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Volumn 101, Issue 12, 2003, Pages 4802-4807

Exosite-dependent regulation of factor VIIIa by activated protein C

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; ARGININE; BLOOD CLOTTING FACTOR 8A;

EID: 0038454577     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-01-0126     Document Type: Article
Times cited : (25)

References (47)
  • 1
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon CT. Molecular events that control the protein C anticoagulant pathway. Thromb Haemost. 1993;70:1-5.
    • (1993) Thromb Haemost , vol.70 , pp. 1-5
    • Esmon, C.T.1
  • 2
    • 0026704809 scopus 로고
    • Regulation of blood coagulation by the protein C system
    • Walker FJ, Fay PJ. Regulation of blood coagulation by the protein C system. FASEB J. 1992;6:2561-2567.
    • (1992) FASEB J , vol.6 , pp. 2561-2567
    • Walker, F.J.1    Fay, P.J.2
  • 3
    • 0028110027 scopus 로고
    • The mechanism of inactivation of human factor V and human factor Va by activated protein C
    • Kalafatis M, Rand MD, Mann KG. The mechanism of inactivation of human factor V and human factor Va by activated protein C. J Biol Chem. 1994;269:31869-31880.
    • (1994) J Biol Chem , vol.269 , pp. 31869-31880
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 4
    • 0021210403 scopus 로고
    • Structure and function of protein C
    • Stenflo J. Structure and function of protein C. Semin Thromb Hemost. 1984;10:109-121.
    • (1984) Semin Thromb Hemost , vol.10 , pp. 109-121
    • Stenflo, J.1
  • 5
    • 0026063331 scopus 로고
    • Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors
    • Stenflo J. Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. Blood. 1991;78:1637-1651.
    • (1991) Blood , vol.78 , pp. 1637-1651
    • Stenflo, J.1
  • 6
    • 0030468098 scopus 로고    scopus 로고
    • The 2.8 A crystal structure of Gla-domainless activated protein C
    • Mather T, Oganessyan V, Hof P, et al. The 2.8 A crystal structure of Gla-domainless activated protein C. EMBO J. 1996;15:6822-6831.
    • (1996) EMBO J , vol.15 , pp. 6822-6831
    • Mather, T.1    Oganessyan, V.2    Hof, P.3
  • 7
    • 0024431034 scopus 로고
    • The refined 1.9 A crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg chlorometheylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9 A crystal structure of human α-thrombin: interaction with D-Phe-Pro-Arg chlorometheylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989;8:3467-3475.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 8
    • 0037076527 scopus 로고    scopus 로고
    • Contribution of basic residues of the 70-80-loop to heparin binding and anticoagulant function of activated protein C
    • Yang L, Manithody C, Rezaie AR. Contribution of basic residues of the 70-80-loop to heparin binding and anticoagulant function of activated protein C. Biochemistry. 2002;41:6149-6157.
    • (2002) Biochemistry , vol.41 , pp. 6149-6157
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 9
    • 0035933906 scopus 로고    scopus 로고
    • Secondary substrate-binding exosite in the serine protease domain of activated protein C important for cleavage at Arg-506 but not at Arg-306 in factor Va
    • Friedrich U, Nicolaes GAF, Villoutreix BO, Dahlbäck B. Secondary substrate-binding exosite in the serine protease domain of activated protein C important for cleavage at Arg-506 but not at Arg-306 in factor Va. J Biol Chem. 2001;276:23105-23108.
    • (2001) J Biol Chem , vol.276 , pp. 23105-23108
    • Friedrich, U.1    Nicolaes, G.A.F.2    Villoutreix, B.O.3    Dahlbäck, B.4
  • 10
    • 0037047277 scopus 로고    scopus 로고
    • Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C
    • Gale AJ, Tsavaler A, Griffin JH. Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C. J Biol Chem. 2002;277:28836-28840.
    • (2002) J Biol Chem , vol.277 , pp. 28836-28840
    • Gale, A.J.1    Tsavaler, A.2    Griffin, J.H.3
  • 11
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • Mann KG, Jenny RJ, Krishnaswamy S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Ann Rev Biochem. 1988;57:915-956.
    • (1988) Ann Rev Biochem , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 12
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie B, Furie BC. The molecular basis of blood coagulation. Cell. 1988;53:505-518.
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 13
    • 0018860405 scopus 로고
    • Preparation and properties of bovine factor VIII (antihemophilic factor)
    • Vehar GA, Davie EW. Preparation and properties of bovine factor VIII (antihemophilic factor). Biochemistry. 1980;19:401-410.
    • (1980) Biochemistry , vol.19 , pp. 401-410
    • Vehar, G.A.1    Davie, E.W.2
  • 15
    • 0021677942 scopus 로고
    • Structure of human factor VIII
    • Vehar GA, Keyt B, Eaton D, et al. Structure of human factor VIII. Nature. 1984;312:337-342.
    • (1984) Nature , vol.312 , pp. 337-342
    • Vehar, G.A.1    Keyt, B.2    Eaton, D.3
  • 16
    • 0023918199 scopus 로고
    • Blood coagulation factors V and VIII: Structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders
    • Kane WH, Davie EW. Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood. 1988;71:539-555.
    • (1988) Blood , vol.71 , pp. 539-555
    • Kane, W.H.1    Davie, E.W.2
  • 17
    • 0032402122 scopus 로고    scopus 로고
    • The life cycle of coagulation factor VIII in view of its structure and function
    • Lenting PJ, van Mourik JA, Mertens K. The life cycle of coagulation factor VIII in view of its structure and function. Blood. 1998;92:3983-3996.
    • (1998) Blood , vol.92 , pp. 3983-3996
    • Lenting, P.J.1    Van Mourik, J.A.2    Mertens, K.3
  • 18
    • 0018786088 scopus 로고
    • The subunit structure of thrombin-activated factor V: Isolation of activated factor V, separation of subunits and reconstitution of biological activity
    • Esmon CT. The subunit structure of thrombin-activated factor V: isolation of activated factor V, separation of subunits and reconstitution of biological activity, J Biol Chem. 1979;254:964-973.
    • (1979) J Biol Chem , vol.254 , pp. 964-973
    • Esmon, C.T.1
  • 19
    • 0021046120 scopus 로고
    • The factor Xa-catalyzed activation of factor V
    • Foster WB, Nesheim ME, Mann KG. The factor Xa-catalyzed activation of factor V. J Biol Chem. 1983;258:13970-13977.
    • (1983) J Biol Chem , vol.258 , pp. 13970-13977
    • Foster, W.B.1    Nesheim, M.E.2    Mann, K.G.3
  • 21
    • 0022454539 scopus 로고
    • Proteolytic processing of human factor VIII: Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
    • Eaton D, Rodriguez H, Vehar GA. Proteolytic processing of human factor VIII: correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity. Biochemistry. 1986;25:505-512.
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 22
    • 0026708655 scopus 로고
    • Characterization of the interaction between the A2 subunit and A1/A3-C1-C2 dimer in human factor VIIIa
    • Fay PJ, Smudzin TM. Characterization of the interaction between the A2 subunit and A1/A3-C1-C2 dimer in human factor VIIIa. J Biol Chem. 1992;267:13246-13250.
    • (1992) J Biol Chem , vol.267 , pp. 13246-13250
    • Fay, P.J.1    Smudzin, T.M.2
  • 23
    • 0036124011 scopus 로고    scopus 로고
    • Factor V and thrombotic diseases: Description of a Janus-faced protein
    • Nicolaes GAF, Dahlbäck B, Factor V and thrombotic diseases: description of a Janus-faced protein. Arterioscler Thromb Vasc Biol. 2002;22:530-538.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 530-538
    • Nicolaes, G.A.F.1    Dahlbäck, B.2
  • 27
    • 0034161511 scopus 로고    scopus 로고
    • Regulation of factor Villa by human activated protein C and protein S: Inactivation of cofactor in the intrinsic factor Xase
    • O'Brien LM, Mastri M, Fay PJ. Regulation of factor Villa by human activated protein C and protein S: inactivation of cofactor in the intrinsic factor Xase. Blood. 2000;95:1714-1720.
    • (2000) Blood , vol.95 , pp. 1714-1720
    • O'Brien, L.M.1    Mastri, M.2    Fay, P.J.3
  • 28
    • 0035844272 scopus 로고    scopus 로고
    • Vitronectin functions as a cofactor for rapid inhibition of activated protein C by plasminogen activator inhibitor-1: Implications for the mechanism of profibrinolytic action of activated protein C
    • Rezaie AR. Vitronectin functions as a cofactor for rapid inhibition of activated protein C by plasminogen activator inhibitor-1: Implications for the mechanism of profibrinolytic action of activated protein C. J Biol Chem. 2001;276:15567-15570.
    • (2001) J Biol Chem , vol.276 , pp. 15567-15570
    • Rezaie, A.R.1
  • 29
    • 0028122250 scopus 로고
    • Isolation and characterization of thrombin-activated human factor VIII
    • Curtis JE, Helgerson SL, Parker ET, Lollar P. Isolation and characterization of thrombin-activated human factor VIII. J Biol Chem. 1994;269:6246-6251.
    • (1994) J Biol Chem , vol.269 , pp. 6246-6251
    • Curtis, J.E.1    Helgerson, S.L.2    Parker, E.T.3    Lollar, P.4
  • 30
    • 0031027575 scopus 로고    scopus 로고
    • Localization of a factor X interactive site in the A1 subunit of factor VIIIa
    • Lapan KA, Fay PJ. Localization of a factor X interactive site in the A1 subunit of factor VIIIa. J Biol Chem. 1997;272:2082-2088.
    • (1997) J Biol Chem , vol.272 , pp. 2082-2088
    • Lapan, K.A.1    Fay, P.J.2
  • 31
    • 0037023727 scopus 로고    scopus 로고
    • Cofactor activities of factor VIIIa and A2 subunit following cleavage of A1 subunit at Arg336
    • Koszelak ME, Schmidt K, Freas J, Mastri M, Fay PJ. Cofactor activities of factor VIIIa and A2 subunit following cleavage of A1 subunit at Arg336. J Biol Chem. 2002;277:11664-11669.
    • (2002) J Biol Chem , vol.277 , pp. 11664-11669
    • Koszelak, M.E.1    Schmidt, K.2    Freas, J.3    Mastri, M.4    Fay, P.J.5
  • 32
    • 0037188360 scopus 로고    scopus 로고
    • Role of basic residues of the autolysis loop in the catalytic function of factor Xa
    • Manithody C, Yang L, Rezaie AR. Role of basic residues of the autolysis loop in the catalytic function of factor Xa. Biochemistry. 2002;41:6780-6788.
    • (2002) Biochemistry , vol.41 , pp. 6780-6788
    • Manithody, C.1    Yang, L.2    Rezaie, A.R.3
  • 33
    • 0030029895 scopus 로고    scopus 로고
    • Tryptophan60-D in the B-insertion loop of thrombin modulates the thrombin-antithrombin reaction
    • Rezaie AR. Tryptophan60-D in the B-insertion loop of thrombin modulates the thrombin-antithrombin reaction. Biochemistry. 1996;35:1918-1924.
    • (1996) Biochemistry , vol.35 , pp. 1918-1924
    • Rezaie, A.R.1
  • 34
    • 0027972573 scopus 로고
    • Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C
    • Smirnov MD, Esmon CT. Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C. J Biol Chem. 1994;269:816-819.
    • (1994) J Biol Chem , vol.269 , pp. 816-819
    • Smirnov, M.D.1    Esmon, C.T.2
  • 36
    • 0028290275 scopus 로고
    • Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa
    • Shen L, Dahlbäck B. Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa. J Biol Chem. 1994;269:18735-18738.
    • (1994) J Biol Chem , vol.269 , pp. 18735-18738
    • Shen, L.1    Dahlbäck, B.2
  • 37
    • 0030843304 scopus 로고    scopus 로고
    • Activated protein C cleavage of factor Va leads to dissociation of the A2 domain
    • Mann KG, Hockin MF, Begin KJ, Kalafatis M. Activated protein C cleavage of factor Va leads to dissociation of the A2 domain. J Biol Chem. 1997;272:20678-20683.
    • (1997) J Biol Chem , vol.272 , pp. 20678-20683
    • Mann, K.G.1    Hockin, M.F.2    Begin, K.J.3    Kalafatis, M.4
  • 38
    • 0025021593 scopus 로고
    • Identification of the binding site for activated protein C on the light chain of factors V and VIII
    • Walker FJ, Scandella D, Fay PJ. Identification of the binding site for activated protein C on the light chain of factors V and VIII. J Biol Chem. 1990;265:1484-1489,
    • (1990) J Biol Chem , vol.265 , pp. 1484-1489
    • Walker, F.J.1    Scandella, D.2    Fay, P.J.3
  • 39
    • 0037082464 scopus 로고    scopus 로고
    • 3-Dimensional structure of membrane-bound coagulation factor VIII: Modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography
    • Stoilova-McPhie S, Villoutreix BO, Mertens K, Kemball-Cook G, Holzenburg A. 3-dimensional structure of membrane-bound coagulation factor VIII: modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography. Blood. 2002;99:1215-1223.
    • (2002) Blood , vol.99 , pp. 1215-1223
    • Stoilova-McPhie, S.1    Villoutreix, B.O.2    Mertens, K.3    Kemball-Cook, G.4    Holzenburg, A.5
  • 40
    • 0037449806 scopus 로고    scopus 로고
    • Altered interaction between the A1 and A2 subunits of factor Villa following cleavage of A1 subunit by factor Xa
    • Nogami K, Wakabayashi H, Schmidt K, Fay PJ. Altered interaction between the A1 and A2 subunits of factor Villa following cleavage of A1 subunit by factor Xa. J Biol Chem. 2003;278:1634-1641.
    • (2003) J Biol Chem , vol.278 , pp. 1634-1641
    • Nogami, K.1    Wakabayashi, H.2    Schmidt, K.3    Fay, P.J.4
  • 41
    • 0035844226 scopus 로고    scopus 로고
    • Factor IXa:factor VIIIa interaction: Helix 330-338 of factor IXa interacts with residues 558-565 and spatially adjacent region of the A2 subunit of factor VIIIa
    • Bajaj SP, Schmidt AE, Mathur A, Padmanabhan K, Mastri M, Fay PJ. Factor IXa:factor VIIIa interaction: helix 330-338 of factor IXa interacts with residues 558-565 and spatially adjacent region of the A2 subunit of factor VIIIa. J Biol Chem. 2001;276:16302-16309.
    • (2001) J Biol Chem , vol.276 , pp. 16302-16309
    • Bajaj, S.P.1    Schmidt, A.E.2    Mathur, A.3    Padmanabhan, K.4    Mastri, M.5    Fay, P.J.6
  • 42
    • 0027938728 scopus 로고
    • Factor Villa A2 subunit residues 558-565 represent a factor IXa interactive site
    • Fay PJ, Beattie T, Huggins CF, Regan LM. Factor Villa A2 subunit residues 558-565 represent a factor IXa interactive site. J Biol Chem. 1994;269:20522-20527.
    • (1994) J Biol Chem , vol.269 , pp. 20522-20527
    • Fay, P.J.1    Beattie, T.2    Huggins, C.F.3    Regan, L.M.4
  • 43
    • 0026630953 scopus 로고
    • Direct detection of activated protein C in blood from human subjects
    • Gruber A, Griffin JH. Direct detection of activated protein C in blood from human subjects. Blood. 1992;79:2340-2348.
    • (1992) Blood , vol.79 , pp. 2340-2348
    • Gruber, A.1    Griffin, J.H.2
  • 44
    • 0028940777 scopus 로고
    • Human protein C and activated protein C: Components of the human anticoagulation system
    • Castellino FJ. Human protein C and activated protein C: components of the human anticoagulation system. Trends Cardiovasc Med. 1995;5:55-62.
    • (1995) Trends Cardiovasc Med , vol.5 , pp. 55-62
    • Castellino, F.J.1
  • 46
    • 0027220449 scopus 로고
    • Conversion of glutamic acid 192 to glutamine in activated protein C changes the substrate specificity and increases reactivity toward macromolecular inhibitors
    • Rezaie AR, Esmon CT. Conversion of glutamic acid 192 to glutamine in activated protein C changes the substrate specificity and increases reactivity toward macromolecular inhibitors. J Biol Chem. 1993;268:19943-19948.
    • (1993) J Biol Chem , vol.268 , pp. 19943-19948
    • Rezaie, A.R.1    Esmon, C.T.2
  • 47
    • 0029935853 scopus 로고    scopus 로고
    • Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII
    • Esmon CT, Lollar P. Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII. J Biol Chem. 1996;271:13882-13887.
    • (1996) J Biol Chem , vol.271 , pp. 13882-13887
    • Esmon, C.T.1    Lollar, P.2


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