메뉴 건너뛰기




Volumn 123, Issue 25, 2014, Pages 3979-3987

TFPI cofactor function of protein S: Essential role of the protein S SHBG-like domain

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C4B BINDING PROTEIN; PROTEIN S; SEX HORMONE BINDING GLOBULIN; TISSUE FACTOR PATHWAY INHIBITOR;

EID: 84902668872     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2014-01-551812     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 0023924263 scopus 로고
    • Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains
    • Wun TC, Kretzmer KK, Girard TJ, Miletich JP, Broze GJ Jr. Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains. J Biol Chem. 1988;263(13):6001-6004.
    • (1988) J Biol Chem , vol.263 , Issue.13 , pp. 6001-6004
    • Wun, T.C.1    Kretzmer, K.K.2    Girard, T.J.3    Miletich, J.P.4    Broze Jr., G.J.5
  • 2
    • 84860303349 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: Structure-function
    • Broze GJ Jr, Girard TJ. Tissue factor pathway inhibitor: structure-function. Front Biosci (Landmark Ed). 2012;17:262-280.
    • (2012) Front Biosci (Landmark Ed) , vol.17 , pp. 262-280
    • Broze Jr., G.J.1    Girard, T.J.2
  • 3
    • 0038481254 scopus 로고    scopus 로고
    • Low levels of tissue factor pathway inhibitor (TFPI) increase the risk of venous thrombosis
    • DOI 10.1182/blood-2002-10-3188
    • Dahm A, Van Hylckama Vlieg A, Bendz B, Rosendaal F, Bertina RM, Sandset PM. Low levels of tissue factor pathway inhibitor (TFPI) increase the risk of venous thrombosis. Blood. 2003;101(11):4387-4392. (Pubitemid 36857803)
    • (2003) Blood , vol.101 , Issue.11 , pp. 4387-4392
    • Dahm, A.1    Van Hylckama, V.A.2    Bendz, B.3    Rosendaal, F.4    Bertina, R.M.5    Sandset, P.M.6
  • 5
    • 0026341831 scopus 로고
    • The C-terminus of tissue factor pathway inhibitor is essential to its anticoagulant activity
    • Nordfang O, Bjørn SE, Valentin S, et al. The C-terminus of tissue factor pathway inhibitor is essential to its anticoagulant activity. Biochemistry. 1991;30(43):10371-10376.
    • (1991) Biochemistry , vol.30 , Issue.43 , pp. 10371-10376
    • Nordfang, O.1    Bjørn, S.E.2    Valentin, S.3
  • 6
    • 0028154010 scopus 로고
    • Kinetics of the inhibition of human factor Xa by full-length and truncated recombinant tissue factor pathway inhibitor
    • Lindhout T, Willems G, Blezer R, Hemker HC. Kinetics of the inhibition of human factor Xa by full-length and truncated recombinant tissue factor pathway inhibitor. Biochem J. 1994;297(Pt 1):131-136. (Pubitemid 24025614)
    • (1994) Biochemical Journal , vol.297 , Issue.1 , pp. 131-136
    • Lindhout, T.1    Willems, G.2    Blezer, R.3    Hemker, H.C.4
  • 7
    • 0026668480 scopus 로고
    • Tissue factor pathway inhibitor: The carboxy-terminus is required for optimal inhibition of factor Xa
    • Wesselschmidt R, Likert K, Girard T, Wun TC, Broze GJ Jr. Tissue factor pathway inhibitor: the carboxy-terminus is required for optimal inhibition of factor Xa. Blood. 1992;79(8):2004-2010.
    • (1992) Blood. , vol.79 , Issue.8 , pp. 2004-2010
    • Wesselschmidt, R.1    Likert, K.2    Girard, T.3    Wun, T.C.4    Broze Jr., G.J.5
  • 8
    • 0030738021 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor gene disruption produces intrauterine lethality in mice
    • Huang ZF, Higuchi D, Lasky N, Broze GJ Jr. Tissue factor pathway inhibitor gene disruption produces intrauterine lethality in mice. Blood. 1997;90(3):944-951. (Pubitemid 27314126)
    • (1997) Blood , vol.90 , Issue.3 , pp. 944-951
    • Huang, Z.-F.1    Higuchi, D.2    Lasky, N.3    Broze Jr., G.J.4
  • 10
    • 0031964419 scopus 로고    scopus 로고
    • Clarification of the risk for venous thrombosis associated with hereditary protein S deficiency by investigation of a large kindred with a characterized gene defect
    • Simmonds RE, Ireland H, Lane DA, Zöller B, García de Frutos P, Dahlbäck B. Clarification of the risk for venous thrombosis associated with hereditary protein S deficiency by investigation of a large kindred with a characterized gene defect. Ann Intern Med. 1998;128(1):8-14.
    • (1998) Ann Intern Med , vol.128 , Issue.1 , pp. 8-14
    • Simmonds, R.E.1    Ireland, H.2    Lane, D.A.3    Zöller, B.4    García De Frutos, P.5    Dahlbäck, B.6
  • 11
    • 0023851665 scopus 로고
    • The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: Insight into its possible mechanism of action
    • Broze GJ Jr, Warren LA, Novotny WF, Higuchi DA, Girard JJ, Miletich JP. The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action. Blood. 1988;71(2):335-343. (Pubitemid 18089519)
    • (1988) Blood , vol.71 , Issue.2 , pp. 335-343
    • Broze Jr., G.J.1    Warren, L.A.2    Novotny, W.F.3    Higuchi, D.A.4    Girard, J.J.5    Miletich, J.P.6
  • 12
    • 0021792015 scopus 로고
    • Inhibition of tissue factor/factor VIIa activity in plasma requires factor X and an additional plasma component
    • Sanders NL, Bajaj SP, Zivelin A, Rapaport SI. Inhibition of tissue factor/factor VIIa activity in plasma requires factor X and an additional plasma component. Blood. 1985;66(1):204-212. (Pubitemid 15004805)
    • (1985) Blood , vol.66 , Issue.1 , pp. 204-212
    • Sanders, N.L.1    Bajaj, S.P.2    Zivelin, A.3    Rapaport, S.I.4
  • 13
    • 0024543984 scopus 로고
    • Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor
    • DOI 10.1038/338518a0
    • Girard TJ, Warren LA, Novotny WF, et al. Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature. 1989;338(6215):518-520. (Pubitemid 19107996)
    • (1989) Nature , vol.338 , Issue.6215 , pp. 518-520
    • Girard, T.J.1    Warren, L.A.2    Novotny, W.F.3    Likert, K.M.4    Brown, S.G.5    Miletich, J.P.6    Broze Jr., G.J.7
  • 14
    • 0027724106 scopus 로고
    • Kinetics of factor Xa inhibition by tissue factor pathway inhibitor
    • Huang ZF, Wun TC, Broze GJ Jr. Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J Biol Chem. 1993;268(36):26950-26955.
    • (1993) J Biol Chem. , vol.268 , Issue.36 , pp. 26950-26955
    • Huang, Z.F.1    Wun, T.C.2    Broze Jr., G.J.3
  • 16
    • 77956547096 scopus 로고    scopus 로고
    • The Kunitz-3 domain of TFPI-alpha is required for protein S-dependent enhancement of factor Xa inhibition
    • Ndonwi M, Tuley EA, Broze GJ Jr. The Kunitz-3 domain of TFPI-alpha is required for protein S-dependent enhancement of factor Xa inhibition. Blood. 2010;116(8):1344-1351.
    • (2010) Blood. , vol.116 , Issue.8 , pp. 1344-1351
    • Ndonwi, M.1    Tuley, E.A.2    Broze Jr., G.J.3
  • 17
    • 84871080504 scopus 로고    scopus 로고
    • Identification of functionally important residues in TFPI Kunitz domain 3 required for the enhancement of its activity by protein S
    • Ahnström J, Andersson HM, Hockey V, et al. Identification of functionally important residues in TFPI Kunitz domain 3 required for the enhancement of its activity by protein S. Blood. 2012;120(25):5059-5062.
    • (2012) Blood. , vol.120 , Issue.25 , pp. 5059-5062
    • Ahnström, J.1    Andersson, H.M.2    Hockey, V.3
  • 19
    • 0023689701 scopus 로고
    • Structural study of long arm fragments of laminin. Evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chains
    • Deutzmann R, Huber J, Schmetz KA, Oberbäumer I, Hartl L. Structural study of long arm fragments of laminin. Evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chains. Eur J Biochem. 1988;177(1):35-45.
    • (1988) Eur J Biochem. , vol.177 , Issue.1 , pp. 35-45
    • Deutzmann, R.1    Huber, J.2    Schmetz, K.A.3    Oberbäumer, I.4    Hartl, L.5
  • 20
    • 0026691698 scopus 로고
    • Sex hormone-binding globulin, androgen-binding protein, and vitamin K-dependent protein S are homologous to laminin A, merosin, and Drosophila crumbs protein
    • Joseph DR, Baker ME. Sex hormone-binding globulin, androgen-binding protein, and vitamin K-dependent protein S are homologous to laminin A, merosin, and Drosophila crumbs protein. FASEB J. 1992;6(7):2477-2481.
    • (1992) FASEB J , vol.6 , Issue.7 , pp. 2477-2481
    • Joseph, D.R.1    Baker, M.E.2
  • 21
    • 0025313879 scopus 로고
    • Inhibition of cofactor activity of protein S by a complex of protein S and C4b-binding protein. Evidence for inactive ternary complex formation between protein S, C4b-binding protein, and activated protein C
    • Nishioka J, Suzuki K. Inhibition of cofactor activity of protein S by a complex of protein S and C4b-binding protein. Evidence for inactive ternary complex formation between protein S, C4b-binding protein, and activated protein C. J Biol Chem. 1990;265(16):9072-9076.
    • (1990) J Biol Chem. , vol.265 , Issue.16 , pp. 9072-9076
    • Nishioka, J.1    Suzuki, K.2
  • 22
    • 0022929854 scopus 로고
    • Inhibition of protein C(a) cofactor function of human and bovine protein S by C4b-binding protein
    • Dahlbäck B. Inhibition of protein Ca cofactor function of human and bovine protein S by C4b-binding protein. J Biol Chem. 1986;261(26):12022-12027. (Pubitemid 17202758)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.26 , pp. 12022-12027
    • Dahlback, B.1
  • 23
    • 55949086628 scopus 로고    scopus 로고
    • Protein S deficiency: A clinical perspective
    • ten Kate MK, van der Meer J. Protein S deficiency: a clinical perspective. Haemophilia. 2008;14(6):1222-1228.
    • (2008) Haemophilia , vol.14 , Issue.6 , pp. 1222-1228
    • Ten Kate, M.K.1    Van Der Meer, J.2
  • 24
    • 0344765519 scopus 로고    scopus 로고
    • The SHBG-like region of protein S is crucial for factor V-dependent APC-cofactor function
    • Nyberg P, Dahlbäck B, García de Frutos P. The SHBG-like region of protein S is crucial for factor V-dependent APC-cofactor function. FEBS Lett. 1998;433(1-2):28-32.
    • (1998) FEBS Lett , vol.433 , Issue.1-2 , pp. 28-32
    • Nyberg, P.1    Dahlbäck, B.2    García De Frutos, P.3
  • 25
    • 0033854083 scopus 로고    scopus 로고
    • The second laminin G-type domain of protein S is indispensable for expression of full cofactor activity in activated protein C-catalysed inactivation of factor Va and factor VIIIa
    • Evenäs P, García de Frutos P, Nicolaes GA, Dahlbäck B. The second laminin G-type domain of protein S is indispensable for expression of full cofactor activity in activated protein C-catalysed inactivation of factor Va and factor VIIIa. Thromb Haemost. 2000;84(2):271-277.
    • (2000) Thromb Haemost , vol.84 , Issue.2 , pp. 271-277
    • Evenäs, P.1    García De Frutos, P.2    Nicolaes, G.A.3    Dahlbäck, B.4
  • 26
    • 77954707351 scopus 로고    scopus 로고
    • Activated protein C cofactor function of protein S: A critical role for Asp95 in the EGF1-like domain
    • Andersson HM, Arantes MJ, Crawley JT, et al. Activated protein C cofactor function of protein S: a critical role for Asp95 in the EGF1-like domain. Blood. 2010;115(23):4878-4885.
    • (2010) Blood , vol.115 , Issue.23 , pp. 4878-4885
    • Andersson, H.M.1    Arantes, M.J.2    Crawley, J.T.3
  • 27
    • 79959187738 scopus 로고    scopus 로고
    • Activated protein C cofactor function of protein S: A novel role for a γ-carboxyglutamic acid residue
    • Ahnström J, Andersson HM, Canis K, et al. Activated protein C cofactor function of protein S: a novel role for a γ-carboxyglutamic acid residue. Blood. 2011;117(24):6685-6693.
    • (2011) Blood , vol.117 , Issue.24 , pp. 6685-6693
    • Ahnström, J.1    Andersson, H.M.2    Canis, K.3
  • 28
    • 11144240514 scopus 로고    scopus 로고
    • The gamma-carboxyglutamic acid domain of anticoagulant protein S is involved in activated protein C cofactor activity, independently of phospholipid binding
    • DOI 10.1182/blood-2004-06-2176
    • Saller F, Villoutreix BO, Amelot A, et al. The gamma-carboxyglutamic acid domain of anticoagulant protein S is involved in activated protein C cofactor activity, independently of phospholipid binding. Blood. 2005;105(1):122-130. (Pubitemid 40053073)
    • (2005) Blood , vol.105 , Issue.1 , pp. 122-130
    • Saller, F.1    Villoutreix, B.O.2    Amelot, A.3    Kaabache, T.4    Le, B.B.F.5    Aiach, M.6    Gandrille, S.7    Borgel, D.8
  • 30
    • 0025303669 scopus 로고
    • Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies
    • Dahlbäck 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(14):8127-8135.
    • (1990) J Biol Chem , vol.265 , Issue.14 , pp. 8127-8135
    • Dahlbäck, B.1    Hildebrand, B.2    Malm, J.3
  • 31
    • 0043092166 scopus 로고    scopus 로고
    • Importance of Protein S and Phospholipid for Activated Protein C-mediated Cleavages in Factor Va
    • DOI 10.1074/jbc.M303829200
    • Norstrøm EA, Steen M, Tran S, Dahlbäck B. Importance of protein S and phospholipid for activated protein C-mediated cleavages in factor Va. J Biol Chem. 2003;278(27):24904-24911. (Pubitemid 37548650)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24904-24911
    • Norstrom, E.A.1    Steen, M.2    Tran, S.3    Dahlback, B.4
  • 32
    • 0021210064 scopus 로고
    • Ultrastructure of C4b-binding protein fragments formed by limited proteolysis using chymotrypsin
    • Dahlbäck B, Müller-Eberhard HJ. Ultrastructure of C4b-binding protein fragments formed by limited proteolysis using chymotrypsin. J Biol Chem. 1984;259(19):11631-11634. (Pubitemid 14022071)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.19 , pp. 11631-11634
    • Dahlback, B.1    Muller-Eberhard, H.J.2
  • 33
    • 0022650448 scopus 로고
    • Unusual ultrastructure of complement-component-C4b-binding protein of human complement by synchroton X-ray scattering and hydrodynamic analysis
    • Perkins SJ, Chung LP, Reid KB. Unusual ultrastructure of complement-component-C4b-binding protein of human complement by synchrotron X-ray scattering and hydrodynamic analysis. Biochem J. 1986;233(3):799-807. (Pubitemid 16116154)
    • (1986) Biochemical Journal , vol.233 , Issue.3 , pp. 799-807
    • Perkins, S.J.1    Chung, L.P.2    Reid, K.B.M.3
  • 34
    • 74749084650 scopus 로고    scopus 로고
    • Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma
    • Castoldi E, Simioni P, Tormene D, Rosing J, Hackeng TM. Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma. J Thromb Haemost. 2010;8(2):294-300.
    • (2010) J Thromb Haemost , vol.8 , Issue.2 , pp. 294-300
    • Castoldi, E.1    Simioni, P.2    Tormene, D.3    Rosing, J.4    Hackeng, T.M.5
  • 35
    • 84891831625 scopus 로고    scopus 로고
    • Protein S is a cofactor for platelet and endothelial tissue factor pathway inhibitor-α but not for cell surface-associated tissue factor pathway inhibitor
    • Wood JP, Ellery PE, Maroney SA, Mast AE. Protein S is a cofactor for platelet and endothelial tissue factor pathway inhibitor-α but not for cell surface-associated tissue factor pathway inhibitor. Arterioscler Thromb Vasc Biol. 2014;34(1):169-176.
    • (2014) Arterioscler Thromb Vasc Biol , vol.34 , Issue.1 , pp. 169-176
    • Wood, J.P.1    Ellery, P.E.2    Maroney, S.A.3    Mast, A.E.4
  • 37
    • 0035342451 scopus 로고    scopus 로고
    • Three-dimensional model of the SHBG-like region of anticoagulant protein S: New structure-function insights
    • Villoutreix BO, Dahlbäck B, Borgel D, Gandrille S, Muller YA. Three-dimensional model of the SHBG-like region of anticoagulant protein S: new structure-function insights. Proteins. 2001;43(2):203-216.
    • (2001) Proteins. , vol.43 , Issue.2 , pp. 203-216
    • Villoutreix, B.O.1    Dahlbäck, B.2    Borgel, D.3    Gandrille, S.4    Muller, Y.A.5
  • 38
    • 0037177873 scopus 로고    scopus 로고
    • Structural requirements of anticoagulant, protein S for its binding to the complement regulator C4b-binding protein
    • DOI 10.1074/jbc.M103036200
    • Giri TK, Linse S, García de Frutos P, Yamazaki T, Villoutreix BO, Dahlbäck B. Structural requirements of anticoagulant protein S for its binding to the complement regulator C4b-binding protein. J Biol Chem. 2002;277(17):15099-15106. (Pubitemid 34952588)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 15099-15106
    • Giri, T.K.1    Linse, S.2    De Frutos, P.G.3    Yamazaki, T.4    Villoutreix, B.O.5    Dahlback, B.6
  • 39
    • 0033573154 scopus 로고    scopus 로고
    • Both G-type domains of protein S are required for the high-affinity interaction with C4b-binding protein
    • Evenäs P, García De Frutos P, Linse S, Dahlbäck B. Both G-type domains of protein S are required for the high-affinity interaction with C4b-binding protein. Eur J Biochem. 1999;266(3):935-942.
    • (1999) Eur J Biochem , vol.266 , Issue.3 , pp. 935-942
    • Evenäs, P.1    García De Frutos, P.2    Linse, S.3    Dahlbäck, B.4
  • 40
    • 0029982380 scopus 로고    scopus 로고
    • Factor Xa enhances the binding of tissue factor pathway inhibitor to acidic phospholipids
    • Valentin S, Schousboe I. Factor Xa enhances the binding of tissue factor pathway inhibitor to acidic phospholipids. Thromb Haemost. 1996;75(5):796-800. (Pubitemid 26181856)
    • (1996) Thrombosis and Haemostasis , vol.75 , Issue.5 , pp. 796-800
    • Valentin, S.1    Schousboe, I.2
  • 41
    • 0032502244 scopus 로고    scopus 로고
    • Transient high affinity binding of tissue factor pathway inhibitor- factor Xa complexes to negatively charged phospholipid membranes
    • DOI 10.1021/bi972194+
    • Willems GM, Janssen MP, Salemink I, Wun TC, Lindhout T. Transient high affinity binding of tissue factor pathway inhibitor-factor Xa complexes to negatively charged phospholipid membranes. Biochemistry. 1998;37(10):3321-3328. (Pubitemid 28125559)
    • (1998) Biochemistry , vol.37 , Issue.10 , pp. 3321-3328
    • Willems, G.M.1    Janssen, M.P.2    Salemink, I.3    Wun, T.-C.4    Lindhout, T.5
  • 42
    • 0037039284 scopus 로고    scopus 로고
    • Structural mechanism for heparin-binding of the third Kunitz domain of human tissue factor pathway inhibitor
    • DOI 10.1021/bi011299g
    • Mine S, Yamazaki T, Miyata T, Hara S, Kato H. Structural mechanism for heparin-binding of the third Kunitz domain of human tissue factor pathway inhibitor. Biochemistry. 2002;41(1):78-85. (Pubitemid 34049383)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 78-85
    • Mine, S.1    Yamazaki, T.2    Miyata, T.3    Hara, S.4    Kato, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.