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Volumn 97, Issue 10, 1996, Pages 2342-2350

The relationship between the fibrinogen D domain self-association/cross-linking site (γXL) and the fibrinogen Dusart abnormality (Aα R554C-albumin): Clues to thrombophilia in the "Dusart syndrome"

Author keywords

Factor XIII; Fibrin; Fibrinogen; Plasminogen; Thrombophilia

Indexed keywords

BLOOD CLOTTING FACTOR 13; DEXTRAN; FIBRIN; FIBRINOGEN VARIANT; GLYCEROL; PLASMINOGEN;

EID: 0029885335     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118677     Document Type: Article
Times cited : (35)

References (46)
  • 2
    • 0028877613 scopus 로고
    • Familial Dysfibrinogenemia and Thrombophilia
    • Haverkate, F., and M. Samama. 1995. Familial Dysfibrinogenemia and Thrombophilia. Thromb. Haemost. 73:151-161.
    • (1995) Thromb. Haemost. , vol.73 , pp. 151-161
    • Haverkate, F.1    Samama, M.2
  • 4
    • 0020596374 scopus 로고
    • A new type of congenital dysfibrinogenaemia with defective fibrin lysis-Dusard syndrome: Possible relation to thrombosis
    • Soria, J., C. Soria, and J.P. Caen. 1983. A new type of congenital dysfibrinogenaemia with defective fibrin lysis-Dusard syndrome: possible relation to thrombosis. Br. J. Haematol. 53:575-586.
    • (1983) Br. J. Haematol. , vol.53 , pp. 575-586
    • Soria, J.1    Soria, C.2    Caen, J.P.3
  • 5
    • 0028051450 scopus 로고
    • A correlation between thrombotic disease and a specific fibrinogen abnormality (Aα 554 Arg → Cys) in two unrelated kindred, Dusart and Chapel Hill III
    • Wada, Y., and S.T. Lord. 1994. A correlation between thrombotic disease and a specific fibrinogen abnormality (Aα 554 Arg → Cys) in two unrelated kindred, Dusart and Chapel Hill III. Blood. 84: 3709-3714.
    • (1994) Blood , vol.84 , pp. 3709-3714
    • Wada, Y.1    Lord, S.T.2
  • 6
    • 0027476203 scopus 로고
    • The polymerization of fibrinogen Dusart (Aα 554 Arg → Cys) after removal of carboxy terminal regions of the Aα chains
    • Siebenlist, K.R., M.W. Mosesson, J.P. DiOrio, J. Soria, C. Soria, and J.P. Caen. 1993. The polymerization of fibrinogen Dusart (Aα 554 Arg → Cys) after removal of carboxy terminal regions of the Aα chains. Blood Coag. Fibrinol. 4:61-65.
    • (1993) Blood Coag. Fibrinol. , vol.4 , pp. 61-65
    • Siebenlist, K.R.1    Mosesson, M.W.2    DiOrio, J.P.3    Soria, J.4    Soria, C.5    Caen, J.P.6
  • 7
    • 0021341834 scopus 로고
    • Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation
    • Lijnen, H.R., J. Soria, C. Soria, D. Collen, and J.P. Caen. 1984. Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation. Thromb. Haemostasis. 51: 108-109.
    • (1984) Thromb. Haemostasis , vol.51 , pp. 108-109
    • Lijnen, H.R.1    Soria, J.2    Soria, C.3    Collen, D.4    Caen, J.P.5
  • 8
    • 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., J. Soria, M. Mirshahi, M. Hirsch, F.B. Dagonnet, J. Caen, and C. Soria. 1993. Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. J. Clin. Invest. 82:2462-2469.
    • (1993) J. Clin. Invest. , vol.82 , pp. 2462-2469
    • Collet, J.-P.1    Soria, J.2    Mirshahi, M.3    Hirsch, M.4    Dagonnet, F.B.5    Caen, J.6    Soria, C.7
  • 9
    • 0028809739 scopus 로고
    • The covalent structure of factor XIIIa-crosslinked fibrinogen fibrils
    • Mosesson, M.W., K.R. Siebenlist, J.F. Hainfeld, and J.S. Wall. 1995. The covalent structure of factor XIIIa-crosslinked fibrinogen fibrils. J. Struct. Biol. 115:88-101.
    • (1995) J. Struct. Biol. , vol.115 , pp. 88-101
    • Mosesson, M.W.1    Siebenlist, K.R.2    Hainfeld, J.F.3    Wall, J.S.4
  • 10
    • 0029111701 scopus 로고
    • The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ 275 Arg → Cys)
    • Mosesson, M.W., K.R. Siebenlist, J.P. DiOrio, M. Matsuda, J.F. Hainfeld, and J.S. Wall. 1995. The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ 275 Arg → Cys). J. Clin. Invest. 96:1053-1058.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1053-1058
    • Mosesson, M.W.1    Siebenlist, K.R.2    DiOrio, J.P.3    Matsuda, M.4    Hainfeld, J.F.5    Wall, J.S.6
  • 11
    • 0015799023 scopus 로고
    • Adsorption of plasmic fragment D to thrombin modified fibrinogen-sepharose
    • Kudryk, B., J. Reuterby, and B. Blombäck. 1973. Adsorption of plasmic fragment D to thrombin modified fibrinogen-sepharose. Thromb. Res. 2:297-304.
    • (1973) Thromb. Res. , vol.2 , pp. 297-304
    • Kudryk, B.1    Reuterby, J.2    Blombäck, B.3
  • 12
    • 0018129207 scopus 로고
    • A two-step fibrinogen-fibrin transition in blood coagulation
    • Blombäck, B., B. Hessel, D. Hogg, and L. Therkildsen. 1978. A two-step fibrinogen-fibrin transition in blood coagulation. Nature (Lond.). 275:501-505.
    • (1978) Nature (Lond.) , vol.275 , pp. 501-505
    • Blombäck, B.1    Hessel, B.2    Hogg, D.3    Therkildsen, L.4
  • 13
    • 0020645321 scopus 로고
    • Fibrin polymerization sites in fibrinogen and fibrin fragments
    • Budzynski, A.Z., S.A. Olexa, and B.V. Pandya. 1983. Fibrin polymerization sites in fibrinogen and fibrin fragments. Ann. NY Acad. Sci. 408:301-314.
    • (1983) Ann. NY Acad. Sci. , vol.408 , pp. 301-314
    • Budzynski, A.Z.1    Olexa, S.A.2    Pandya, B.V.3
  • 17
    • 0000649033 scopus 로고
    • Fibrinoligase. The fibrin stabilizing factor system
    • Lorand, L., and T. Gotoh. 1970. Fibrinoligase. The fibrin stabilizing factor system. Methods Enzymol. 19:770-782.
    • (1970) Methods Enzymol. , vol.19 , pp. 770-782
    • Lorand, L.1    Gotoh, T.2
  • 18
    • 0001408345 scopus 로고
    • The preparation and some properties of fibrinogen precipitated from human plasma by glycine
    • Kazal, L.A., S. Amsel, O.P. Miller, and L.M. Tocantins. 1963. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc. Soc. Exp. Biol. Med. 113:989-994.
    • (1963) Proc. Soc. Exp. Biol. Med. , vol.113 , pp. 989-994
    • Kazal, L.A.1    Amsel, S.2    Miller, O.P.3    Tocantins, L.M.4
  • 19
    • 0013947566 scopus 로고
    • The preparation and properties of human fibrinogen of relatively high solubility
    • Mosesson, M.W., and S. Sherry. 1966. The preparation and properties of human fibrinogen of relatively high solubility. Biochemistry. 5:2829-2835.
    • (1966) Biochemistry , vol.5 , pp. 2829-2835
    • Mosesson, M.W.1    Sherry, S.2
  • 20
    • 0000287082 scopus 로고
    • Subfractions of human fibrinogen. Preparation and analysis
    • Mosesson, M.W., and J.S. Finlayson. 1963. Subfractions of human fibrinogen. Preparation and analysis. J. Lab. Clin. Med. 62:663-674.
    • (1963) J. Lab. Clin. Med. , vol.62 , pp. 663-674
    • Mosesson, M.W.1    Finlayson, J.S.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0015748003 scopus 로고
    • The essential covalent structure of human fibrinogen evinced by analysis of derivatives formed during plasmic hydrolysis
    • Mosesson, M.W., J.S. Finlayson, and D.K. Galanakis. 1973. The essential covalent structure of human fibrinogen evinced by analysis of derivatives formed during plasmic hydrolysis. J. Biol. Chem. 248:7913-7929.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7913-7929
    • Mosesson, M.W.1    Finlayson, J.S.2    Galanakis, D.K.3
  • 23
    • 0015501514 scopus 로고
    • High molecular weight derivatives of human fibrinogen produced by plasmin
    • Marder, V.J., A.Z. Budzynski, and H.L. James. 1972. High molecular weight derivatives of human fibrinogen produced by plasmin. J. Biol. Chem. 244:4775-4781.
    • (1972) J. Biol. Chem. , vol.244 , pp. 4775-4781
    • Marder, V.J.1    Budzynski, A.Z.2    James, H.L.3
  • 25
    • 0015523610 scopus 로고
    • Heterogeneities of human fibrinogen. I. Structural and related studies of plasma fibrinogens which are high solubility catabolic intermediates
    • Mosesson, M.W., J.S. Finlayson, R.A. Umfleet, and D.K. Galanakis. 1972. Heterogeneities of human fibrinogen. I. Structural and related studies of plasma fibrinogens which are high solubility catabolic intermediates. J. Biol. Chem. 247:5210-5219.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5210-5219
    • Mosesson, M.W.1    Finlayson, J.S.2    Umfleet, R.A.3    Galanakis, D.K.4
  • 26
    • 0016207447 scopus 로고
    • Comparison of human plasma fibrinogen subfractions and early fibrinogen derivatives
    • Mosesson, M.W., D.K. Galanakis, and J.S. Finlayson. 1974. Comparison of human plasma fibrinogen subfractions and early fibrinogen derivatives. J. Biol. Chem. 249:4656-4664.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4656-4664
    • Mosesson, M.W.1    Galanakis, D.K.2    Finlayson, J.S.3
  • 27
    • 0021044029 scopus 로고
    • Human fibrinogen heterogeneities: Determination of the major Aα chain derivatives in blood
    • Galanakis, D.K., and M.W. Mosesson. 1983. Human fibrinogen heterogeneities: determination of the major Aα chain derivatives in blood. Thromb. Res. 31:403-413.
    • (1983) Thromb. Res. , vol.31 , pp. 403-413
    • Galanakis, D.K.1    Mosesson, M.W.2
  • 28
    • 0002102219 scopus 로고
    • Structure-function-evolution relationship in fibrinogen
    • A. Henschen, H. Graeff H, and F. Lottspeich, editors. W de Gruyter, Berlin
    • Henschen, A., F. Lottspeich, M. Kehl, C. Southan, and J. Lucas. 1982. Structure-function-evolution relationship in fibrinogen. In Fibrinogen. Recent Biochemical and Medical Aspects. A. Henschen, H. Graeff H, and F. Lottspeich, editors. W de Gruyter, Berlin. 67-82.
    • (1982) Fibrinogen. Recent Biochemical and Medical Aspects , pp. 67-82
    • Henschen, A.1    Lottspeich, F.2    Kehl, M.3    Southan, C.4    Lucas, J.5
  • 29
    • 0017615917 scopus 로고
    • Amino acid sequence studies on the α chain of human fibrinogen. Covalent structure of the α-chain portion of fragment D
    • Doolittle, R.F., K.G. Cassman, B.A. Cottrell, S.J. Friezner, and T. Takagi. 1977. Amino acid sequence studies on the α chain of human fibrinogen. Covalent structure of the α-chain portion of fragment D. Biochemistry. 16:1710-1715.
    • (1977) Biochemistry , vol.16 , pp. 1710-1715
    • Doolittle, R.F.1    Cassman, K.G.2    Cottrell, B.A.3    Friezner, S.J.4    Takagi, T.5
  • 30
    • 0028808075 scopus 로고
    • Orientation of the carboxy-terminal regions of fibrin γ chain dimers determined from the cross-linked products formed in mixtures of fibrin, fragment D, and factor XIIIa
    • Siebenlist, K.R., D.A. Meh, J.S. Wall, J.F. Hainfeld, and M.W. Mosesson. 1995. Orientation of the carboxy-terminal regions of fibrin γ chain dimers determined from the cross-linked products formed in mixtures of fibrin, fragment D, and factor XIIIa. Thromb. Haemostasis 74:1113-1119.
    • (1995) Thromb. Haemostasis , vol.74 , pp. 1113-1119
    • Siebenlist, K.R.1    Meh, D.A.2    Wall, J.S.3    Hainfeld, J.F.4    Mosesson, M.W.5
  • 31
    • 0026748589 scopus 로고
    • Characterization of the γ chain platelet binding site on fibrinogen fragment D
    • Kirschbaum, N.E., M.W. Mosesson, and D.L. Amrani. 1992. Characterization of the γ chain platelet binding site on fibrinogen fragment D. Blood. 79:2643-2648.
    • (1992) Blood , vol.79 , pp. 2643-2648
    • Kirschbaum, N.E.1    Mosesson, M.W.2    Amrani, D.L.3
  • 32
    • 0027379584 scopus 로고
    • Carboxyl-terminal portions of the a chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization
    • Veklich, Y.I., O.V. Gorkun, L.V. Medved, W. Nieuwenhuizen, and J.W. Weisel. 1993. Carboxyl-terminal portions of the a chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization. J. Biol. Chem. 268:13577-13585.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13577-13585
    • Veklich, Y.I.1    Gorkun, O.V.2    Medved, L.V.3    Nieuwenhuizen, W.4    Weisel, J.W.5
  • 33
    • 0016759666 scopus 로고
    • Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa)
    • Kanaide, H., and J.R. Shainoff. 1975. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa). J. Lab. Clin. Med. 85:574-597.
    • (1975) J. Lab. Clin. Med. , vol.85 , pp. 574-597
    • Kanaide, H.1    Shainoff, J.R.2
  • 34
    • 0017069460 scopus 로고
    • Effects of dextran on the molecular structure and tensile behavior of human fibrin
    • Dhall, T.Z., W.A.J. Bryce, and D.P. Dhall. 1976. Effects of dextran on the molecular structure and tensile behavior of human fibrin. Thromb. Haemost. 35:737-745.
    • (1976) Thromb. Haemost. , vol.35 , pp. 737-745
    • Dhall, T.Z.1    Bryce, W.A.J.2    Dhall, D.P.3
  • 35
    • 0001204684 scopus 로고
    • Dextran-induced changes in fibrin fiber size and density based on wavelength dependence of gel turbidity
    • Carr, ME., and D.A. Gabriel. 1980. Dextran-induced changes in fibrin fiber size and density based on wavelength dependence of gel turbidity. Macromolecules. 13:1473-1477.
    • (1980) Macromolecules , vol.13 , pp. 1473-1477
    • Carr, M.E.1    Gabriel, D.A.2
  • 36
    • 0019199058 scopus 로고
    • The effect of dextran 70 on the structure of plasma-derived fibrin gels
    • Carr, M.E., and D.A. Gabriel. 1980. The effect of dextran 70 on the structure of plasma-derived fibrin gels. J. Lab. Clin. Med. 96: 985-993.
    • (1980) J. Lab. Clin. Med. , vol.96 , pp. 985-993
    • Carr, M.E.1    Gabriel, D.A.2
  • 37
    • 33947443359 scopus 로고
    • Preparation and properties of serum and plasma proteins. VIII. The conversion of human fibrinogen to fibrin under various conditions
    • Ferry, J.D., and P.R. Morrison. 1947. Preparation and properties of serum and plasma proteins. VIII. The conversion of human fibrinogen to fibrin under various conditions. J. Am. Chem. Soc. 69: 388-400.
    • (1947) J. Am. Chem. Soc. , vol.69 , pp. 388-400
    • Ferry, J.D.1    Morrison, P.R.2
  • 38
    • 3142634462 scopus 로고
    • The conversion of fibrinogen to fibrin. XI. Light scattering studies on clotting systems inhibited by hexamethylene glycol
    • Ferry, J.D., S. Shulman, K. Gutfreund, and S. Katz. 1952. The conversion of fibrinogen to fibrin. XI. Light scattering studies on clotting systems inhibited by hexamethylene glycol. J. Amer. Chem. Soc. 74:5709-5715.
    • (1952) J. Amer. Chem. Soc. , vol.74 , pp. 5709-5715
    • Ferry, J.D.1    Shulman, S.2    Gutfreund, K.3    Katz, S.4
  • 39
    • 0014143974 scopus 로고
    • Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility
    • Mosesson, M.W., N. Alkjaersig, B. Sweet, and S. Sherry. 1967. Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility. Biochemistry. 6:3279-3287.
    • (1967) Biochemistry , vol.6 , pp. 3279-3287
    • Mosesson, M.W.1    Alkjaersig, N.2    Sweet, B.3    Sherry, S.4
  • 40
    • 0025136902 scopus 로고
    • Location of the binding site "b" for lateral polymerization of fibrin
    • Hasegawa, N., and S. Sasaki. 1990. Location of the binding site "b" for lateral polymerization of fibrin. Thromb. Res. 57:183-195.
    • (1990) Thromb. Res. , vol.57 , pp. 183-195
    • Hasegawa, N.1    Sasaki, S.2
  • 42
    • 0019779251 scopus 로고
    • Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy
    • Mosesson, M.W., J.F. Hainfeld, R.H. Haschemeyer, and J.S. Wall. 1981. Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy. J. Mol. Biol. 153:695-718.
    • (1981) J. Mol. Biol. , vol.153 , pp. 695-718
    • Mosesson, M.W.1    Hainfeld, J.F.2    Haschemeyer, R.H.3    Wall, J.S.4
  • 43
    • 0004782883 scopus 로고
    • Identification of covalently linked trimeric and tetrameric D domains in cross-linked fibrin
    • Mosesson, M.W., K.R. Siebenlist, D.L. Amrani, and J.P. DiOrio. 1989. Identification of covalently linked trimeric and tetrameric D domains in cross-linked fibrin. Proc. Natl. Acad. Sci. USA. 86:1113-1117.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1113-1117
    • Mosesson, M.W.1    Siebenlist, K.R.2    Amrani, D.L.3    Diorio, J.P.4
  • 44
    • 0027247825 scopus 로고
    • Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular branch junction
    • Mosesson, M.W., J.P. DiOrio, K.R. Siebenlist, J.S. Wall, and J.F. Hainfeld. 1993. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular branch junction. Blood. 82:1517-1521.
    • (1993) Blood , vol.82 , pp. 1517-1521
    • Mosesson, M.W.1    DiOrio, J.P.2    Siebenlist, K.R.3    Wall, J.S.4    Hainfeld, J.F.5
  • 45
    • 0026491075 scopus 로고
    • The effect of fibrin structure on fibrinolysis
    • Gabriel, D.A., K. Muga, and E.M. Boothroyd. 1992. The effect of fibrin structure on fibrinolysis. J. Biol. Chem. 267:24259-24263.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24259-24263
    • Gabriel, D.A.1    Muga, K.2    Boothroyd, E.M.3
  • 46
    • 0029100827 scopus 로고
    • Effect of fibrin structure on plasmin-mediated dissolution of plasma clots
    • Carr, M.E., Jr., and B.M. Alving. 1995. Effect of fibrin structure on plasmin-mediated dissolution of plasma clots. Blood Coag. Fibrinol. 6:567-573.
    • (1995) Blood Coag. Fibrinol. , vol.6 , pp. 567-573
    • Carr Jr., M.E.1    Alving, B.M.2


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