fukudome, K., and Esmon, C. T. (1994) Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor, J. Biol. Chem. 269, 26486-26491.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26486-26491
    • Fukudome, K.1    Esmon, C.T.2
  • 18
    • 0037067752 scopus 로고    scopus 로고
    • The crystal structure of the endothelial protein C receptor and a bound phospholipids
    • Oganesyan, V., Oganesyan, N., Terzyan, S., Qu, D., Dauter, Z., Esmon, N. L., and Esmon, C. T. (2002) The crystal structure of the endothelial protein C receptor and a bound phospholipids, J. Biol. Chem. 277, 24851-24854.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24851-24854
    • Oganesyan, V.1    Oganesyan, N.2    Terzyan, S.3    Qu, D.4    Dauter, Z.5    Esmon, N.L.6    Esmon, C.T.7
  • 19
    • 0027174502 scopus 로고
    • Binding of calcium to synthetic peptides containing gamma-carboxyglutamic acid
    • Colpitts, T. L., and Castellino, F. J. (1993) Binding of calcium to synthetic peptides containing gamma-carboxyglutamic acid, Int. J. Pept. Protein Res. 41, 567-575.
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 567-575
    • Colpitts, T.L.1    Castellino, F.J.2
  • 20
    • 0030449042 scopus 로고    scopus 로고
    • Calcium binding properties of synthetic γ-carboxyglutamic acid-containing marine cone snail "leeper" peptides, conantokin-G and conantokin-T
    • Prorok, M., Warder, S. E., Blandl, T., and Castellino, F. J. (1996) Calcium binding properties of synthetic γ-carboxyglutamic acid-containing marine cone snail "leeper" peptides, conantokin-G and conantokin-T, Biochemistry 35, 16528-16534.
    • (1996) Biochemistry , vol.35 , pp. 16528-16534
    • Prorok, M.1    Warder, S.E.2    Blandl, T.3    Castellino, F.J.4
  • 21
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y.-H., Yang, J. T., and Martinez, H. M. (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion, Biochemistry 11, 4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.-H.1    Yang, J.T.2    Martinez, H.M.3
  • 22
    • 0027942676 scopus 로고
    • Membrane binding properties of the factor IX gamma-carboxy-glutamic acid-rich domain prepared by chemical synthesis
    • Jacobs, M., Freedman, S. J., Furie, B. C., and Furie, B. (1994) Membrane binding properties of the factor IX gamma-carboxy-glutamic acid-rich domain prepared by chemical synthesis, J. Biol. Chem. 269, 25494-25501.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25494-25501
    • Jacobs, M.1    Freedman, S.J.2    Furie, B.C.3    Furie, B.4
  • 23
    • 0022483092 scopus 로고
    • The interaction of bovine factor IX, its activation intermediate, factor IX alpha, and its activation products, factor IXa alpha and factor IXa beta, with acidic phospholipid vesicles of various compositions
    • Beals, J. M., and Castellino, F. J. (1986) The interaction of bovine factor IX, its activation intermediate, factor IX alpha, and its activation products, factor IXa alpha and factor IXa beta, with acidic phospholipid vesicles of various compositions, Biochem. J. 236, 861-869.
    • (1986) Biochem. J. , vol.236 , pp. 861-869
    • Beals, J.M.1    Castellino, F.J.2
  • 26
    • 0029083550 scopus 로고
    • Structure of the calcium ion-bound γ-carboxyglutamic acid-rich domain of factor IX
    • Freedman, S. J., Furie, B. C., Furie, B., and Baleja, J. D. (1995) Structure of the calcium ion-bound γ-carboxyglutamic acid-rich domain of factor IX, Biochemistry 34, 12126-12137.
    • (1995) Biochemistry , vol.34 , pp. 12126-12137
    • Freedman, S.J.1    Furie, B.C.2    Furie, B.3    Baleja, J.D.4
  • 27
    • 0028986860 scopus 로고
    • Structure of the metal-free γ-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy
    • Freedman, S. J., Furie, B. C., Furie, B., and Baleja, J. D. (1995) Structure of the metal-free γ-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy, J. Biol. Chem. 270, 7980-7987.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7980-7987
    • Freedman, S.J.1    Furie, B.C.2    Furie, B.3    Baleja, J.D.4
  • 28
    • 0027532543 scopus 로고
    • Domain structure and domain-domain interactions in human coagulation factor IX
    • Vysotchin, A., Medved, L. V., and Ingham, K. C. (1993) Domain structure and domain-domain interactions in human coagulation factor IX, J. Biol. Chem. 268, 24339-24345.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24339-24345
    • Vysotchin, A.1    Medved, L.V.2    Ingham, K.C.3
  • 29
    • 0025800437 scopus 로고
    • Structure of bovine prothrombin fragment 1 refined at 2.25 Å resolution
    • Seshadri, T. P., Tulinsky, A., Skrzypczak-Jankun, E., and Park, C. H. (1991) Structure of bovine prothrombin fragment 1 refined at 2.25 Å resolution, J. Mol. Biol. 220, 481-494.
    • (1991) J. Mol. Biol. , vol.220 , pp. 481-494
    • Seshadri, T.P.1    Tulinsky, A.2    Skrzypczak-Jankun, E.3    Park, C.H.4
  • 30
    • 0028670884 scopus 로고
    • Functions of individual g-carboxyglutamic acid (gla) residues of human protein C. Determination of functionally nonessential Gla residues and correlations with their mode of binding to calcium
    • Christiansen, W. T., Tulinsky, A., and Castellino, F. J. (1994) Functions of individual g-carboxyglutamic acid (gla) residues of human protein C. Determination of functionally nonessential Gla residues and correlations with their mode of binding to calcium, Biochemistry 33, 14993-15000.
    • (1994) Biochemistry , vol.33 , pp. 14993-15000
    • Christiansen, W.T.1    Tulinsky, A.2    Castellino, F.J.3
  • 32
    • 0025737863 scopus 로고
    • Stucture-activity analysis of binding kinetics for NMDA receptor competitive antagonists: The influence of conformational restriction
    • Benveniste, M., and Mayer, M. L. (1991) Stucture-activity analysis of binding kinetics for NMDA receptor competitive antagonists: the influence of conformational restriction, Br. J. Pharmacol. 104, 207-221.
    • (1991) Br. J. Pharmacol. , vol.104 , pp. 207-221
    • Benveniste, M.1    Mayer, M.L.2
  • 33
    • 2342586724 scopus 로고    scopus 로고
    • Conformational analysis of drug-like molecules bound to proteins: An extensive study of ligand reorganization upon binding
    • Perola, E., and Charifson, P. S. (2004) Conformational analysis of drug-like molecules bound to proteins: an extensive study of ligand reorganization upon binding, J. Med. Chem. 47, 2499-2510.
    • (2004) J. Med. Chem. , vol.47 , pp. 2499-2510
    • Perola, E.1    Charifson, P.S.2
  • 34
    • 0034999419 scopus 로고    scopus 로고
    • Amino acid determinants for NMDA receptor inhibition by conantokin-T
    • Warder, S. E., Blandl, T., Klein, R. C., Castellino, F. J., and Prorok, M. (2001) Amino acid determinants for NMDA receptor inhibition by conantokin-T, J. Neurochem. 77, 812-822.
    • (2001) J. Neurochem. , vol.77 , pp. 812-822
    • Warder, S.E.1    Blandl, T.2    Klein, R.C.3    Castellino, F.J.4    Prorok, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.