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Volumn 7, Issue 5, 2009, Pages 825-832

Discordant fibrin formation in hemophilia

Author keywords

Factor XIII; Fibrin; Fibrinopeptides; Hemophilia

Indexed keywords

BLOOD CLOTTING FACTOR 13; BLOOD CLOTTING FACTOR 13A; FIBRIN; FIBRINOPEPTIDE; FIBRINOPEPTIDE A; FIBRINOPEPTIDE B; RECOMBINANT BLOOD CLOTTING FACTOR 8; THROMBOPLASTIN;

EID: 65349131350     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2009.03306.x     Document Type: Article
Times cited : (68)

References (43)
  • 1
    • 0038101450 scopus 로고    scopus 로고
    • Haemophilias A and B
    • Bolton-Maggs PH, Pasi KJ. Haemophilias A and B. Lancet 2003; 361: 1801-9.
    • (2003) Lancet , vol.361 , pp. 1801-1809
    • Bolton-Maggs, P.H.1    Pasi, K.J.2
  • 2
    • 0028078717 scopus 로고
    • Hemophilia A
    • Hoyer LW. Hemophilia A. N Engl J Med 1994;330:38-47.
    • (1994) N Engl J Med , vol.330 , pp. 38-47
    • Hoyer, L.W.1
  • 5
    • 0025772165 scopus 로고
    • Cooperative activation of human factor IX by the human extrinsic pathway of blood coagulation
    • Lawson JH, Mann KG. Cooperative activation of human factor IX by the human extrinsic pathway of blood coagulation. J Biol Chem 1991; 266: 11317-27.
    • (1991) J Biol Chem , vol.266 , pp. 11317-11327
    • Lawson, J.H.1    Mann, K.G.2
  • 6
    • 0026668615 scopus 로고
    • Components and assembly of the factor X activating complex
    • Ahmad SS, Rawala-Sheikh R, Walsh PN. Components and assembly of the factor X activating complex. Semin Thromb Hemost 1992; 18: 311-23.
    • (1992) Semin Thromb Hemost , vol.18 , pp. 311-323
    • Ahmad, S.S.1    Rawala-Sheikh, R.2    Walsh, P.N.3
  • 9
    • 0014191175 scopus 로고
    • Actions of thrombin and other coagulant and proteolytic enzymes on blood platelets
    • Davey MG, Luscher EF. Actions of thrombin and other coagulant and proteolytic enzymes on blood platelets. Nature 1967; 216: 857-8.
    • (1967) Nature , vol.216 , pp. 857-858
    • Davey, M.G.1    Luscher, E.F.2
  • 10
    • 0034972479 scopus 로고    scopus 로고
    • Factor XIII: Structure, activation, and interactions with fibrinogen and fibrin
    • Lorand L. Factor XIII: Structure, activation, and interactions with fibrinogen and fibrin. Ann NY Acad Sci 2001; 936: 291-311.
    • (2001) Ann NY Acad Sci , vol.936 , pp. 291-311
    • Lorand, L.1
  • 11
    • 1842293383 scopus 로고    scopus 로고
    • Evaluation of the initiation phase of blood coagulation using ultrasensitive assays for serine proteases
    • Butenas S, van't Veer C, Mann KG. Evaluation of the initiation phase of blood coagulation using ultrasensitive assays for serine proteases. J Biol Chem 1997; 272: 21527-33.
    • (1997) J Biol Chem , vol.272 , pp. 21527-21533
    • Butenas, S.1    van't Veer, C.2    Mann, K.G.3
  • 12
    • 0036660207 scopus 로고    scopus 로고
    • Thrombin functions during tissue factor-induced blood coagulation
    • Brummel KE, Paradis SG, Butenas S, Mann KG. Thrombin functions during tissue factor-induced blood coagulation. Blood 2002; 100: 148-52.
    • (2002) Blood , vol.100 , pp. 148-152
    • Brummel, K.E.1    Paradis, S.G.2    Butenas, S.3    Mann, K.G.4
  • 14
    • 10544253848 scopus 로고    scopus 로고
    • Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma
    • Broze GJ Jr, Higuchi DA. Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma. Blood 1996; 88: 3815-23.
    • (1996) Blood , vol.88 , pp. 3815-3823
    • Broze, G.J.1    Higuchi, D.A.2
  • 15
    • 20844443318 scopus 로고    scopus 로고
    • The effect of platelets on fibrin gel structure formed in the presence of recombinant factor VIIa in hemophilia plasma and in plasma from a patient with Glanzmann thrombasthenia
    • He S, Ekman GJ, Hedner U. The effect of platelets on fibrin gel structure formed in the presence of recombinant factor VIIa in hemophilia plasma and in plasma from a patient with Glanzmann thrombasthenia. J Thromb Haemost 2005; 3: 272-9.
    • (2005) J Thromb Haemost , vol.3 , pp. 272-279
    • He, S.1    Ekman, G.J.2    Hedner, U.3
  • 18
    • 34447648526 scopus 로고    scopus 로고
    • Restoring hemostatic thrombin generation at the time of cutaneous wounding does not normalize healing in hemophilia.B
    • McDonald A, Hoffman M, Hedner U, Roberts HR, Monroe DM. Restoring hemostatic thrombin generation at the time of cutaneous wounding does not normalize healing in hemophilia.B. J Thromb Haemost 2007; 5: 1577-83.
    • (2007) J Thromb Haemost , vol.5 , pp. 1577-1583
    • McDonald, A.1    Hoffman, M.2    Hedner, U.3    Roberts, H.R.4    Monroe, D.M.5
  • 19
    • 0034657826 scopus 로고    scopus 로고
    • An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model
    • Nagashima M, Werner M, Wang M, Zhao L, Light DR, Pagila R, Morser J, Verhallen P. An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model. Thromb Res 2000; 98: 333-42.
    • (2000) Thromb Res , vol.98 , pp. 333-342
    • Nagashima, M.1    Werner, M.2    Wang, M.3    Zhao, L.4    Light, D.R.5    Pagila, R.6    Morser, J.7    Verhallen, P.8
  • 20
    • 0032746651 scopus 로고    scopus 로고
    • Factor XI dependent and independent activation of thrombin activatable fibrinolysis inhibitor (TAFI) in plasma associated with clot formation
    • Bouma BN, Mosnier LO, Meijers JC, Griffin JH. Factor XI dependent and independent activation of thrombin activatable fibrinolysis inhibitor (TAFI) in plasma associated with clot formation. Thromb Haemost 1999; 82: 1703-8.
    • (1999) Thromb Haemost , vol.82 , pp. 1703-1708
    • Bouma, B.N.1    Mosnier, L.O.2    Meijers, J.C.3    Griffin, J.H.4
  • 21
    • 6444220108 scopus 로고    scopus 로고
    • Decreased factor XIII availability for thrombin and early loss of clot firmness in patients with unexplained intraoperative bleeding
    • Wettstein P, Haeberli A, Stutz M, Rohner M, Corbetta C, Gabi K, Schnider T, Korte W. Decreased factor XIII availability for thrombin and early loss of clot firmness in patients with unexplained intraoperative bleeding. Anesth Analg 2004; 99: 1564-9.
    • (2004) Anesth Analg , vol.99 , pp. 1564-1569
    • Wettstein, P.1    Haeberli, A.2    Stutz, M.3    Rohner, M.4    Corbetta, C.5    Gabi, K.6    Schnider, T.7    Korte, W.8
  • 22
    • 0033529539 scopus 로고    scopus 로고
    • An integrated study of fibrinogen during blood coagulation
    • Brummel KE, Butenas S, Mann KG. An integrated study of fibrinogen during blood coagulation. J Biol Chem 1999; 274: 22862-70.
    • (1999) J Biol Chem , vol.274 , pp. 22862-22870
    • Brummel, K.E.1    Butenas, S.2    Mann, K.G.3
  • 23
    • 0036464599 scopus 로고    scopus 로고
    • Mechanism of factor VIIa-dependent coagulation in hemophilia blood
    • Butenas S, Brummel KE, Branda RF, Paradis SG, Mann KG. Mechanism of factor VIIa-dependent coagulation in hemophilia blood. Blood 2002; 99: 923-30.
    • (2002) Blood , vol.99 , pp. 923-930
    • Butenas, S.1    Brummel, K.E.2    Branda, R.F.3    Paradis, S.G.4    Mann, K.G.5
  • 27
    • 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
  • 28
    • 0017601513 scopus 로고
    • Mass-length ratio of fibrin fibers from gel permeation and light scattering
    • Carr ME Jr, Shen LL, Hermans J. Mass-length ratio of fibrin fibers from gel permeation and light scattering. Biopolymers 1977; 16: 1-15.
    • (1977) Biopolymers , vol.16 , pp. 1-15
    • Carr, M.E.1    Shen, L.L.2    Hermans, J.3
  • 30
    • 0027965921 scopus 로고
    • Fibrin in human plasma: Gel architectures governed by rate and nature of fibrinogen activation
    • Blomback B, Carlsson K, Fatah K, Hessel B, Procyk R. Fibrin in human plasma: Gel architectures governed by rate and nature of fibrinogen activation. Thromb Res 1994; 75: 521-38.
    • (1994) Thromb Res , vol.75 , pp. 521-538
    • Blomback, B.1    Carlsson, K.2    Fatah, K.3    Hessel, B.4    Procyk, R.5
  • 31
    • 34047229067 scopus 로고    scopus 로고
    • Thrombin generation and fibrin clot structure
    • Wolberg AS. Thrombin generation and fibrin clot structure. Blood Rev 2007; 21: 131-42.
    • (2007) Blood Rev , vol.21 , pp. 131-142
    • Wolberg, A.S.1
  • 32
    • 0018129207 scopus 로고
    • A two-step fibrinogen-fibrin transition in blood coagulation
    • Blomback B, Hessel B, Hogg D, Therkildsen L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature 1978; 275: 501-5.
    • (1978) Nature , vol.275 , pp. 501-505
    • Blomback, B.1    Hessel, B.2    Hogg, D.3    Therkildsen, L.4
  • 33
    • 0018597469 scopus 로고
    • Assembly of fibrin. A light scattering study
    • Hantgan RR, Hermans J. Assembly of fibrin. A light scattering study. J Biol Chem 1979; 254: 11272-81.
    • (1979) J Biol Chem , vol.254 , pp. 11272-11281
    • Hantgan, R.R.1    Hermans, J.2
  • 34
    • 0019210979 scopus 로고
    • Fibrin assembly: A comparison of electron microscopic and light scattering results
    • Hantgan R, Fowler W, Erickson H, Hermans J. Fibrin assembly: A comparison of electron microscopic and light scattering results. Thromb Haemost 1980; 44: 119-24.
    • (1980) Thromb Haemost , vol.44 , pp. 119-124
    • Hantgan, R.1    Fowler, W.2    Erickson, H.3    Hermans, J.4
  • 36
    • 0033152222 scopus 로고    scopus 로고
    • Blood coagulation factor XIII: Structure and function
    • Muszbek L, Yee VC, Hevessy Z. Blood coagulation factor XIII: Structure and function. Thromb Res 1999; 94: 271-305.
    • (1999) Thromb Res , vol.94 , pp. 271-305
    • Muszbek, L.1    Yee, V.C.2    Hevessy, Z.3
  • 37
    • 0002591546 scopus 로고    scopus 로고
    • Structure and function of factor XIII
    • In: Colman RW, Hirsh J, Marder VJ, Clowes AW, George JN, eds. Philadelphia: Lippincott Williams & Wilkins
    • Lowey AG, McDonagh J, Mikkola H, Teller DC, Yee VC. Structure and function of factor XIII. In: Colman RW, Hirsh J, Marder VJ, Clowes AW, George JN, eds. Hemostasis and Thrombosis. Philadelphia: Lippincott Williams & Wilkins, 2001: 233-47.
    • (2001) Hemostasis and Thrombosis , pp. 233-247
    • Lowey, A.G.1    McDonagh, J.2    Mikkola, H.3    Teller, D.C.4    Yee, V.C.5
  • 38
    • 0023697021 scopus 로고
    • Factor XIII-induced crosslinking in solutions of fibrinogen and fibronectin
    • Procyk R, Blomback B. Factor XIII-induced crosslinking in solutions of fibrinogen and fibronectin. Biochim Biophys Acta 1988; 967: 304-13.
    • (1988) Biochim Biophys Acta , vol.967 , pp. 304-313
    • Procyk, R.1    Blomback, B.2
  • 39
    • 0020351368 scopus 로고
    • Cross-linking of alpha 2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor
    • Tamaki T, Aoki N. Cross-linking of alpha 2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor. J Biol Chem 1982; 257: 14767-72.
    • (1982) J Biol Chem , vol.257 , pp. 14767-14772
    • Tamaki, T.1    Aoki, N.2
  • 40
    • 0018682304 scopus 로고
    • Cross-linking of fibronectin to collagen by blood coagulation Factor XIIIa
    • Mosher DF, Schad PE. Cross-linking of fibronectin to collagen by blood coagulation Factor XIIIa. J Clin Invest 1979; 64: 781-7.
    • (1979) J Clin Invest , vol.64 , pp. 781-787
    • Mosher, D.F.1    Schad, P.E.2
  • 41
    • 0017699096 scopus 로고
    • Cross-linking of actin and fibrin by fibrin-stabilizing factor
    • Mui PT, Ganguly P. Cross-linking of actin and fibrin by fibrin-stabilizing factor. Am J Physiol 1977; 233: H346-9.
    • (1977) Am J Physiol , vol.233
    • Mui, P.T.1    Ganguly, P.2
  • 42
    • 0023215552 scopus 로고
    • Characterization of thrombospondin as a substrate for factor XIII transglutaminase
    • Lynch GW, Slayter HS, Miller BE, McDonagh J. Characterization of thrombospondin as a substrate for factor XIII transglutaminase. J Biol Chem 1987; 262: 1772-8.
    • (1987) J Biol Chem , vol.262 , pp. 1772-1778
    • Lynch, G.W.1    Slayter, H.S.2    Miller, B.E.3    McDonagh, J.4
  • 43
    • 36348983304 scopus 로고    scopus 로고
    • Tranexamic acid combined with recombinant factor VIII increases clot resistance to accelerated fibrinolysis in severe hemophilia A
    • Hvas AM, Sorensen HT, Norengaard L, Christiansen K, Ingerslev J, Sorensen B. Tranexamic acid combined with recombinant factor VIII increases clot resistance to accelerated fibrinolysis in severe hemophilia A. J Thromb Haemost 2007; 5: 2408-14.
    • (2007) J Thromb Haemost , vol.5 , pp. 2408-2414
    • Hvas, A.M.1    Sorensen, H.T.2    Norengaard, L.3    Christiansen, K.4    Ingerslev, J.5    Sorensen, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.