메뉴 건너뛰기




Volumn 130, Issue 3, 2012, Pages 528-534

Thrombomodulin-dependent effect of factor v Leiden mutation on the cross-linking of α2-plasmin inhibitor to fibrin and its consequences on fibrinolysis

Author keywords

2 plasmin inhibitor; factor V Leiden mutation; factor XIII; fibrinolysis; thrombin activatable fibrinolysis inhibitor

Indexed keywords

ALPHA 2 ANTIPLASMIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; FIBRIN; PHOSPHOLIPID; RECOMBINANT THROMBOMODULIN; TISSUE PLASMINOGEN ACTIVATOR;

EID: 84865208467     PISSN: 00493848     EISSN: 18792472     Source Type: Journal    
DOI: 10.1016/j.thromres.2012.05.019     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0028959158 scopus 로고
    • Inherited thrombophilia: Resistance to activated protein C as a pathogenic factor of venous thromboembolism
    • B. Dahlback Inherited thrombophilia: Resistance to activated protein C as a pathogenic factor of venous thromboembolism Blood 85 1995 607 614
    • (1995) Blood , vol.85 , pp. 607-614
    • Dahlback, B.1
  • 2
    • 0033519051 scopus 로고    scopus 로고
    • Venous thrombosis: A multicausal disease
    • F.R. Rosendaal Venous thrombosis: A multicausal disease Lancet 353 1999 1167 1173
    • (1999) Lancet , vol.353 , pp. 1167-1173
    • Rosendaal, F.R.1
  • 3
    • 0028314865 scopus 로고
    • Mutation in blood coagulation factor v associated with resistance to activated protein C
    • R.M. Bertina, B.P. Koeleman, T. Koster, F.R. Rosendaal, R.J. Dirven, and H. de Ronde Mutation in blood coagulation factor V associated with resistance to activated protein C Nature 369 1994 64 67
    • (1994) Nature , vol.369 , pp. 64-67
    • Bertina, R.M.1    Koeleman, B.P.2    Koster, T.3    Rosendaal, F.R.4    Dirven, R.J.5    De Ronde, H.6
  • 4
    • 34548698444 scopus 로고    scopus 로고
    • Coagulation factor v and thrombophilia: Background and mechanisms
    • K. Segers, B. Dahlback, and G.A. Nicolaes Coagulation factor V and thrombophilia: Background and mechanisms Thromb Haemost 98 2007 530 542
    • (2007) Thromb Haemost , vol.98 , pp. 530-542
    • Segers, K.1    Dahlback, B.2    Nicolaes, G.A.3
  • 5
    • 47249084343 scopus 로고    scopus 로고
    • Advances in understanding pathogenic mechanisms of thrombophilic disorders
    • B. Dahlback Advances in understanding pathogenic mechanisms of thrombophilic disorders Blood 112 2008 19 27
    • (2008) Blood , vol.112 , pp. 19-27
    • Dahlback, B.1
  • 6
    • 1642530216 scopus 로고    scopus 로고
    • Increased tissue factor-initiated prothrombin activation as a result of the Arg506 - > Gln mutation in factor VLEIDEN
    • C. van 't Veer, M. Kalafatis, R.M. Bertina, P. Simioni, and K.G. Mann Increased tissue factor-initiated prothrombin activation as a result of the Arg506 - > Gln mutation in factor VLEIDEN J Biol Chem 272 1997 20721 20729
    • (1997) J Biol Chem , vol.272 , pp. 20721-20729
    • Van 'T Veer, C.1    Kalafatis, M.2    Bertina, R.M.3    Simioni, P.4    Mann, K.G.5
  • 7
    • 0033561431 scopus 로고    scopus 로고
    • Cleavage of factor v at Arg 506 by activated protein C and the expression of anticoagulant activity of factor v
    • E. Thorelli, R.J. Kaufman, and B. Dahlback Cleavage of factor V at Arg 506 by activated protein C and the expression of anticoagulant activity of factor V Blood 93 1999 2552 2558
    • (1999) Blood , vol.93 , pp. 2552-2558
    • Thorelli, E.1    Kaufman, R.J.2    Dahlback, B.3
  • 8
    • 2542486395 scopus 로고    scopus 로고
    • Impaired APC cofactor activity of factor v plays a major role in the APC resistance associated with the factor v Leiden (R506Q) and R2 (H1299R) mutations
    • E. Castoldi, J.M. Brugge, G.A. Nicolaes, D. Girelli, G. Tans, and J. Rosing Impaired APC cofactor activity of factor V plays a major role in the APC resistance associated with the factor V Leiden (R506Q) and R2 (H1299R) mutations Blood 103 2004 4173 4179
    • (2004) Blood , vol.103 , pp. 4173-4179
    • Castoldi, E.1    Brugge, J.M.2    Nicolaes, G.A.3    Girelli, D.4    Tans, G.5    Rosing, J.6
  • 9
    • 0031058039 scopus 로고    scopus 로고
    • Regulation of tissue factor initiated thrombin generation by the stoichiometric inhibitors tissue factor pathway inhibitor, antithrombin-III, and heparin cofactor-II
    • C. van 't Veer, and K.G. Mann Regulation of tissue factor initiated thrombin generation by the stoichiometric inhibitors tissue factor pathway inhibitor, antithrombin-III, and heparin cofactor-II J Biol Chem 272 1997 4367 4377
    • (1997) J Biol Chem , vol.272 , pp. 4367-4377
    • Van 'T Veer, C.1    Mann, K.G.2
  • 10
    • 33646480218 scopus 로고    scopus 로고
    • Inflammation and the activated protein C anticoagulant pathway
    • C.T. Esmon Inflammation and the activated protein C anticoagulant pathway Semin Thromb Hemost 32 Suppl. 1 2006 49 60
    • (2006) Semin Thromb Hemost , vol.32 , Issue.SUPPL. 1 , pp. 49-60
    • Esmon, C.T.1
  • 11
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • L. Bajzar, R. Manuel, and M.E. Nesheim Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor J Biol Chem 270 1995 14477 14484
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 12
    • 77953779759 scopus 로고    scopus 로고
    • What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse?
    • J. Morser, E.C. Gabazza, T. Myles, and L.L. Leung What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse? J Thromb Haemost 8 2010 868 876
    • (2010) J Thromb Haemost , vol.8 , pp. 868-876
    • Morser, J.1    Gabazza, E.C.2    Myles, T.3    Leung, L.L.4
  • 13
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • M. Nesheim, W. Wang, M. Boffa, M. Nagashima, J. Morser, and L. Bajzar Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis Thromb Haemost 78 1997 386 391
    • (1997) Thromb Haemost , vol.78 , pp. 386-391
    • Nesheim, M.1    Wang, W.2    Boffa, M.3    Nagashima, M.4    Morser, J.5    Bajzar, L.6
  • 14
    • 0141707850 scopus 로고    scopus 로고
    • Thrombin and fibrinolysis
    • M. Nesheim Thrombin and fibrinolysis Chest 124 2003 33S 39S
    • (2003) Chest , vol.124
    • Nesheim, M.1
  • 15
    • 33750222459 scopus 로고    scopus 로고
    • Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis
    • L.O. Mosnier, and B.N. Bouma Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis Arterioscler Thromb Vasc Biol 26 2006 2445 2453
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 2445-2453
    • Mosnier, L.O.1    Bouma, B.N.2
  • 16
    • 0029810712 scopus 로고    scopus 로고
    • An antifibrinolytic mechanism describing the prothrombotic effect associated with factor VLeiden
    • L. Bajzar, M. Kalafatis, P. Simioni, and P.B. Tracy An antifibrinolytic mechanism describing the prothrombotic effect associated with factor VLeiden J Biol Chem 271 1996 22949 22952
    • (1996) J Biol Chem , vol.271 , pp. 22949-22952
    • Bajzar, L.1    Kalafatis, M.2    Simioni, P.3    Tracy, P.B.4
  • 17
    • 0035173479 scopus 로고    scopus 로고
    • Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin
    • L.O. Mosnier, J.C. Meijers, and B.N. Bouma Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin Thromb Haemost 85 2001 5 11
    • (2001) Thromb Haemost , vol.85 , pp. 5-11
    • Mosnier, L.O.1    Meijers, J.C.2    Bouma, B.N.3
  • 19
    • 79960076132 scopus 로고    scopus 로고
    • Factor XIII: A coagulation factor with multiple plasmatic and cellular functions
    • L. Muszbek, Z. Bereczky, Z. Bagoly, I. Komaromi, and E. Katona Factor XIII: A coagulation factor with multiple plasmatic and cellular functions Physiol Rev 91 2011 931 972
    • (2011) Physiol Rev , vol.91 , pp. 931-972
    • Muszbek, L.1    Bereczky, Z.2    Bagoly, Z.3    Komaromi, I.4    Katona, E.5
  • 20
    • 0022872450 scopus 로고
    • Thrombomodulin inhibits the activation of factor XIII by thrombin
    • J. Polgar, I. Lerant, L. Muszbek, and R. Machovich Thrombomodulin inhibits the activation of factor XIII by thrombin Thromb Res 43 1986 685 690
    • (1986) Thromb Res , vol.43 , pp. 685-690
    • Polgar, J.1    Lerant, I.2    Muszbek, L.3    MacHovich, R.4
  • 21
    • 0042858157 scopus 로고    scopus 로고
    • Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate
    • H. Philippou, J. Rance, T. Myles, S.W. Hall, R.A. Ariens, and P.J. Grant Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate J Biol Chem 278 2003 32020 32026
    • (2003) J Biol Chem , vol.278 , pp. 32020-32026
    • Philippou, H.1    Rance, J.2    Myles, T.3    Hall, S.W.4    Ariens, R.A.5    Grant, P.J.6
  • 22
    • 84858336194 scopus 로고    scopus 로고
    • Thrombomodulin-dependent effect of factor V(Leiden) mutation on factor XIII activation
    • 10.1016/j.thromres.2011.06.030
    • Z. Koncz, Z. Bagoly, G. Haramura, Z.A. Mezei, and L. Muszbek Thrombomodulin-dependent effect of factor V(Leiden) mutation on factor XIII activation Thromb Res 2011 10.1016/j.thromres.2011.06.030
    • (2011) Thromb Res
    • Koncz, Z.1    Bagoly, Z.2    Haramura, G.3    Mezei, Z.A.4    Muszbek, L.5
  • 23
    • 0034307686 scopus 로고    scopus 로고
    • Val34Leu polymorphism of plasma factor XIII: Biochemistry and epidemiology in familial thrombophilia
    • I. Balogh, G. Szoke, L. Karpati, U. Wartiovaara, E. Katona, and I. Komaromi Val34Leu polymorphism of plasma factor XIII: Biochemistry and epidemiology in familial thrombophilia Blood 96 2000 2479 2486
    • (2000) Blood , vol.96 , pp. 2479-2486
    • Balogh, I.1    Szoke, G.2    Karpati, L.3    Wartiovaara, U.4    Katona, E.5    Komaromi, I.6
  • 24
    • 0034254319 scopus 로고    scopus 로고
    • The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure
    • R.A. Ariens, H. Philippou, C. Nagaswami, J.W. Weisel, D.A. Lane, and P.J. Grant The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure Blood 96 2000 988 995
    • (2000) Blood , vol.96 , pp. 988-995
    • Ariens, R.A.1    Philippou, H.2    Nagaswami, C.3    Weisel, J.W.4    Lane, D.A.5    Grant, P.J.6
  • 25
    • 33747754789 scopus 로고    scopus 로고
    • The combined effect of fibrin formation and factor XIII A subunit Val34Leu polymorphism on the activation of factor XIII in whole plasma
    • A.H. Shemirani, G. Haramura, Z. Bagoly, and L. Muszbek The combined effect of fibrin formation and factor XIII A subunit Val34Leu polymorphism on the activation of factor XIII in whole plasma Biochim Biophys Acta 1764 2006 1420 1423
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1420-1423
    • Shemirani, A.H.1    Haramura, G.2    Bagoly, Z.3    Muszbek, L.4
  • 26
    • 0034528993 scopus 로고    scopus 로고
    • Effect of factor XIII Val34Leu on alpha2-antiplasmin incorporation into fibrin
    • V. Schroder, and H.P. Kohler Effect of factor XIII Val34Leu on alpha2-antiplasmin incorporation into fibrin Thromb Haemost 84 2000 1128 1130
    • (2000) Thromb Haemost , vol.84 , pp. 1128-1130
    • Schroder, V.1    Kohler, H.P.2
  • 27
    • 0028000665 scopus 로고
    • Activated protein C resistance as an additional risk factor for thrombosis in protein C-deficient families
    • B.P. Koeleman, P.H. Reitsma, C.F. Allaart, and R.M. Bertina Activated protein C resistance as an additional risk factor for thrombosis in protein C-deficient families Blood 84 1994 1031 1035
    • (1994) Blood , vol.84 , pp. 1031-1035
    • Koeleman, B.P.1    Reitsma, P.H.2    Allaart, C.F.3    Bertina, R.M.4
  • 28
    • 4444249428 scopus 로고    scopus 로고
    • Rapid detection of the factor XIII Val34Leu (163 G->T) polymorphism by real-time PCR using fluorescence resonance energy transfer detection and melting curve analysis
    • A.H. Shemirani, and L. Muszbek Rapid detection of the factor XIII Val34Leu (163 G->T) polymorphism by real-time PCR using fluorescence resonance energy transfer detection and melting curve analysis Clin Chem Lab Med 42 2004 877 879
    • (2004) Clin Chem Lab Med , vol.42 , pp. 877-879
    • Shemirani, A.H.1    Muszbek, L.2
  • 29
    • 0033529539 scopus 로고    scopus 로고
    • An integrated study of fibrinogen during blood coagulation
    • K.E. Brummel, S. Butenas, and K.G. Mann An integrated study of fibrinogen during blood coagulation J Biol Chem 274 1999 22862 22870
    • (1999) J Biol Chem , vol.274 , pp. 22862-22870
    • Brummel, K.E.1    Butenas, S.2    Mann, K.G.3
  • 30
    • 0018909419 scopus 로고
    • Human coagluation factor v purification and thrombin-catalyzed activation
    • B. Dahlback Human coagluation factor V purification and thrombin-catalyzed activation J Clin Invest 66 1980 583 591
    • (1980) J Clin Invest , vol.66 , pp. 583-591
    • Dahlback, B.1
  • 31
    • 50849110526 scopus 로고    scopus 로고
    • Thrombomodulin-modified thrombin generation after in vivo recombinant factor VIII treatment in severe hemophilia A
    • A.W. Dielis, W.M. Balliel, R. van Oerle, W.T. Hermens, H.M. Spronk, and H. Ten Cate Thrombomodulin-modified thrombin generation after in vivo recombinant factor VIII treatment in severe hemophilia A Haematologica 93 2008 1351 1357
    • (2008) Haematologica , vol.93 , pp. 1351-1357
    • Dielis, A.W.1    Balliel, W.M.2    Van Oerle, R.3    Hermens, W.T.4    Spronk, H.M.5    Ten Cate, H.6
  • 32
    • 0018864494 scopus 로고
    • Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor
    • Y. Sakata, and N. Aoki Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor J Clin Invest 65 1980 290 297
    • (1980) J Clin Invest , vol.65 , pp. 290-297
    • Sakata, Y.1    Aoki, N.2
  • 34
    • 2342447229 scopus 로고    scopus 로고
    • A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion
    • K.N. Lee, K.W. Jackson, V.J. Christiansen, K.H. Chung, and P.A. McKee A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion Blood 103 2004 3783 3788
    • (2004) Blood , vol.103 , pp. 3783-3788
    • Lee, K.N.1    Jackson, K.W.2    Christiansen, V.J.3    Chung, K.H.4    McKee, P.A.5
  • 35
    • 0024423657 scopus 로고
    • Expression and characterization of pro alpha 2-plasmin inhibitor
    • Y. Sumi, Y. Ichikawa, Y. Nakamura, O. Miura, and N. Aoki Expression and characterization of pro alpha 2-plasmin inhibitor J Biochem 106 1989 703 707
    • (1989) J Biochem , vol.106 , pp. 703-707
    • Sumi, Y.1    Ichikawa, Y.2    Nakamura, Y.3    Miura, O.4    Aoki, N.5
  • 36
    • 0027315990 scopus 로고
    • Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma
    • K. Bangert, A.H. Johnsen, U. Christensen, and S. Thorsen Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma Biochem J 291 Pt 2 1993 623 625
    • (1993) Biochem J , vol.291 , Issue.PART 2 , pp. 623-625
    • Bangert, K.1    Johnsen, A.H.2    Christensen, U.3    Thorsen, S.4
  • 37
    • 0022979474 scopus 로고
    • Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor
    • S. Kimura, and N. Aoki Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor J Biol Chem 261 1986 15591 15595
    • (1986) J Biol Chem , vol.261 , pp. 15591-15595
    • Kimura, S.1    Aoki, N.2
  • 38
    • 0020077284 scopus 로고
    • Significance of cross-linking of alpha 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis
    • Y. Sakata, and N. Aoki Significance of cross-linking of alpha 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis J Clin Invest 69 1982 536 542
    • (1982) J Clin Invest , vol.69 , pp. 536-542
    • Sakata, Y.1    Aoki, N.2
  • 39
    • 79959486796 scopus 로고    scopus 로고
    • The antifibrinolytic function of factor XIII is exclusively expressed through alpha-antiplasmin cross-linking
    • S.R. Fraser, N.A. Booth, and N.J. Mutch The antifibrinolytic function of factor XIII is exclusively expressed through alpha-antiplasmin cross-linking Blood 117 2011 6371 6374
    • (2011) Blood , vol.117 , pp. 6371-6374
    • Fraser, S.R.1    Booth, N.A.2    Mutch, N.J.3
  • 40
    • 0034758304 scopus 로고    scopus 로고
    • Protein C inhibitor regulates the thrombin-thrombomodulin complex in the up- and down regulation of TAFI activation
    • L.O. Mosnier, M.G. Elisen, B.N. Bouma, and J.C. Meijers Protein C inhibitor regulates the thrombin-thrombomodulin complex in the up- and down regulation of TAFI activation Thromb Haemost 86 2001 1057 1064
    • (2001) Thromb Haemost , vol.86 , pp. 1057-1064
    • Mosnier, L.O.1    Elisen, M.G.2    Bouma, B.N.3    Meijers, J.C.4
  • 41
    • 0034759378 scopus 로고    scopus 로고
    • The role of protein S in the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and regulation of fibrinolysis
    • L.O. Mosnier, J.C. Meijers, and B.N. Bouma The role of protein S in the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and regulation of fibrinolysis Thromb Haemost 86 2001 1040 1046
    • (2001) Thromb Haemost , vol.86 , pp. 1040-1046
    • Mosnier, L.O.1    Meijers, J.C.2    Bouma, B.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.