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Volumn 1, Issue 1, 2003, Pages 124-131

Fibrinogen γ' chain binds thrombin exosite II

Author keywords

Fibrinogen; Heparin; Hirudin; Sulfation; Thrombin

Indexed keywords

DNA; FIBRINOGEN; FIBRINOPEPTIDES GAMMA; HEPARIN; HIRUDIN DERIVATIVE; ISOPROTEIN; RECOMBINANT PROTEIN; THROMBIN; TYROSINE;

EID: 0037923219     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1046/j.1538-7836.2003.00027.x     Document Type: Article
Times cited : (79)

References (51)
  • 1
    • 0034964371 scopus 로고    scopus 로고
    • Fibrinogen: evolution of the structure-function concept: Keynote address at the Fibrinogen 2000 Congress
    • Blombäck B. Fibrinogen: evolution of the structure-function concept: Keynote address at the Fibrinogen 2000 Congress. Ann NY Acad Sci 2001; 936: 1-10.
    • (2001) Ann NY Acad Sci , vol.936 , pp. 1-10
    • Blombäck, B.1
  • 2
    • 0001319829 scopus 로고
    • Note on the adsorption of thrombin on fibrin
    • Seegers WH, Nieft M, Loomis EC. Note on the adsorption of thrombin on fibrin. Science 1945; 101: 520-1.
    • (1945) Science , vol.101 , pp. 520-521
    • Seegers, W.H.1    Nieft, M.2    Loomis, E.C.3
  • 3
    • 0029830698 scopus 로고    scopus 로고
    • Identification and characterization of the thrombin binding sites on fibrin
    • Meh DA, Siebenlist KR, Mosesson MW. Identification and characterization of the thrombin binding sites on fibrin. J Biol Chem 1996; 271: 23121-5.
    • (1996) J Biol Chem , vol.271 , pp. 23121-23125
    • Meh, D.A.1    Siebenlist, K.R.2    Mosesson, M.W.3
  • 4
    • 0023918947 scopus 로고
    • Localization of the binding site on fibrin for the secondary binding site of thrombin
    • Vali Z, Scheraga HA. Localization of the binding site on fibrin for the secondary binding site of thrombin. Biochemistry 1988; 27: 1956-63.
    • (1988) Biochemistry , vol.27 , pp. 1956-1963
    • Vali, Z.1    Scheraga, H.A.2
  • 5
    • 0017728037 scopus 로고
    • Mechanism of action of thrombin on fibrinogen. The reaction of thrombin with fibrinogen-like peptides containing 11, 14, and 16 residues
    • van Nispen JW, Hageman TC, Scheraga HA. Mechanism of action of thrombin on fibrinogen. The reaction of thrombin with fibrinogen-like peptides containing 11, 14, and 16 residues. Arch Biochem Biophys 1977; 182: 227-43.
    • (1977) Arch Biochem Biophys , vol.182 , pp. 227-243
    • van Nispen, J.W.1    Hageman, T.C.2    Scheraga, H.A.3
  • 7
    • 0021184750 scopus 로고
    • γ and γ' chains of human fibrinogen are produced by alternative mRNA processing
    • Chung DW, Davie EW. γ and γ' chains of human fibrinogen are produced by alternative mRNA processing. Biochemistry 1984; 23: 4232-6.
    • (1984) Biochemistry , vol.23 , pp. 4232-4236
    • Chung, D.W.1    Davie, E.W.2
  • 8
    • 0021744551 scopus 로고
    • Structure of the human γ-fibrinogen gene. Alternate mRNA splicing near the 3′ end of the gene produces γA and γB forms of γ-fibrinogen
    • Fornace AJII, Cummings D, Comeau CM, Kant JA, Crabtree GR. Structure of the human γ-fibrinogen gene. Alternate mRNA splicing near the 3′ end of the gene produces γA and γB forms of γ-fibrinogen. J Biol Chem 1984; 259: 12826-30.
    • (1984) J Biol Chem , vol.259 , pp. 12826-12830
    • Fornace, A.J.I.I.1    Cummings, D.2    Comeau, C.M.3    Kant, J.A.4    Crabtree, G.R.5
  • 9
    • 0001452932 scopus 로고
    • Biochemical and chromatographic studies of certain activities associated with human fibrinogen preparations
    • MosessonMW, Finlayson JS. Biochemical and chromatographic studies of certain activities associated with human fibrinogen preparations. J Clin Invest 1963; 42: 747-55.
    • (1963) J Clin Invest , vol.42 , pp. 747-755
    • Mosesson, M.W.1    Finlayson, J.S.2
  • 11
    • 0024449761 scopus 로고
    • The C-terminal sequences of the γ 57.5 chain of human fibrinogen constitute a plasmin sensitive epitope that is exposed in crosslinked fibrin
    • Haidaris PJ, Peerschke EIB, Marder VJ, Francis CW. The C-terminal sequences of the g 57.5 chain of human fibrinogen constitute a plasmin sensitive epitope that is exposed in crosslinked fibrin. Blood 1989; 74: 2437-44.
    • (1989) Blood , vol.74 , pp. 2437-2444
    • Haidaris, P.J.1    Peerschke, E.I.B.2    Marder, V.J.3    Francis, C.W.4
  • 12
    • 0019332653 scopus 로고
    • Demonstration of a large molecular weight variant of the γ chain of normal human plasma fibrinogen
    • Francis CW, Marder VJ, Martin SE. Demonstration of a large molecular weight variant of the γ chain of normal human plasma fibrinogen. J Biol Chem 1980; 255: 5599-604.
    • (1980) J Biol Chem , vol.255 , pp. 5599-5604
    • Francis, C.W.1    Marder, V.J.2    Martin, S.E.3
  • 13
    • 1042289587 scopus 로고
    • Human plasma fibrinogen heterogeneity: Evidence for an extended carboxyl-terminal sequence in a normal γ chain variant (γ')
    • Wolfenstein-Todel C, Mosesson MW. Human plasma fibrinogen heterogeneity: Evidence for an extended carboxyl-terminal sequence in a normal γ chain variant (γ'). Proc Natl Acad Sci USA 1980; 77: 5069-73.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5069-5073
    • Wolfenstein-Todel, C.1    Mosesson, M.W.2
  • 14
    • 0024670167 scopus 로고
    • Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III. Implications for heparin therapy
    • Hogg PJ, Jackson CM. Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III. Implications for heparin therapy. Proc Natl Acad Sci USA 1989; 86: 3619-23.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3619-3623
    • Hogg, P.J.1    Jackson, C.M.2
  • 15
    • 0025146426 scopus 로고
    • Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors
    • Weitz JI, Hudoba M, Massel D, Maraganore J, Hirsh J. Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors. J Clin Invest 1990; 86: 385-91.
    • (1990) J Clin Invest , vol.86 , pp. 385-391
    • Weitz, J.I.1    Hudoba, M.2    Massel, D.3    Maraganore, J.4    Hirsh, J.5
  • 16
    • 0015821564 scopus 로고
    • The purification and mechanism of action of human antithrombin-heparin cofactor
    • Rosenberg RD, Damus PS. The purification and mechanism of action of human antithrombin-heparin cofactor. J Biol Chem 1973; 248: 6490-505.
    • (1973) J Biol Chem , vol.248 , pp. 6490-6505
    • Rosenberg, R.D.1    Damus, P.S.2
  • 18
    • 0028007619 scopus 로고
    • The influence of fibrinogen and fibrin on thrombin generation - evidence for feedback activation of the clotting system by clot bound thrombin
    • Kumar R, Beguin S, Hemker HC. The influence of fibrinogen and fibrin on thrombin generation - evidence for feedback activation of the clotting system by clot bound thrombin. Thromb Haemost 1994; 72: 713-21.
    • (1994) Thromb Haemost , vol.72 , pp. 713-721
    • Kumar, R.1    Beguin, S.2    Hemker, H.C.3
  • 19
    • 0030611710 scopus 로고    scopus 로고
    • Resistance of γA/γ' fibrin clots to fibrinolysis
    • Falls LA, Farrell DH. Resistance of γA/γ' fibrin clots to fibrinolysis. J Biol Chem 1997; 272: 14251-6.
    • (1997) J Biol Chem , vol.272 , pp. 14251-14256
    • Falls, L.A.1    Farrell, D.H.2
  • 20
    • 0034644660 scopus 로고    scopus 로고
    • The role of γA/γ' fibrinogen in plasma factor XIII activation
    • Moaddel M, Falls LA, Farrell DH. The role of γA/γ' fibrinogen in plasma factor XIII activation. J Biol Chem 2000; 275: 32135-40.
    • (2000) J Biol Chem , vol.275 , pp. 32135-32140
    • Moaddel, M.1    Falls, L.A.2    Farrell, D.H.3
  • 21
    • 0036301930 scopus 로고    scopus 로고
    • Association of γA/γ' fibrinogen levels and coronary artery disease
    • Lovely RS, Falls LA, Al-Mondhiry HA, et al. Association of γA/γ' fibrinogen levels and coronary artery disease. Thromb Haemost 2002; 88: 26-31.
    • (2002) Thromb Haemost , vol.88 , pp. 26-31
    • Lovely, R.S.1    Falls, L.A.2    Al-Mondhiry, H.A.3
  • 22
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • BodeW, Turk D, Karshikov A. The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1992; 1: 426-71.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 23
    • 0023770729 scopus 로고
    • Anion-binding exosite of human α-thrombin and fibrin (ogen) recognition
    • Fenton JWII, Olson TA, Zabinski MP, Wilner GD. Anion-binding exosite of human α-thrombin and fibrin (ogen) recognition. Biochemistry 1988; 27: 7106-12.
    • (1988) Biochemistry , vol.27 , pp. 7106-7112
    • Fenton II, J.W.1    Olson, T.A.2    Zabinski, M.P.3    Wilner, G.D.4
  • 24
    • 0032553446 scopus 로고    scopus 로고
    • Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes
    • Myles T, Church FC, Whinna HC, Monard D, Stone SR. Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes. J Biol Chem 1998; 273: 31203-8.
    • (1998) J Biol Chem , vol.273 , pp. 31203-31208
    • Myles, T.1    Church, F.C.2    Whinna, H.C.3    Monard, D.4    Stone, S.R.5
  • 27
    • 0027409404 scopus 로고
    • A player of many parts: the spotlight falls on thrombin's structure
    • Stubbs MT, Bode W. A player of many parts: the spotlight falls on thrombin's structure. Thromb Res 1993; 69: 1-58.
    • (1993) Thromb Res , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 28
    • 0027410184 scopus 로고
    • Active site and exosite binding of α-thrombin
    • Tulinsky A, Qiu X. Active site and exosite binding of α-thrombin. Blood Coagul Fibrinolysis 1993; 4: 305-12.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 305-312
    • Tulinsky, A.1    Qiu, X.2
  • 30
    • 0034635224 scopus 로고    scopus 로고
    • The Asp(272)-Glu(282) region of platelet glycoprotein Ibα interacts with the heparinbinding site of α-thrombin and protects the enzyme from the heparincatalyzed inhibition by antithrombin III
    • De Cristofaro R, De Candia E, Rutella S, Weitz JI. The Asp(272)-Glu(282) region of platelet glycoprotein Ibα interacts with the heparinbinding site of α-thrombin and protects the enzyme from the heparincatalyzed inhibition by antithrombin III. J Biol Chem 2000; 275: 3887-95.
    • (2000) J Biol Chem , vol.275 , pp. 3887-3895
    • De Cristofaro, R.1    De Candia, E.2    Rutella, S.3    Weitz, J.I.4
  • 31
    • 0035794133 scopus 로고    scopus 로고
    • Platelet glycoprotein Ibα binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin
    • Li CQ, Vindigni A, Sadler JE, Wardell MR. Platelet glycoprotein Ibα binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin. J Biol Chem 2001; 276: 6161-8.
    • (2001) J Biol Chem , vol.276 , pp. 6161-6168
    • Li, C.Q.1    Vindigni, A.2    Sadler, J.E.3    Wardell, M.R.4
  • 33
    • 0022521744 scopus 로고
    • Kinetics of the inhibition of thrombin by hirudin
    • Stone SR, Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry 1986; 25: 4622-8.
    • (1986) Biochemistry , vol.25 , pp. 4622-4628
    • Stone, S.R.1    Hofsteenge, J.2
  • 34
    • 0022998259 scopus 로고
    • Identification of two sites of sulfation of human heparin cofactor II
    • Hortin GL, Tollefsen DM, Strauss AW. Identification of two sites of sulfation of human heparin cofactor II. J BiolChem1986; 261: 15827-30.
    • (1986) J BiolChem , vol.261 , pp. 15827-15830
    • Hortin, G.L.1    Tollefsen, D.M.2    Strauss, A.W.3
  • 35
    • 0028940892 scopus 로고
    • Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in vonWillebrand factor and α-thrombin binding
    • Marchese P, Murata M, Mazzucato M, Pradella P, De Marco L, Ware J, Ruggeri ZM. Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in vonWillebrand factor and α-thrombin binding. J Biol Chem 1995; 270: 9571-8.
    • (1995) J Biol Chem , vol.270 , pp. 9571-9578
    • Marchese, P.1    Murata, M.2    Mazzucato, M.3    Pradella, P.4    De Marco, L.5    Ware, J.6    Ruggeri, Z.M.7
  • 36
    • 0028231924 scopus 로고
    • Posttranslational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity
    • Pittman DD, Tomkinson KN, Michnick D, Selighsohn U, Kaufman RJ. Posttranslational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity. Biochemistry 1994; 33: 6952-9.
    • (1994) Biochemistry , vol.33 , pp. 6952-6959
    • Pittman, D.D.1    Tomkinson, K.N.2    Michnick, D.3    Selighsohn, U.4    Kaufman, R.J.5
  • 37
    • 0028058606 scopus 로고
    • Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage
    • Michnick DA, Pittman DD, Wise RJ, Kaufman RJ. Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage. J Biol Chem 1994; 269: 20095-102.
    • (1994) J Biol Chem , vol.269 , pp. 20095-20102
    • Michnick, D.A.1    Pittman, D.D.2    Wise, R.J.3    Kaufman, R.J.4
  • 38
    • 0000603919 scopus 로고
    • On the occurrence and significance of tyrosine sulfation in fibrinogen
    • Henschen A. On the occurrence and significance of tyrosine sulfation in fibrinogen. Blood Coag Fibrinolysis 1993; 4: 822.
    • (1993) Blood Coag Fibrinolysis , vol.4 , pp. 822
    • Henschen, A.1
  • 40
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 1985; 82: 488-92.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0020426116 scopus 로고
    • Organization of the rat γ-fibrinogen gene. Alternative mRNA splice patterns produce the γA and γB(γ') chains of fibrinogen
    • Crabtree GR, Kant JA. Organization of the rat γ-fibrinogen gene. Alternative mRNA splice patterns produce the γA and γB(γ') chains of fibrinogen. Cell 1982; 31: 159-66.
    • (1982) Cell , vol.31 , pp. 159-166
    • Crabtree, G.R.1    Kant, J.A.2
  • 44
    • 0024296783 scopus 로고
    • Tyrosine O-sulfation of the fibrinogen gB chain in primary cultures of rat hepatocytes
    • Hirose S, Oda K, Ikehara Y. Tyrosine O-sulfation of the fibrinogen gB chain in primary cultures of rat hepatocytes. J Biol Chem 1988; 263: 7426-30.
    • (1988) J Biol Chem , vol.263 , pp. 7426-7430
    • Hirose, S.1    Oda, K.2    Ikehara, Y.3
  • 45
    • 0026713781 scopus 로고
    • Recognition of substrates by tyrosylprotein sulfotransferase. Determination of affinity by acidic amino acids near the target sites
    • Lin WH, Larsen K, Hortin GL, Roth JA. Recognition of substrates by tyrosylprotein sulfotransferase. Determination of affinity by acidic amino acids near the target sites. J Biol Chem 1992; 267: 2876-9.
    • (1992) J Biol Chem , vol.267 , pp. 2876-2879
    • Lin, W.H.1    Larsen, K.2    Hortin, G.L.3    Roth, J.A.4
  • 47
    • 0030830185 scopus 로고    scopus 로고
    • Evidence for allosteric linkage between exosites 1 and 2 of thrombin
    • Fredenburgh JC, Stafford AR, Weitz JI. Evidence for allosteric linkage between exosites 1 and 2 of thrombin. J Biol Chem 1997; 272: 25493-9.
    • (1997) J Biol Chem , vol.272 , pp. 25493-25499
    • Fredenburgh, J.C.1    Stafford, A.R.2    Weitz, J.I.3
  • 49
    • 0023105044 scopus 로고
    • Inhibited thrombins: interactions with fibrinogen and fibrin
    • Kaminski M, McDonagh J. Inhibited thrombins: interactions with fibrinogen and fibrin. Biochem J 1987; 242: 881-7.
    • (1987) Biochem J , vol.242 , pp. 881-887
    • Kaminski, M.1    McDonagh, J.2
  • 50
    • 0029995667 scopus 로고    scopus 로고
    • Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen
    • Hogg PJ, Jackson CM, Labanowski JK, Bock PE. Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen. J Biol Chem 1996; 271: 26088-95.
    • (1996) J Biol Chem , vol.271 , pp. 26088-26095
    • Hogg, P.J.1    Jackson, C.M.2    Labanowski, J.K.3    Bock, P.E.4
  • 51
    • 0033525536 scopus 로고    scopus 로고
    • Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II
    • Becker DL, Fredenburgh JC, Stafford AR, Weitz JI. Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II. J Biol Chem 1999; 274: 6226-33.
    • (1999) J Biol Chem , vol.274 , pp. 6226-6233
    • Becker, D.L.1    Fredenburgh, J.C.2    Stafford, A.R.3    Weitz, J.I.4


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