메뉴 건너뛰기




Volumn 100, Issue 8, 2002, Pages 2812-2819

Protein S GLA-domain mutations causing impaired Ca2+-induced phospholipid binding and severe functional protein S deficiency

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; PHOSPHOLIPID; PROTEIN S; VITAMIN K GROUP;

EID: 0037108445     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-03-0909     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0002971870 scopus 로고    scopus 로고
    • Regulation of coagulation
    • Loscalzo J, Schafer Al, eds. Baltimore, MD: Williams and Wilkins
    • Simmonds RE, Lane DA. Regulation of coagulation. In: Loscalzo J, Schafer Al, eds. Thrombosis and Hemorrhage. 2nd ed. Baltimore, MD: Williams and Wilkins; 1998:45-76.
    • (1998) Thrombosis and Hemorrhage. 2nd ed. , pp. 45-76
    • Simmonds, R.E.1    Lane, D.A.2
  • 2
    • 0028832910 scopus 로고
    • The protein C anticoagulant system: Inherited defects as basis for venous thrombosis
    • Dahlback B. The protein C anticoagulant system: inherited defects as basis for venous thrombosis. Thromb Res. 1995;77:1-43.
    • (1995) Thromb Res , vol.77 , pp. 1-43
    • Dahlback, B.1
  • 3
    • 0029033740 scopus 로고
    • Protein C deficiency in a controlled series of unselected outpatients: An infrequent but clear clear risk factor for venous thrombosis (Leiden Thrombophilia Study)
    • Koster T, Rosendaal FR, Briet E, et al. Protein C deficiency in a controlled series of unselected outpatients: an infrequent but clear clear risk factor for venous thrombosis (Leiden Thrombophilia Study). Blood. 1995;85:2756-2761.
    • (1995) Blood , vol.85 , pp. 2756-2761
    • Koster, T.1    Rosendaal, F.R.2    Briet, E.3
  • 4
    • 0033678567 scopus 로고    scopus 로고
    • Protein S deficiency: A database of mutations - Summary of the first update: For the Plasma Coagulation Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis
    • Gandrille S, Borgel D, Sala N, et al. Protein S deficiency: a database of mutations - summary of the first update: for the Plasma Coagulation Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb Haemost. 2000;84:918.
    • (2000) Thromb Haemost , vol.84 , pp. 918
    • Gandrille, S.1    Borgel, D.2    Sala, N.3
  • 6
    • 10544236115 scopus 로고    scopus 로고
    • Identification of 19 protein S gene mutations in patients with phenotypic protein S deficiency and thrombosis: Protein S Study Group
    • Simmonds RE, Ireland H, Kunz G, Lane DA. Identification of 19 protein S gene mutations in patients with phenotypic protein S deficiency and thrombosis: Protein S Study Group. Blood. 1996; 88:4195-4204.
    • (1996) Blood , vol.88 , pp. 4195-4204
    • Simmonds, R.E.1    Ireland, H.2    Kunz, G.3    Lane, D.A.4
  • 7
    • 0036166536 scopus 로고    scopus 로고
    • Genetic and phenotypic variability between families with hereditary protein S deficiency
    • Rezende SM, Simmonds RE, Zoller B, et al. Genetic and phenotypic variability between families with hereditary protein S deficiency. Thromb Haemost. 2002;87:258-265.
    • (2002) Thromb Haemost , vol.87 , pp. 258-265
    • Rezende, S.M.1    Simmonds, R.E.2    Zoller, B.3
  • 8
    • 0032519708 scopus 로고    scopus 로고
    • Characterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulinlike domain
    • van Wijnen M, Stam JG, Chang GTG, et al. Characterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulinlike domain. Biochem J. 1998;330: 389-396.
    • (1998) Biochem J , vol.330 , pp. 389-396
    • Van Wijnen, M.1    Stam, J.G.2    Chang, G.T.G.3
  • 9
    • 0025098670 scopus 로고
    • Expression of completely gamma-carboxylated and beta-hydroxylated recombinant human vitamin-K-dependent protein S with full biological activity
    • Malm J, Cohen E, Dackowski W, Dahlback B, Wydro R. Expression of completely gamma-carboxylated and beta-hydroxylated recombinant human vitamin-K-dependent protein S with full biological activity. Eur J Biochem. 1990;187:737-743.
    • (1990) Eur J Biochem , vol.187 , pp. 737-743
    • Malm, J.1    Cohen, E.2    Dackowski, W.3    Dahlback, B.4    Wydro, R.5
  • 10
    • 0025303669 scopus 로고
    • Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies
    • Dahlback B, Hildebrand B, Malm J. Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies. J Biol Chem. 1990;265:8127-8135.
    • (1990) J Biol Chem , vol.265 , pp. 8127-8135
    • Dahlback, B.1    Hildebrand, B.2    Malm, J.3
  • 13
    • 0002437420 scopus 로고
    • Vitamin K-dependent proteins
    • Stamatoyannopoulos G, Nienhuis AW, Mejerus PW, Varmus H, eds. Philadelphia, PA: WB Saunders
    • Stenflo J, Dahlback B. Vitamin K-dependent proteins. In: Stamatoyannopoulos G, Nienhuis AW, Mejerus PW, Varmus H, eds. The molecular basis of blood diseases. 2nd ed. Philadelphia, PA: WB Saunders; 1994:565-597.
    • (1994) The molecular basis of blood diseases. 2nd ed. , pp. 565-597
    • Stenflo, J.1    Dahlback, B.2
  • 14
    • 0033559305 scopus 로고    scopus 로고
    • Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid
    • Furie B, Bouchard BA, Furie BC. Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid. Blood. 1999;93:1798-1808.
    • (1999) Blood , vol.93 , pp. 1798-1808
    • Furie, B.1    Bouchard, B.A.2    Furie, B.C.3
  • 15
    • 0026610682 scopus 로고
    • The calcium ion and membrane binding structure of the gla domain of Ca-prothrombin fragment 1
    • Soriano-Garcia M, Padmanabhan K, devos AM, Tulinsky A. The calcium ion and membrane binding structure of the gla domain of Ca-prothrombin fragment 1. Biochemistry. 1992;31:2554-2566.
    • (1992) Biochemistry , vol.31 , pp. 2554-2566
    • Soriano-Garcia, M.1    Padmanabhan, K.2    DeVos, A.M.3    Tulinsky, A.4
  • 16
    • 0029083550 scopus 로고
    • Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX
    • Freedman SJ, Furie BC, Furie B, Baleja JD. Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX. Biochemistry. 1995;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
  • 17
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner DW, D'Arcy A, Chene C, et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature. 1996; 380:41-46.
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chene, C.3
  • 18
    • 0035912739 scopus 로고    scopus 로고
    • Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X
    • Mizuno H, Fujimoto Z, Atoda H, Morita T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc Natl Acad Sci U S A. 2001;98:7230-7234.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7230-7234
    • Mizuno, H.1    Fujimoto, Z.2    Atoda, H.3    Morita, T.4
  • 19
    • 0030056114 scopus 로고    scopus 로고
    • Identification of the phospholipid binding site in the vitamin k-dependent blood coagulation protein factor IX
    • Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. Identification of the phospholipid binding site in the vitamin k-dependent blood coagulation protein factor IX. J Biol Chem. 1996; 271:16227-16236.
    • (1996) J Biol Chem , vol.271 , pp. 16227-16236
    • Freedman, S.J.1    Blostein, M.D.2    Baleja, J.D.3    Jacobs, M.4    Furie, B.C.5    Furie, B.6
  • 20
    • 0025773368 scopus 로고
    • The role of the epidermal growth factor-1 and hydrophobic stack domains of human factor IX in binding to endothelial cells
    • Cheung W-F, Straight D, Smith KJ, Lin S-W, Roberts HR, Stafford DW. The role of the epidermal growth factor-1 and hydrophobic stack domains of human factor IX in binding to endothelial cells. J Biol Chem. 1991;266:8797-8800.
    • (1991) J Biol Chem , vol.266 , pp. 8797-8800
    • Cheung, W.-F.1    Straight, D.2    Smith, K.J.3    Lin, S.-W.4    Roberts, H.R.5    Stafford, D.W.6
  • 21
    • 0026660188 scopus 로고
    • The binding of human factor IX to endothelial cells is mediated by residues 3-11
    • Cheung W-F, Nobuko H, Smith KJ, Stafford DW. The binding of human factor IX to endothelial cells is mediated by residues 3-11. J Biol Chem. 1992;267:20529-20531.
    • (1992) J Biol Chem , vol.267 , pp. 20529-20531
    • Cheung, W.-F.1    Nobuko, H.2    Smith, K.J.3    Stafford, D.W.4
  • 22
    • 0035968172 scopus 로고    scopus 로고
    • The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes
    • Falls LA, Furie BC, Jacobs M, Furie B, Rigby AC. The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes. J Biol Chem. 2001;276:23895-23902.
    • (2001) J Biol Chem , vol.276 , pp. 23895-23902
    • Falls, L.A.1    Furie, B.C.2    Jacobs, M.3    Furie, B.4    Rigby, A.C.5
  • 23
    • 0029148317 scopus 로고
    • Hydrophobic amino acid residues of human anticoagulant protein C that contribute to its functional binding to phospholipid vesicles
    • Christiansen WT, Jalbert LR, Robertson RM, Jhingan A, Prorok M, Castellino FJ. Hydrophobic amino acid residues of human anticoagulant protein C that contribute to its functional binding to phospholipid vesicles. Biochemistry. 1995;34: 10376-10382.
    • (1995) Biochemistry , vol.34 , pp. 10376-10382
    • Christiansen, W.T.1    Jalbert, L.R.2    Robertson, R.M.3    Jhingan, A.4    Prorok, M.5    Castellino, F.J.6
  • 24
    • 0029945107 scopus 로고    scopus 로고
    • The hydrophobic nature of residue-5 human protein C is a major determinant of its functional interactions with acidic phospholipid vesicles
    • Jalbert LR, Chan JCY, Christiansen WT, Castellino FJ. The hydrophobic nature of residue-5 human protein C is a major determinant of its functional interactions with acidic phospholipid vesicles. Biochemistry. 1996;35:7093-7099.
    • (1996) Biochemistry , vol.35 , pp. 7093-7099
    • Jalbert, L.R.1    Chan, J.C.Y.2    Christiansen, W.T.3    Castellino, F.J.4
  • 25
    • 0027968913 scopus 로고
    • The binding energy of human coagulation protein C to acidic phospholipid vesicles contains a major contribution from leucine 5 in the gamma-carboxyglutamic acid domain
    • Zhang L, Castellino FJ. The binding energy of human coagulation protein C to acidic phospholipid vesicles contains a major contribution from leucine 5 in the gamma-carboxyglutamic acid domain. J Biol Chem. 1994;269:3590-3595.
    • (1994) J Biol Chem , vol.269 , pp. 3590-3595
    • Zhang, L.1    Castellino, F.J.2
  • 26
    • 0017875774 scopus 로고
    • Interaction of vitamin K dependent proteins with membranes
    • Nelsestuen GL, Kisiel W, Di Scipio RG. Interaction of vitamin K dependent proteins with membranes. Biochemistry. 1978;17:2134-2138.
    • (1978) Biochemistry , vol.17 , pp. 2134-2138
    • Nelsestuen, G.L.1    Kisiel, W.2    Di Scipio, R.G.3
  • 27
    • 0030967015 scopus 로고    scopus 로고
    • Comparison of naturally occurring vitamin K-dependent proteins: Correlation of amino acid sequences and membrane binding properties suggests a membrane contact site
    • McDonald JF, Shah AM, Schwalbe RA, Kisiel W, Dahlback B, Nelsestuen GL. Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site. Biochemistry. 1997;36:5120-5127.
    • (1997) Biochemistry , vol.36 , pp. 5120-5127
    • McDonald, J.F.1    Shah, A.M.2    Schwalbe, R.A.3    Kisiel, W.4    Dahlback, B.5    Nelsestuen, G.L.6
  • 28
    • 0032515998 scopus 로고    scopus 로고
    • Manipulation of the membrane binding site of vitamin K-dependent proteins: Enhanced biological function of human factor VII
    • Shah AM, Kisiel W, Foster DC, Nelsestuen GL. Manipulation of the membrane binding site of vitamin K-dependent proteins: enhanced biological function of human factor VII. Proc Natl Acad Sci U S A. 1998;95:4229-4234.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4229-4234
    • Shah, A.M.1    Kisiel, W.2    Foster, D.C.3    Nelsestuen, G.L.4
  • 29
    • 0032553444 scopus 로고    scopus 로고
    • Enhancement of human protein C function by site-directed mutagenesis of the gamacarboxyglutamic acid domain
    • Shen L, Shah AM, Dahlback B, Nelsestuen GL. Enhancement of human protein C function by site-directed mutagenesis of the gamacarboxyglutamic acid domain. J Biol Chem. 1998;273: 31086-31091.
    • (1998) J Biol Chem , vol.273 , pp. 31086-31091
    • Shen, L.1    Shah, A.M.2    Dahlback, B.3    Nelsestuen, G.L.4
  • 30
    • 0019849380 scopus 로고
    • Regulation of activated protein C by protein S: The role of phospholipid in factor Va inactivation
    • Walker FJ. Regulation of activated protein C by protein S: the role of phospholipid in factor Va inactivation. J Biol Chem. 1981;256:11128-11131.
    • (1981) J Biol Chem , vol.256 , pp. 11128-11131
    • Walker, F.J.1
  • 31
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann KG, Nesheim ME, Church WR, Haley P, Krishnaswamy S. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood. 1990;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
  • 32
    • 0029808712 scopus 로고    scopus 로고
    • The interaction of protein S with the phospholipid surface is essential for the activated protein C-independent activity of protein S
    • van Wijnen M, Stam JG, van't Veer C, et al. The interaction of protein S with the phospholipid surface is essential for the activated protein C-independent activity of protein S. Thromb Haemost. 1996;76:397-403.
    • (1996) Thromb Haemost , vol.76 , pp. 397-403
    • Van Wijnen, M.1    Stam, J.G.2    Van't Veer, C.3
  • 33
    • 0032496225 scopus 로고    scopus 로고
    • Human protein S cleavage and inactivation by coagulation factor Xa
    • Long GL, Lu D, Xie RL, Kalafatis M. Human protein S cleavage and inactivation by coagulation factor Xa. J Biol Chem. 1998;273:11521-11526.
    • (1998) J Biol Chem , vol.273 , pp. 11521-11526
    • Long, G.L.1    Lu, D.2    Xie, R.L.3    Kalafatis, M.4
  • 34
    • 0027513138 scopus 로고
    • Protein S binding to human endothelial cells is required for expression of cofactor activity for activated protein C
    • Hackeng TM, Hessing M, van't Veer C, et al. Protein S binding to human endothelial cells is required for expression of cofactor activity for activated protein C. J Biol Chem. 1993;268:3993-4000.
    • (1993) J Biol Chem , vol.268 , pp. 3993-4000
    • Hackeng, T.M.1    Hessing, M.2    Van't Veer, C.3
  • 35
    • 0032502796 scopus 로고    scopus 로고
    • A chimeric protein C containing the prothombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity
    • Smirnov MD, Safa O, Regan L, et al. A chimeric protein C containing the prothombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity. J Biol Chem. 1998; 273:9031-9040.
    • (1998) J Biol Chem , vol.273 , pp. 9031-9040
    • Smirnov, M.D.1    Safa, O.2    Regan, L.3
  • 36
    • 0031137254 scopus 로고    scopus 로고
    • A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S: From biostructural pathology to species-specific cofactor activity
    • Villoutreix BO, Teleman O, Dahlback B. A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S: from biostructural pathology to species-specific cofactor activity. J Comput Aided Mol Des. 1997;11:293-304.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 293-304
    • Villoutreix, B.O.1    Teleman, O.2    Dahlback, B.3
  • 37
    • 0029031301 scopus 로고
    • Structure-function assessment of the role of the helical stack domain in the properties of human recombinant protein C and activated protein C
    • Christiansen WT, Geng J-P, Castellino FJ. Structure-function assessment of the role of the helical stack domain in the properties of human recombinant protein C and activated protein C. Biochemistry. 1995;34:8082-8090.
    • (1995) Biochemistry , vol.34 , pp. 8082-8090
    • Christiansen, W.T.1    Geng, J.-P.2    Castellino, F.J.3
  • 38
    • 0028871033 scopus 로고
    • Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene
    • Gandriile S, Borgel D, Eschwege-Gufflet V, et al. Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene. Blood. 1995;85:130-138.
    • (1995) Blood , vol.85 , pp. 130-138
    • Gandriile, S.1    Borgel, D.2    Eschwege-Gufflet, V.3
  • 39
    • 0032492690 scopus 로고    scopus 로고
    • Structure/function analyses of recombinant variants of human factor Xa: Factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles
    • Larson PJ, Camire RM, Wong D, et al. Structure/function analyses of recombinant variants of human factor Xa: factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles. Biochemistry. 1998;37:5029-5038.
    • (1998) Biochemistry , vol.37 , pp. 5029-5038
    • Larson, P.J.1    Camire, R.M.2    Wong, D.3
  • 40
    • 0027358796 scopus 로고
    • The importance of specific gamma-carboxyglutamic acid residues in prothrombin: Evaluation by site-specific mutagenesis
    • Ratcliffe JV, Furie B, Furie BC. The importance of specific gamma-carboxyglutamic acid residues in prothrombin: evaluation by site-specific mutagenesis. J Biol Chem. 1993;268:24339-24345.
    • (1993) J Biol Chem , vol.268 , pp. 24339-24345
    • Ratcliffe, J.V.1    Furie, B.2    Furie, B.C.3
  • 41
    • 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, Castelino FJ. Role of individual gamma-carboxyglutamic acid residues of activated human protein C in defining its in vitro anticoagulant activity. Blood. 1992;80:942-952.
    • (1992) Blood , vol.80 , pp. 942-952
    • Zhang, L.1    Jhingan, A.2    Castelino, F.J.3
  • 42
    • 0029671099 scopus 로고    scopus 로고
    • Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa is required for its binding to cofactor VIIIa
    • Larson PJ, Stanfield-Oakley SA, VanDusen WJ, et al. Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa is required for its binding to cofactor VIIIa. J Biol Chem. 1996;271:3869-3876.
    • (1996) J Biol Chem , vol.271 , pp. 3869-3876
    • Larson, P.J.1    Stanfield-Oakley, S.A.2    VanDusen, W.J.3
  • 43
    • 0030844859 scopus 로고    scopus 로고
    • Hemophilia B: Database of point mutations and short additions and deletions
    • Giannelli F, Green PM, Sommer SS, et al. Hemophilia B: database of point mutations and short additions and deletions. Nucleic Acids Res. 1997; 25:133-135.
    • (1997) Nucleic Acids Res , vol.25 , pp. 133-135
    • Giannelli, F.1    Green, P.M.2    Sommer, S.S.3
  • 44
    • 0023154513 scopus 로고
    • Cloning and characterization of human liver cDNA encoding a protein S precursor
    • Hoskins J, Norman DK, Beckmann RJ, Long GL. Cloning and characterization of human liver cDNA encoding a protein S precursor. Proc Natl Acad Sci U S A. 1987;84:349-353.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 349-353
    • Hoskins, J.1    Norman, D.K.2    Beckmann, R.J.3    Long, G.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.