메뉴 건너뛰기




Volumn 118, Issue 5, 2006, Pages 651-661

In vitro fibrin clot formation and fibrinolysis using heterozygous plasma fibrinogen from γAsn319, Asp320 deletion dysfibrinogen, Otsu I

Author keywords

319; 320 deletion; Dysfibrinogen; Fibrin clot formation; Fibrinolysis; Tissue type plasminogen activator

Indexed keywords

FIBRIN; FIBRINOGEN; FIBRINOGEN OTSU 1; PLASMIN; PLASMINOGEN; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG;

EID: 33748775473     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.thromres.2005.10.013     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 0040119537 scopus 로고
    • Evidence for four different polymerization sites involved in human fibrin formation
    • Olexa S.A., and Budzynski A.Z. Evidence for four different polymerization sites involved in human fibrin formation. Proc Natl Acad Sci U S A 77 (1980) 1374-1378
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1374-1378
    • Olexa, S.A.1    Budzynski, A.Z.2
  • 2
    • 33748802575 scopus 로고    scopus 로고
    • http://www.geht.org/pages/databaseang/fibrinogen/.
  • 3
    • 0025816449 scopus 로고
    • A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization
    • Koopman J., Haverkate F., Briet E., and Lord S.T. A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem 266 (1991) 13456-13461
    • (1991) J Biol Chem , vol.266 , pp. 13456-13461
    • Koopman, J.1    Haverkate, F.2    Briet, E.3    Lord, S.T.4
  • 4
    • 0028877613 scopus 로고
    • Familial dysfibrinogenemia and thrombophilia. Report on a study of the SSC subcommittee on fibrinogen
    • Haverkate S., and Samama M. Familial dysfibrinogenemia and thrombophilia. Report on a study of the SSC subcommittee on fibrinogen. Thromb Haemost 73 (1995) 151-161
    • (1995) Thromb Haemost , vol.73 , pp. 151-161
    • Haverkate, S.1    Samama, M.2
  • 6
    • 0030725658 scopus 로고    scopus 로고
    • Severely impaired polymerization of recombinant fibrinogen γ-364 Asp→His, the substitution discovered in a heterozygous individual
    • Okumura N., Gorkun O.V., and Lord S.T. Severely impaired polymerization of recombinant fibrinogen γ-364 Asp→His, the substitution discovered in a heterozygous individual. J Biol Chem 272 (1997) 29596-29601
    • (1997) J Biol Chem , vol.272 , pp. 29596-29601
    • Okumura, N.1    Gorkun, O.V.2    Lord, S.T.3
  • 7
    • 0142060996 scopus 로고    scopus 로고
    • Fibrinogen Otsu I: A γAsn319, Asp320 deletion dysfibrinogen identified in an asymptomatic pregnant woman
    • Terasawa F., Hogan K.A., Kani S., Hirose M., Eguchi Y., Noda Y., et al. Fibrinogen Otsu I: A γAsn319, Asp320 deletion dysfibrinogen identified in an asymptomatic pregnant woman. Thromb Haemost 90 (2003) 757-758
    • (2003) Thromb Haemost , vol.90 , pp. 757-758
    • Terasawa, F.1    Hogan, K.A.2    Kani, S.3    Hirose, M.4    Eguchi, Y.5    Noda, Y.6
  • 8
    • 0141785263 scopus 로고    scopus 로고
    • Fibrinogen Kosai and Ogasa: Bβ15Gly→Cys (GGT→TGT) substitution associated with impairment of fibrinopeptide B release and lateral aggregation
    • Hirota-Kawadobora M., Terasawa F., Yonekawa O., Sahara N., Shimizu E., Okumura N., et al. Fibrinogen Kosai and Ogasa: Bβ15Gly→Cys (GGT→TGT) substitution associated with impairment of fibrinopeptide B release and lateral aggregation. J Thromb Haemost 1 (2003) 275-283
    • (2003) J Thromb Haemost , vol.1 , pp. 275-283
    • Hirota-Kawadobora, M.1    Terasawa, F.2    Yonekawa, O.3    Sahara, N.4    Shimizu, E.5    Okumura, N.6
  • 9
    • 3242667358 scopus 로고    scopus 로고
    • Recombinant fibrinogen, γ275Arg→Cys exhibits formation of disulfide bond with cysteine and severely impaired D:D interactions
    • Ishikawa S., Hirota-Kawadobora M., Tozuka M., Ishii K., Terasawa F., and Okumura N. Recombinant fibrinogen, γ275Arg→Cys exhibits formation of disulfide bond with cysteine and severely impaired D:D interactions. J Thromb Haemost 2 (2003) 468-475
    • (2003) J Thromb Haemost , vol.2 , pp. 468-475
    • Ishikawa, S.1    Hirota-Kawadobora, M.2    Tozuka, M.3    Ishii, K.4    Terasawa, F.5    Okumura, N.6
  • 10
    • 4444286155 scopus 로고    scopus 로고
    • Investigation of residues in the fibrin(ogen) γ chain involved in tissue plasminogen activator binding and plasminogen activation
    • Wilhelm S.E., Lounes K.C., and Lord S.T. Investigation of residues in the fibrin(ogen) γ chain involved in tissue plasminogen activator binding and plasminogen activation. Blood Coagul Fibrinolysis 15 (2004) 451-461
    • (2004) Blood Coagul Fibrinolysis , vol.15 , pp. 451-461
    • Wilhelm, S.E.1    Lounes, K.C.2    Lord, S.T.3
  • 11
    • 0035209672 scopus 로고    scopus 로고
    • Disintegration and reorganization of fibrin networks during tissue-type plasminogen activator-induced clot lysis
    • Meh D.A., Mosesson M.W., DiOrio J.P., Siebenlist K.R., Hernandez I., Amrani D.L., et al. Disintegration and reorganization of fibrin networks during tissue-type plasminogen activator-induced clot lysis. Blood Coagul Fibrinolysis 12 (2001) 637-672
    • (2001) Blood Coagul Fibrinolysis , vol.12 , pp. 637-672
    • Meh, D.A.1    Mosesson, M.W.2    DiOrio, J.P.3    Siebenlist, K.R.4    Hernandez, I.5    Amrani, D.L.6
  • 12
    • 0034977041 scopus 로고    scopus 로고
    • Clot lysis of variant recombinant fibrinogens confirms that fiber diameter is a major determinant of lysis rate
    • Mullin J.L., Norfolk S.E., Weisel J.W., and Lord S.T. Clot lysis of variant recombinant fibrinogens confirms that fiber diameter is a major determinant of lysis rate. Ann NY Acad Sci 936 (2001) 331-334
    • (2001) Ann NY Acad Sci , vol.936 , pp. 331-334
    • Mullin, J.L.1    Norfolk, S.E.2    Weisel, J.W.3    Lord, S.T.4
  • 13
    • 0032787011 scopus 로고    scopus 로고
    • Hypofibrinogenemia associates with a heterozygous missense mutation γ153Cys to Arg (Matsumoto IV): in vitro expression demonstrates defective secretion of the variant fibrinogen
    • Terasawa F., Okumura N., Kitano K., Hayashida N., Shimosaka M., and Okazaki M. Hypofibrinogenemia associates with a heterozygous missense mutation γ153Cys to Arg (Matsumoto IV): in vitro expression demonstrates defective secretion of the variant fibrinogen. Blood 94 (1999) 4122-4131
    • (1999) Blood , vol.94 , pp. 4122-4131
    • Terasawa, F.1    Okumura, N.2    Kitano, K.3    Hayashida, N.4    Shimosaka, M.5    Okazaki, M.6
  • 14
    • 13444283500 scopus 로고    scopus 로고
    • Residue γ153Cys is essential for the formation of the complexes Aαγ and Bβγ, assembly intermediates for the AαBβγ complex and intact fibrinogen
    • Terasawa F., Fujita K., and Okumura N. Residue γ153Cys is essential for the formation of the complexes Aαγ and Bβγ, assembly intermediates for the AαBβγ complex and intact fibrinogen. Clin Chim Acta 353 (2005) 157-164
    • (2005) Clin Chim Acta , vol.353 , pp. 157-164
    • Terasawa, F.1    Fujita, K.2    Okumura, N.3
  • 15
    • 0009571155 scopus 로고
    • Impaired platelet aggregation support by two dysfibrinogens: a γ319-320 deletion and a γ310Met→Thr substitution
    • Glanakis D.K., Spitzer S.G., Scharrer I., and Peerschke E.I. Impaired platelet aggregation support by two dysfibrinogens: a γ319-320 deletion and a γ310Met→Thr substitution. Thromb Haemost 69 (1993) 2564
    • (1993) Thromb Haemost , vol.69 , pp. 2564
    • Glanakis, D.K.1    Spitzer, S.G.2    Scharrer, I.3    Peerschke, E.I.4
  • 16
    • 14044276227 scopus 로고    scopus 로고
    • The fibrinolytic system and thrombotic tendency
    • Kluft C. The fibrinolytic system and thrombotic tendency. Pathophysiol Haemost Thromb 33 (2003/4) 425-429
    • (2003) Pathophysiol Haemost Thromb , vol.33 , pp. 425-429
    • Kluft, C.1
  • 17
    • 0031568321 scopus 로고    scopus 로고
    • Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen
    • Yee V.C., Pratt K.P., Côté H.C.P., Le Trong I., Chung D.W., Davie E.W., et al. Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen. Structure 5 (1997) 125-138
    • (1997) Structure , vol.5 , pp. 125-138
    • Yee, V.C.1    Pratt, K.P.2    Côté, H.C.P.3    Le Trong, I.4    Chung, D.W.5    Davie, E.W.6
  • 18
    • 0034719105 scopus 로고    scopus 로고
    • Conversion of fibrinogen to fibrin: mechanism of exposure of tPA- and plasminogen-binding sites
    • Yakovlev S., Makogonenko E., Kurochkina N., Nieuwenhuizen W., Ingham K., and Medved L. Conversion of fibrinogen to fibrin: mechanism of exposure of tPA- and plasminogen-binding sites. Biochemistry 39 (2000) 15730-15741
    • (2000) Biochemistry , vol.39 , pp. 15730-15741
    • Yakovlev, S.1    Makogonenko, E.2    Kurochkina, N.3    Nieuwenhuizen, W.4    Ingham, K.5    Medved, L.6
  • 19
    • 0026521641 scopus 로고
    • Localization in the fibrinogen γ-chain of a new site that is involved in the acceleration of the tissue-type plasminogen activator-catalyzed activation of plasminogen
    • Yonekawa O., Voskuilen M., and Nieuwenhuizen W. Localization in the fibrinogen γ-chain of a new site that is involved in the acceleration of the tissue-type plasminogen activator-catalyzed activation of plasminogen. Biochem J 283 (1992) 187-191
    • (1992) Biochem J , vol.283 , pp. 187-191
    • Yonekawa, O.1    Voskuilen, M.2    Nieuwenhuizen, W.3
  • 20
    • 13244277924 scopus 로고    scopus 로고
    • Neonatal bleeding and decreased plasma fibrinogen levels in mice modeled after the dysfibrinogen Vlissingen/Frankfult IV
    • Hogan K.A., Merenbloom B.K., Kim H.S., and Lord S.T. Neonatal bleeding and decreased plasma fibrinogen levels in mice modeled after the dysfibrinogen Vlissingen/Frankfult IV. J Thromb Haemost 2 (2004) 1484-1487
    • (2004) J Thromb Haemost , vol.2 , pp. 1484-1487
    • Hogan, K.A.1    Merenbloom, B.K.2    Kim, H.S.3    Lord, S.T.4
  • 21
    • 0020596374 scopus 로고
    • A new type of congenital dysfibrinogenaemia with defective fibrin lysis - Dusard syndrome: possible relation to thrombosis
    • Soria J., Soria C., and Caen J.-P. A new type of congenital dysfibrinogenaemia with defective fibrin lysis - Dusard syndrome: possible relation to thrombosis. Br J Haematol 53 (1983) 575-586
    • (1983) Br J Haematol , vol.53 , pp. 575-586
    • Soria, J.1    Soria, C.2    Caen, J.-P.3
  • 22
    • 0021341834 scopus 로고
    • Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation
    • Lijnen H.R., Soria J., Soria C., Collen D., and Caen J.-P. Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation. Thromb Haemost 51 (1984) 108-109
    • (1984) Thromb Haemost , vol.51 , pp. 108-109
    • Lijnen, H.R.1    Soria, J.2    Soria, C.3    Collen, D.4    Caen, J.-P.5
  • 23
    • 0027299807 scopus 로고
    • Molecular basis for fibrinogen Dusart (Aα554Arg→Cys) and its association with abnormal fibrin polymerization and thrombophilia
    • Koopman J., Haverkate F., Grimbergen J., Lord S.T., Mosesson M.W., DiOrio J.P., et al. Molecular basis for fibrinogen Dusart (Aα554Arg→Cys) and its association with abnormal fibrin polymerization and thrombophilia. J Clin Invest 91 (1993) 1637-1643
    • (1993) J Clin Invest , vol.91 , pp. 1637-1643
    • Koopman, J.1    Haverkate, F.2    Grimbergen, J.3    Lord, S.T.4    Mosesson, M.W.5    DiOrio, J.P.6
  • 24
    • 0027517306 scopus 로고
    • Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure
    • Collet J.-P., Soria J., Mirshahi M., et al. Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. Blood 82 (1993) 2462-2469
    • (1993) Blood , vol.82 , pp. 2462-2469
    • Collet, J.-P.1    Soria, J.2    Mirshahi, M.3
  • 25
    • 0030068432 scopus 로고    scopus 로고
    • Fibrinogen Dusart: electron microscopy of molecules, fibers and clots, and viscoelastic properties of clots
    • Collet J.-P., Woodhead J.L., Soria J., et al. Fibrinogen Dusart: electron microscopy of molecules, fibers and clots, and viscoelastic properties of clots. Biophys J 70 (1996) 500-510
    • (1996) Biophys J , vol.70 , pp. 500-510
    • Collet, J.-P.1    Woodhead, J.L.2    Soria, J.3
  • 26
    • 0029885335 scopus 로고    scopus 로고
    • The relationship between the fibrinogen D domain self-association/cross-linking site (γXL) and the fibrinogen Dusart abnormality (AαR554C-albumin). Clues to thrombophilia in the "Dusart syndrome"
    • Mosesson M.W., Siebenlist K.R., Hainfeld J.F., Wall J.S., Soria C., and Caen J.P. The relationship between the fibrinogen D domain self-association/cross-linking site (γXL) and the fibrinogen Dusart abnormality (AαR554C-albumin). Clues to thrombophilia in the "Dusart syndrome". J Clin Invest 97 (1996) 2342-2350
    • (1996) J Clin Invest , vol.97 , pp. 2342-2350
    • Mosesson, M.W.1    Siebenlist, K.R.2    Hainfeld, J.F.3    Wall, J.S.4    Soria, C.5    Caen, J.P.6
  • 27
    • 0026769907 scopus 로고
    • Molecular basis of Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of Bβ68Ala→Thr
    • Koopman J., Harverkate F., Lord S.T., Grimbergen J., and Mannucci P.M. Molecular basis of Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of Bβ68Ala→Thr. J Clin Invest 90 (1992) 238-244
    • (1992) J Clin Invest , vol.90 , pp. 238-244
    • Koopman, J.1    Harverkate, F.2    Lord, S.T.3    Grimbergen, J.4    Mannucci, P.M.5
  • 28
    • 0035399185 scopus 로고    scopus 로고
    • Fibrinogen Naples I (Bβ A68T) nonsubstrate thrombin-binding capacities
    • Meh D.A., Mosesson M.W., et al. Fibrinogen Naples I (Bβ A68T) nonsubstrate thrombin-binding capacities. Thromb Res 103 (2001) 63-73
    • (2001) Thromb Res , vol.103 , pp. 63-73
    • Meh, D.A.1    Mosesson, M.W.2
  • 29
    • 0026507160 scopus 로고
    • Abnormal fibrinogens Ijmuiden (BβArg14→Cys) and Nijmegen (BβArg44→Cys) form disulfide-linked fibrinogen-albumin complexes
    • Koopman J., Harverkate F., and Grimbergen J. Abnormal fibrinogens Ijmuiden (BβArg14→Cys) and Nijmegen (BβArg44→Cys) form disulfide-linked fibrinogen-albumin complexes. Proc Natl Acad Sci 89 (1992) 3478-3482
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 3478-3482
    • Koopman, J.1    Harverkate, F.2    Grimbergen, J.3
  • 30
    • 0023766964 scopus 로고
    • Fibrinogen Nijmegen: congenital dysfibrinogenemia associated with impaired t-PA mediated plasminogen activation and decreased binding of t-PA
    • Engesse L., Koopman J., and de Munk G. Fibrinogen Nijmegen: congenital dysfibrinogenemia associated with impaired t-PA mediated plasminogen activation and decreased binding of t-PA. Thromb Haemost 60 (1988) 113-120
    • (1988) Thromb Haemost , vol.60 , pp. 113-120
    • Engesse, L.1    Koopman, J.2    de Munk, G.3
  • 31
    • 0032765219 scopus 로고    scopus 로고
    • Dysfibrinogenemia and thrombosis
    • Mosesson M.W. Dysfibrinogenemia and thrombosis. Sem Thrmb Hemost 25 (1999) 311-319
    • (1999) Sem Thrmb Hemost , vol.25 , pp. 311-319
    • Mosesson, M.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.