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Volumn 1854, Issue 10, 2015, Pages 1351-1356

Asymmetric processing of mutant factor X Arg386Cys reveals differences between intrinsic and extrinsic pathway activation

Author keywords

Activation determinant; Amino acid substitution; Coagulation serine proteases; Factor X; Factor X deficiency; Recombinant expression

Indexed keywords

ALANINE; ARGININE; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 8A; BLOOD CLOTTING FACTOR 9; BLOOD CLOTTING FACTOR 9A; CHYMOTRYPSIN; CYSTEINE; LIGAND; RECOMBINANT PROTEIN; THIOL; THROMBIN; BLOOD CLOTTING FACTOR 10A; METALLOPROTEINASE; PROTEIN BINDING; RUSSELLYSIN;

EID: 84937596938     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2015.05.012     Document Type: Article
Times cited : (8)

References (40)
  • 1
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • S. Krishnaswamy Exosite-driven substrate specificity and function in coagulation J. Thromb. Haemost. 3 2005 54 67
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 54-67
    • Krishnaswamy, S.1
  • 2
    • 77956544191 scopus 로고    scopus 로고
    • Ligand binding shuttles thrombin along a continuum of zymogen- and proteinase-like states
    • P. Kamath, J.A. Huntington, and S. Krishnaswamy Ligand binding shuttles thrombin along a continuum of zymogen- and proteinase-like states J. Biol. Chem. 285 2010 28651 28658
    • (2010) J. Biol. Chem. , vol.285 , pp. 28651-28658
    • Kamath, P.1    Huntington, J.A.2    Krishnaswamy, S.3
  • 3
    • 84897537641 scopus 로고    scopus 로고
    • Natural inhibitors of thrombin
    • J.A. Huntington Natural inhibitors of thrombin Thromb. Haemost. 111 2014 583 589
    • (2014) Thromb. Haemost. , vol.111 , pp. 583-589
    • Huntington, J.A.1
  • 4
    • 36349012420 scopus 로고    scopus 로고
    • Intrinsic pathway of coagulation and arterial thrombosis
    • D. Gailani, and T. Renné Intrinsic pathway of coagulation and arterial thrombosis Arterioscler. Thromb. Vasc. Biol. 27 2007 2507 2513
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 2507-2513
    • Gailani, D.1    Renné, T.2
  • 9
    • 0036331972 scopus 로고    scopus 로고
    • Reduced activation of the Gla19Ala FX variant via the extrinsic coagulation pathway results in symptomatic CRMred FX deficiency
    • M. Pinotti, G. Marchetti, M. Baroni, F. Cinotti, M. Morfini, and F. Bernardi Reduced activation of the Gla19Ala FX variant via the extrinsic coagulation pathway results in symptomatic CRMred FX deficiency Thromb. Haemost. 88 2002 236 241
    • (2002) Thromb. Haemost. , vol.88 , pp. 236-241
    • Pinotti, M.1    Marchetti, G.2    Baroni, M.3    Cinotti, F.4    Morfini, M.5    Bernardi, F.6
  • 11
    • 0029661263 scopus 로고    scopus 로고
    • Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein
    • A.E. Rudolph, M.P. Mullane, R. Porche-Sorbet, S. Tsuda, and J.P. Miletich Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein J. Biol. Chem. 271 1996 28601 28606
    • (1996) J. Biol. Chem. , vol.271 , pp. 28601-28606
    • Rudolph, A.E.1    Mullane, M.P.2    Porche-Sorbet, R.3    Tsuda, S.4    Miletich, J.P.5
  • 13
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • D.L. Higgins, and K.G. Mann The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles J. Biol. Chem. 258 1983 6503 6508
    • (1983) J. Biol. Chem. , vol.258 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 14
    • 0037330004 scopus 로고    scopus 로고
    • Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM + FX deficiency
    • M. Pinotti, R.M. Camire, M. Baroni, A. Rajab, G. Marchetti, and F. Bernardi Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM + FX deficiency Thromb. Haemost. 89 2003 243 248
    • (2003) Thromb. Haemost. , vol.89 , pp. 243-248
    • Pinotti, M.1    Camire, R.M.2    Baroni, M.3    Rajab, A.4    Marchetti, G.5    Bernardi, F.6
  • 15
    • 49649122047 scopus 로고    scopus 로고
    • The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly
    • R. Toso, H. Zhu, and R.M. Camire The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly J. Biol. Chem. 283 2008 18627 18635
    • (2008) J. Biol. Chem. , vol.283 , pp. 18627-18635
    • Toso, R.1    Zhu, H.2    Camire, R.M.3
  • 16
    • 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
    • P.J. Larson, R.M. Camire, D. Wong, N.C. Fasano, D.M. Monroe, P.B. Tracy, and K.A. High 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 37 1998 5029 5038
    • (1998) Biochemistry , vol.37 , pp. 5029-5038
    • Larson, P.J.1    Camire, R.M.2    Wong, D.3    Fasano, N.C.4    Monroe, D.M.5    Tracy, P.B.6    High, K.A.7
  • 17
    • 0034700266 scopus 로고    scopus 로고
    • Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide
    • R.M. Camire, P.J. Larson, D.W. Stafford, and K.A. High Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide Biochemistry 39 2000 14322 14329
    • (2000) Biochemistry , vol.39 , pp. 14322-14329
    • Camire, R.M.1    Larson, P.J.2    Stafford, D.W.3    High, K.A.4
  • 22
    • 0017762527 scopus 로고
    • Activation of human factor X (Stuart factor) by a protease from Russell's viper venom
    • R.G. Di Scipio, M.A. Hermodson, and E.W. Davie Activation of human factor X (Stuart factor) by a protease from Russell's viper venom Biochemistry 16 1977 5253 5260
    • (1977) Biochemistry , vol.16 , pp. 5253-5260
    • Di Scipio, R.G.1    Hermodson, M.A.2    Davie, E.W.3
  • 24
    • 0023196008 scopus 로고
    • Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism
    • S. Krishnaswamy, W.R. Church, M.E. Nesheim, and K.G. Mann Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism J. Biol. Chem. 262 1987 3291 3299
    • (1987) J. Biol. Chem. , vol.262 , pp. 3291-3299
    • Krishnaswamy, S.1    Church, W.R.2    Nesheim, M.E.3    Mann, K.G.4
  • 25
  • 27
    • 79551628274 scopus 로고    scopus 로고
    • Prothrombin activation on the activated platelet surface optimizes expression of procoagulant activity
    • J.P. Wood, J.R. Silveira, N.M. Maille, L.M. Haynes, and P.B. Tracy Prothrombin activation on the activated platelet surface optimizes expression of procoagulant activity Blood 117 2011 1710 1718
    • (2011) Blood , vol.117 , pp. 1710-1718
    • Wood, J.P.1    Silveira, J.R.2    Maille, N.M.3    Haynes, L.M.4    Tracy, P.B.5
  • 30
    • 0026710630 scopus 로고
    • Molecular recognition sites on factor Xa which participate in the prothrombinase complex
    • A. Chattopadhyay, H.L. James, and D.S. Fair Molecular recognition sites on factor Xa which participate in the prothrombinase complex J. Biol. Chem. 267 1992 12323 12329
    • (1992) J. Biol. Chem. , vol.267 , pp. 12323-12329
    • Chattopadhyay, A.1    James, H.L.2    Fair, D.S.3
  • 31
  • 32
    • 0037088606 scopus 로고    scopus 로고
    • The contribution of factor Xa to exosite-dependent substrate recognition by prothrombinase
    • M. Wilkens, and S. Krishnaswamy The contribution of factor Xa to exosite-dependent substrate recognition by prothrombinase J. Biol. Chem. 277 2002 9366 9374
    • (2002) J. Biol. Chem. , vol.277 , pp. 9366-9374
    • Wilkens, M.1    Krishnaswamy, S.2
  • 33
    • 0034602993 scopus 로고    scopus 로고
    • Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding
    • A.R. Rezaie Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding J. Biol. Chem. 275 2000 3320 3327
    • (2000) J. Biol. Chem. , vol.275 , pp. 3320-3327
    • Rezaie, A.R.1
  • 34
    • 0035853273 scopus 로고    scopus 로고
    • Four loops of the catalytic domain of factor viia mediate the effect of the first EGF-like domain substitution on factor viia catalytic activity
    • J. Jin, L. Perera, D. Stafford, and L. Pedersen Four loops of the catalytic domain of factor viia mediate the effect of the first EGF-like domain substitution on factor viia catalytic activity J. Mol. Biol. 307 2001 1503 1517
    • (2001) J. Mol. Biol. , vol.307 , pp. 1503-1517
    • Jin, J.1    Perera, L.2    Stafford, D.3    Pedersen, L.4
  • 35
    • 84871416887 scopus 로고    scopus 로고
    • Contribution of the NH2-terminal EGF-domain of factor IXa to the specificity of intrinsic tenase
    • S.H. Qureshi, L. Yang, and A.R. Rezaie Contribution of the NH2-terminal EGF-domain of factor IXa to the specificity of intrinsic tenase Thromb. Haemost. 108 2012 1154 1164
    • (2012) Thromb. Haemost. , vol.108 , pp. 1154-1164
    • Qureshi, S.H.1    Yang, L.2    Rezaie, A.R.3
  • 36
    • 84856287741 scopus 로고    scopus 로고
    • Factor VIII light chain contains a binding site for factor X that contributes to the catalytic efficiency of factor Xase
    • M. Takeyama, H. Wakabayashi, and P.J. Fay Factor VIII light chain contains a binding site for factor X that contributes to the catalytic efficiency of factor Xase Biochemistry 51 2012 820 828
    • (2012) Biochemistry , vol.51 , pp. 820-828
    • Takeyama, M.1    Wakabayashi, H.2    Fay, P.J.3
  • 37
    • 1642493924 scopus 로고    scopus 로고
    • Zymogenic and enzymatic properties of the 70-80 loop mutants of factor X/Xa
    • L. Chen, C. Manithody, L.K. Yang, and A.R. Rezaie Zymogenic and enzymatic properties of the 70-80 loop mutants of factor X/Xa Protein Sci. 13 2004 431 442
    • (2004) Protein Sci. , vol.13 , pp. 431-442
    • Chen, L.1    Manithody, C.2    Yang, L.K.3    Rezaie, A.R.4
  • 38
    • 84878890649 scopus 로고    scopus 로고
    • Six novel missense mutations causing factor X deficiency and application of thrombin generation est
    • Q. Liang, Q. Chen, Q. Ding, F. Wu, X. Wang, X. Xi, and H. Wang Six novel missense mutations causing factor X deficiency and application of thrombin generation est Thromb. Res. 131 2013 554 559
    • (2013) Thromb. Res. , vol.131 , pp. 554-559
    • Liang, Q.1    Chen, Q.2    Ding, Q.3    Wu, F.4    Wang, X.5    Xi, X.6    Wang, H.7
  • 39
    • 84877064531 scopus 로고    scopus 로고
    • Fluorescent amino acids: modular building blocks for the assembly of new tools for chemical biology
    • A.T. Krueger, and B. Imperiali Fluorescent amino acids: modular building blocks for the assembly of new tools for chemical biology Chembiochem 14 2013 788 799
    • (2013) Chembiochem , vol.14 , pp. 788-799
    • Krueger, A.T.1    Imperiali, B.2
  • 40
    • 84906085068 scopus 로고    scopus 로고
    • New insights into the spatiotemporal localization of prothrombinase in vivo
    • L. Ivanciu, S. Krishnaswamy, and R.M. Camire New insights into the spatiotemporal localization of prothrombinase in vivo Blood 124 2014 1705 1714
    • (2014) Blood , vol.124 , pp. 1705-1714
    • Ivanciu, L.1    Krishnaswamy, S.2    Camire, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.