메뉴 건너뛰기




Volumn 108, Issue 2, 2012, Pages 266-276

The Kunitz 1 and Kunitz 3 domains of tissue factor pathway inhibitor are required for efficient inhibition of factor Xa

Author keywords

Anticoagulant; Factor Xa; Protein S; TFPI

Indexed keywords

BLOOD CLOTTING FACTOR 10A; CALCIUM ION; EDETIC ACID; KUNITZ DOMAIN PROTEIN; LEUKOCYTE ELASTASE; PEPTIDES AND PROTEINS; PROTEIN S; TISSUE FACTOR PATHWAY INHIBITOR; UNCLASSIFIED DRUG;

EID: 84864330024     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH11-12-0902     Document Type: Article
Times cited : (23)

References (28)
  • 2
    • 0001495165 scopus 로고
    • Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque
    • Wilcox JN, Smith KM, Schwartz SM, et al. Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque. Proc Natl Acad Sci USA 1989; 86: 2839-2843.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2839-2843
    • Wilcox, J.N.1    Smith, K.M.2    Schwartz, S.M.3
  • 3
    • 0027402655 scopus 로고
    • Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation
    • Morrissey JH, Macik BG, Neuenschwander PF, et al. Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation. Blood 1993; 81: 734-744.
    • (1993) Blood , vol.81 , pp. 734-744
    • Morrissey, J.H.1    Macik, B.G.2    Neuenschwander, P.F.3
  • 4
    • 0013879315 scopus 로고
    • The reaction between bovine brain tissue factor and factors VII and X
    • Nemerson Y. The reaction between bovine brain tissue factor and factors VII and X. Biochemistry 1966; 5: 601-608.
    • (1966) Biochemistry , vol.5 , pp. 601-608
    • Nemerson, Y.1
  • 5
    • 0017639138 scopus 로고
    • Activation of factor IX by the reaction product of tissue factor and factor VII: Additional pathway for initiating blood coagulation
    • Osterud B, Rapaport SI. Activation of factor IX by the reaction product of tissue factor and factor VII: additional pathway for initiating blood coagulation. Proc Natl Acad Sci USA 1977; 74: 5260-5264.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5260-5264
    • Osterud, B.1    Rapaport, S.I.2
  • 6
    • 0024543984 scopus 로고
    • Functional significance of the Kunitztype inhibitory domains of lipoprotein-associated coagulation inhibitor
    • Girard TJ, Warren LA, Novotny WF, et al. Functional significance of the Kunitztype inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature 1989; 338: 518-520.
    • (1989) Nature , vol.338 , pp. 518-520
    • Girard, T.J.1    Warren, L.A.2    Novotny, W.F.3
  • 7
    • 0029082791 scopus 로고
    • Tissue factor pathway inhibitor
    • Broze GJ, Jr. Tissue factor pathway inhibitor. Thromb Haemost 1995; 74: 90-93.
    • (1995) Thromb Haemost , vol.74 , pp. 90-93
    • Broze Jr., G.J.1
  • 8
    • 0345195222 scopus 로고    scopus 로고
    • Inhibitory mechanism of the protein C pathway on tissue factor-induced thrombin generation. Synergistic effect in combination with tissue factor pathway inhibitor
    • van 't Veer C, Golden NJ, Kalafatis M, et al. Inhibitory mechanism of the protein C pathway on tissue factor-induced thrombin generation. Synergistic effect in combination with tissue factor pathway inhibitor. J Biol Chem 1997; 272: 7983-7994.
    • (1997) J Biol Chem , vol.272 , pp. 7983-7994
    • van 't Veer, C.1    Golden, N.J.2    Kalafatis, M.3
  • 9
    • 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, et al. 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: 6001-6004.
    • (1988) J Biol Chem , vol.263 , pp. 6001-6004
    • Wun, T.C.1    Kretzmer, K.K.2    Girard, T.J.3
  • 10
    • 0027363207 scopus 로고
    • Structural requirements for tissue factor pathway inhibitor interactions with factor Xa and heparin
    • Wesselschmidt R, Likert K, Huang Z, et al. Structural requirements for tissue factor pathway inhibitor interactions with factor Xa and heparin. Blood Coagul Fibrinolysis 1993; 4: 661-669.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 661-669
    • Wesselschmidt, R.1    Likert, K.2    Huang, Z.3
  • 11
    • 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: 1344-1351.
    • (2010) Blood , vol.116 , pp. 1344-1351
    • Ndonwi, M.1    Tuley, E.A.2    Broze Jr., G.J.3
  • 12
    • 33644772164 scopus 로고    scopus 로고
    • Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor
    • Hackeng TM, Sere KM, Tans G, et al. Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor. Proc Natl Acad Sci USA 2006; 103: 3106-3111.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3106-3111
    • Hackeng, T.M.1    Sere, K.M.2    Tans, G.3
  • 13
    • 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, et al. 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: 335-343.
    • (1988) Blood , vol.71 , pp. 335-343
    • Broze Jr., G.J.1    Warren, L.A.2    Novotny, W.F.3
  • 14
    • 0024991650 scopus 로고
    • Regulation of coagulation by a multivalent Kunitz-type inhibitor
    • Broze GJ, Jr., Girard TJ, Novotny WF. Regulation of coagulation by a multivalent Kunitz-type inhibitor. Biochemistry 1990; 29: 7539-7546.
    • (1990) Biochemistry , vol.29 , pp. 7539-7546
    • Broze Jr., G.J.1    Girard, T.J.2    Novotny, W.F.3
  • 15
    • 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: 26950-26955.
    • (1993) J Biol Chem , vol.268 , pp. 26950-26955
    • Huang, Z.F.1    Wun, T.C.2    Broze Jr., G.J.3
  • 16
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison JF, Walsh CT. The behavior and significance of slow-binding enzyme inhibitors. Adv Enzymol Relat Areas Mol Biol 1988; 61: 201-301.
    • (1988) Adv Enzymol Relat Areas Mol Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 17
    • 0030033356 scopus 로고    scopus 로고
    • Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue-factor-pathway inhibitor
    • Petersen LC, Bjorn SE, Olsen OH, et al. Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue-factor-pathway inhibitor. Eur J Biochem 1996; 235: 310-316.
    • (1996) Eur J Biochem , vol.235 , pp. 310-316
    • Petersen, L.C.1    Bjorn, S.E.2    Olsen, O.H.3
  • 18
    • 0026594204 scopus 로고
    • The effect of leukocyte elastase on tissue factor pathway inhibitor
    • Higuchi DA, Wun TC, Likert KM, et al. The effect of leukocyte elastase on tissue factor pathway inhibitor. Blood 1992; 79: 1712-1719.
    • (1992) Blood , vol.79 , pp. 1712-1719
    • Higuchi, D.A.1    Wun, T.C.2    Likert, K.M.3
  • 19
    • 9444273450 scopus 로고    scopus 로고
    • Inhibition of thrombin generation by protein S at low procoagulant stimuli: Implications for maintenance of the hemostatic balance
    • Sere KM, Rosing J, Hackeng TM. Inhibition of thrombin generation by protein S at low procoagulant stimuli: implications for maintenance of the hemostatic balance. Blood 2004; 104: 3624-3630.
    • (2004) Blood , vol.104 , pp. 3624-3630
    • Sere, K.M.1    Rosing, J.2    Hackeng, T.M.3
  • 20
    • 0028344289 scopus 로고
    • Refold and characterization of recombinant tissue factor pathway inhibitor expressed in Escherichia coli
    • Diaz-Collier JA, Palmier MO, Kretzmer KK, et al. Refold and characterization of recombinant tissue factor pathway inhibitor expressed in Escherichia coli. Thromb Haemost 1994; 71: 339-346.
    • (1994) Thromb Haemost , vol.71 , pp. 339-346
    • Diaz-Collier, J.A.1    Palmier, M.O.2    Kretzmer, K.K.3
  • 21
    • 0027424985 scopus 로고
    • Characterization of human tissue factor pathway inhibitor variants expressed in Saccharomyces cerevisiae
    • Petersen JG, Meyn G, Rasmussen JS, et al. Characterization of human tissue factor pathway inhibitor variants expressed in Saccharomyces cerevisiae. J Biol Chem 1993; 268: 13344-13351.
    • (1993) J Biol Chem , vol.268 , pp. 13344-13351
    • Petersen, J.G.1    Meyn, G.2    Rasmussen, J.S.3
  • 22
    • 0015610685 scopus 로고
    • A method for the simultaneous isolation of factor X and prothrombin from bovine plasma
    • Esnouf MP, Lloyd PH, Jesty J. A method for the simultaneous isolation of factor X and prothrombin from bovine plasma. Biochem J 1973; 131: 781-789.
    • (1973) Biochem J , vol.131 , pp. 781-789
    • Esnouf, M.P.1    Lloyd, P.H.2    Jesty, J.3
  • 23
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnolzer M, Alewood P, Jones A, et al. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. Int J Pept Protein Res 1992; 40: 180-193.
    • (1992) Int J Pept Protein Res , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3
  • 24
    • 0033621158 scopus 로고    scopus 로고
    • Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
    • Hackeng TM, Griffin JH, Dawson PE. Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc Natl Acad Sci USA 1999; 96: 10068-10073.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10068-10073
    • Hackeng, T.M.1    Griffin, J.H.2    Dawson, P.E.3
  • 26
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson PE, Muir TW, Clark-Lewis I, et al. Synthesis of proteins by native chemical ligation. Science 1994; 266: 776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3
  • 27
    • 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: 1344-1351.
    • (2010) Blood , vol.116 , pp. 1344-1351
    • Ndonwi, M.1    Tuley, E.A.2    Broze Jr., G.J.3
  • 28
    • 0029148567 scopus 로고
    • Kinetics of the inhibition of tissue factor-factor VIIa by tissue factor pathway inhibitor
    • Lindhout T, Franssen J, Willems G. Kinetics of the inhibition of tissue factor-factor VIIa by tissue factor pathway inhibitor. Thromb Haemost 1995; 74: 910-915.
    • (1995) Thromb Haemost , vol.74 , pp. 910-915
    • Lindhout, T.1    Franssen, J.2    Willems, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.