메뉴 건너뛰기




Volumn 40, Issue 8, 2007, Pages 1055-1064

The role of autolysis loop in determining the specificity of coagulation proteases

Author keywords

Activated protein C; Antithrombin; Factor Va; Factor Xa; Serpins

Indexed keywords

ACTIVATED PROTEIN C; ANTITHROMBIN; BLOOD CLOTTING FACTOR; BLOOD CLOTTING FACTOR 5A; MUTANT PROTEIN; PENTASACCHARIDE; PROTEINASE; SERINE PROTEINASE INHIBITOR; TRYPSIN;

EID: 34547733426     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X2006005000137     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0015853889 scopus 로고
    • Anticoagulant action of heparin
    • Damus PS, Hicks M, Rosenberg RD. Anticoagulant action of heparin. Nature 1973; 246: 355-357.
    • (1973) Nature , vol.246 , pp. 355-357
    • Damus, P.S.1    Hicks, M.2    Rosenberg, R.D.3
  • 2
    • 0028773279 scopus 로고
    • Biological implications of a 3 A structure of dimeric antithrombin
    • Carrell RW, Stein PE, Fermi G, Wardell MR. Biological implications of a 3 A structure of dimeric antithrombin. Structure 1994; 2: 257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 3
    • 0001410715 scopus 로고
    • Regulation of thrombin by antithrombin and heparin co-factor II
    • Berliner LJ Editor, New York: Plenum Press;
    • Olson ST, Björk I. Regulation of thrombin by antithrombin and heparin co-factor II. In: Berliner LJ (Editor), Thrombin: structure and function. New York: Plenum Press; 1992. p 159-217.
    • (1992) Thrombin: Structure and function , pp. 159-217
    • Olson, S.T.1    Björk, I.2
  • 4
    • 0020488026 scopus 로고
    • Cloning and expression of the cDNA for human antithrombin III
    • Bock SC, Wion KL, Vehar GA, Lawn RM. Cloning and expression of the cDNA for human antithrombin III. Nucleic Acids Res 1982; 10: 8113-8125.
    • (1982) Nucleic Acids Res , vol.10 , pp. 8113-8125
    • Bock, S.C.1    Wion, K.L.2    Vehar, G.A.3    Lawn, R.M.4
  • 5
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins PG. Serpin structure, mechanism, and function. Chem Rev 2002; 102: 4751-4804.
    • (2002) Chem Rev , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 8
    • 9144269020 scopus 로고    scopus 로고
    • Accellerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin
    • Olson ST, Swanson R, Raub-Segall E, Bedsted T, Sadri M, Petitou M, et al. Accellerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin. Thromb Haemost 2004; 92: 929-939.
    • (2004) Thromb Haemost , vol.92 , pp. 929-939
    • Olson, S.T.1    Swanson, R.2    Raub-Segall, E.3    Bedsted, T.4    Sadri, M.5    Petitou, M.6
  • 9
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson ST, Bjork I, Sheffer R, Craig PA, Shore JD, Choay J. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J Biol Chem 1992; 267: 12528-12538.
    • (1992) J Biol Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 10
    • 0034685780 scopus 로고    scopus 로고
    • The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions
    • Hunlington JA, McCoy A, Belzar KJ, Pei XY, Gettins PG, Carrell RW. The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions. J Biol Chem 2000; 275: 15377-15383.
    • (2000) J Biol Chem , vol.275 , pp. 15377-15383
    • Hunlington, J.A.1    McCoy, A.2    Belzar, K.J.3    Pei, X.Y.4    Gettins, P.G.5    Carrell, R.W.6
  • 11
    • 0032479424 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of haparin binding to factor Xa
    • Rezaie AR. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of haparin binding to factor Xa. J Biol Chem 1998; 273: 16824-16827.
    • (1998) J Biol Chem , vol.273 , pp. 16824-16827
    • Rezaie, A.R.1
  • 12
    • 0034601781 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promobfig the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies
    • Rezaie AR, Olson ST. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promobfig the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies. Biochemistry 2000; 39: 12083-12090.
    • (2000) Biochemistry , vol.39 , pp. 12083-12090
    • Rezaie, A.R.1    Olson, S.T.2
  • 13
    • 0041315481 scopus 로고    scopus 로고
    • Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide
    • Wiebe EM, Stafford AR, Fredenburgh JC, Weitz JI. Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide. J Biol Chem 2003; 278: 35767-35774.
    • (2003) J Biol Chem , vol.278 , pp. 35767-35774
    • Wiebe, E.M.1    Stafford, A.R.2    Fredenburgh, J.C.3    Weitz, J.I.4
  • 14
    • 0021344246 scopus 로고
    • Anticoagulant activities of haparin oligosaccharides and their neutralization by platelet factor 4
    • Lane DA, Denton J, Flynn AM, Thunberg L, Lindahl U. Anticoagulant activities of haparin oligosaccharides and their neutralization by platelet factor 4. Biochem J 1984; 218: 725-732.
    • (1984) Biochem J , vol.218 , pp. 725-732
    • Lane, D.A.1    Denton, J.2    Flynn, A.M.3    Thunberg, L.4    Lindahl, U.5
  • 15
    • 0022977122 scopus 로고
    • Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa
    • Danielsson A, Raub E, Lindahl U, Bjork I. Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa. J Biol Chem 1986; 261: 15467-15473.
    • (1986) J Biol Chem , vol.261 , pp. 15467-15473
    • Danielsson, A.1    Raub, E.2    Lindahl, U.3    Bjork, I.4
  • 16
    • 0024431034 scopus 로고
    • The refined 1.9 A crystal structure of human alpha-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone 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 alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone 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
  • 17
    • 4444283745 scopus 로고    scopus 로고
    • Heparin-activated antithrombin interacts with the autolysis loop of target coaglation proteases
    • Yang L, Manithody C, Rezaie AR. Heparin-activated antithrombin interacts with the autolysis loop of target coaglation proteases. Blood 2004; 104: 1753-1759.
    • (2004) Blood , vol.104 , pp. 1753-1759
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 18
    • 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
  • 19
    • 0042090283 scopus 로고    scopus 로고
    • Contribution of basic residues of the autolysis loop to the substrate and inhibitor specificity of factor IXa
    • Yang L, Manithody C, Olson ST, Rezaie AR. Contribution of basic residues of the autolysis loop to the substrate and inhibitor specificity of factor IXa. J Biol Chem 2003; 278: 25032-25038.
    • (2003) J Biol Chem , vol.278 , pp. 25032-25038
    • Yang, L.1    Manithody, C.2    Olson, S.T.3    Rezaie, A.R.4
  • 20
    • 22144489540 scopus 로고    scopus 로고
    • The functional significance of the autolysis loop in protein C and activated protein C
    • Yang L, Manithody C, Razaie AR. The functional significance of the autolysis loop in protein C and activated protein C. Thromb Haemost 2005; 94: 60-68.
    • (2005) Thromb Haemost , vol.94 , pp. 60-68
    • Yang, L.1    Manithody, C.2    Razaie, A.R.3
  • 21
    • 0027078511 scopus 로고
    • The function of calcium in protein C activation by thrombin and the thrombin-thrombomodulin complex can be distinguished by mutational analysis of protein C derivatives
    • Rezaie AR, Esmon CT. The function of calcium in protein C activation by thrombin and the thrombin-thrombomodulin complex can be distinguished by mutational analysis of protein C derivatives. J Biol Chem 1992; 267: 26104-26109.
    • (1992) J Biol Chem , vol.267 , pp. 26104-26109
    • Rezaie, A.R.1    Esmon, C.T.2
  • 22
    • 0037076527 scopus 로고    scopus 로고
    • Contribution of basic residues of the 70-80-loop to haparin binding and anticoagulant function of activated protein C
    • Yang L, Manithody C, Rezaie AR. Contribution of basic residues of the 70-80-loop to haparin 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
  • 23
    • 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
  • 24
    • 1642493924 scopus 로고    scopus 로고
    • Zymogenic and enzymatic properties of the 70-80 loop mutants of factor X/Xa
    • Chen L, Manithody C, Yang L, Rezaie AR. Zymogenic and enzymatic properties of the 70-80 loop mutants of factor X/Xa. Protein Sci 2004; 13: 431-442.
    • (2004) Protein Sci , vol.13 , pp. 431-442
    • Chen, L.1    Manithody, C.2    Yang, L.3    Rezaie, A.R.4
  • 25
    • 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
  • 26
    • 33646581724 scopus 로고    scopus 로고
    • Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation
    • Johnson DJ, Li W, Adams TE, Huntington JA. Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. EMBO J 2006; 25: 2029-2037.
    • (2006) EMBO J , vol.25 , pp. 2029-2037
    • Johnson, D.J.1    Li, W.2    Adams, T.E.3    Huntington, J.A.4
  • 27
    • 0030468098 scopus 로고    scopus 로고
    • The 2.8 Å crystal structure of Gla-domainless activated protein C
    • Mather T, Oganessyan V, Hof P, Huber R, Foundling S, Esmon C, et al. The 2.8 Å 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    Huber, R.4    Foundling, S.5    Esmon, C.6
  • 28
    • 0034680369 scopus 로고    scopus 로고
    • Preparation, characterization, and the crystal structure of the inhibitor ZK-807834 (C1-1031) complexed with factor Xa
    • Adler M, Davey DD, Phillips GB, Kim SH, Jancarik J, Rumennik G, et al. Preparation, characterization, and the crystal structure of the inhibitor ZK-807834 (C1-1031) complexed with factor Xa. Biochemistry 2000; 39: 12534-12542.
    • (2000) Biochemistry , vol.39 , pp. 12534-12542
    • Adler, M.1    Davey, D.D.2    Phillips, G.B.3    Kim, S.H.4    Jancarik, J.5    Rumennik, G.6
  • 29
    • 0034661942 scopus 로고    scopus 로고
    • The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites
    • Gale AJ, Heeb MJ, Griffin JH. The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites. Blood 2000; 96: 585-593.
    • (2000) Blood , vol.96 , pp. 585-593
    • Gale, A.J.1    Heeb, M.J.2    Griffin, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.