메뉴 건너뛰기




Volumn 50, Issue 42, 2011, Pages 9066-9075

Substitution of the human αc region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: Fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCES; HYDRODYNAMIC RADIUS; MIXED POLYMERS; PROTOFIBRILS; THIN FIBERS;

EID: 80054991411     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201094v     Document Type: Article
Times cited : (31)

References (29)
  • 2
    • 59049099881 scopus 로고    scopus 로고
    • Recommendations for nomenclature on fibrinogen and fibrin
    • Medved, L. and Weisel, J. W. (2009) Recommendations for nomenclature on fibrinogen and fibrin J. Thromb. Haemostasis 7, 355-359
    • (2009) J. Thromb. Haemostasis , vol.7 , pp. 355-359
    • Medved, L.1    Weisel, J.W.2
  • 3
  • 4
    • 0021110096 scopus 로고
    • Structural organization of C-terminal parts of fibrinogen A alpha-chains
    • Medved, L. V., Gorkun, O. V., and Privalov, P. L. (1983) Structural organization of C-terminal parts of fibrinogen A alpha-chains FEBS Lett. 160, 291-295
    • (1983) FEBS Lett. , vol.160 , pp. 291-295
    • Medved, L.V.1    Gorkun, O.V.2    Privalov, P.L.3
  • 6
    • 34547753415 scopus 로고    scopus 로고
    • Direct evidence for specific interactions of the fibrinogen αC-domains with the central E region and with each other
    • DOI 10.1021/bi700944j
    • Litvinov, R. I., Yakovlev, S., Tsurupa, G., Gorkun, O. V., Medved, L., and Weisel, J. W. (2007) Direct Evidence for Specific Interactions of the Fibrinogen αC-Domains with the Central E Region and with Each Other Biochemistry 46, 9133-9142 (Pubitemid 47237388)
    • (2007) Biochemistry , vol.46 , Issue.31 , pp. 9133-9142
    • Litvinov, R.I.1    Yakovlev, S.2    Tsurupa, G.3    Gorkun, O.V.4    Medved, L.5    Weisel, J.W.6
  • 8
    • 0030725658 scopus 로고    scopus 로고
    • Severely impaired polymerization of recombinant fibrinogen γ-364 Asp → His, the substitution discovered in a heterozygous individual
    • DOI 10.1074/jbc.272.47.29596
    • Okumura, N., Gorkun, O. V., and Lord, S. T. (1997) Severely impaired polymerization of recombinant fibrinogen gamma-364 Asp - > His, the substitution discovered in a heterozygous individual J. Biol. Chem. 272, 29596-29601 (Pubitemid 27508049)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.47 , pp. 29596-29601
    • Okumura, N.1    Gorkun, O.V.2    Lord, S.T.3
  • 9
    • 66149110352 scopus 로고    scopus 로고
    • Fibrinogen variant BbetaD432A has normal polymerization but does not bind knob "b"
    • Bowley, S. R. and Lord, S. T. (2009) Fibrinogen variant BbetaD432A has normal polymerization but does not bind knob "B" Blood 113, 4425-4430
    • (2009) Blood , vol.113 , pp. 4425-4430
    • Bowley, S.R.1    Lord, S.T.2
  • 10
    • 0032480786 scopus 로고    scopus 로고
    • Analysis of Aα251 fibrinogen: The αC domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X
    • DOI 10.1021/bi981551t
    • Gorkun, O. V., Henschen-Edman, A. H., Ping, L. F., and Lord, S. T. (1998) Analysis of Aa251 fibrinogen: The αC domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X Biochemistry 37, 15434-15441 (Pubitemid 28516005)
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15434-15441
    • Gorkun, O.V.1    Henschen-Edman, A.H.2    Ping, L.F.3    Lord, S.T.4
  • 11
    • 28444478753 scopus 로고    scopus 로고
    • The αC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis
    • DOI 10.1182/blood-2005-05-2150
    • Collet, J. P., Moen, J. L., Veklich, Y. I., Gorkun, O. V., Lord, S. T., Montalescot, G., and Weisel, J. W. (2005) The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis Blood 106, 3824-3830 (Pubitemid 41739019)
    • (2005) Blood , vol.106 , Issue.12 , pp. 3824-3830
    • Collet, J.-P.1    Moen, J.L.2    Veklich, Y.I.3    Gorkun, O.V.4    Lord, S.T.5    Montalescot, G.6    Weisel, J.W.7
  • 12
    • 0025280399 scopus 로고
    • Bipartite mRNA for chicken alpha-fibrinogen potentially encodes an amino acid sequence homologous to beta- and gamma-fibrinogens
    • Weissbach, L. and Grieninger, G. (1990) Bipartite mRNA for chicken alpha-fibrinogen potentially encodes an amino acid sequence homologous to beta- and gamma-fibrinogens Proc. Natl. Acad. Sci. U. S. A. 87, 5198-5202
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 5198-5202
    • Weissbach, L.1    Grieninger, G.2
  • 13
    • 0035940439 scopus 로고    scopus 로고
    • Crystal structure of native chicken fibrinogen at 2.7 A resolution
    • DOI 10.1021/bi011394p
    • Yang, Z., Kollman, J. M., Pandi, L., and Doolittle, R. F. (2001) Crystal structure of native chicken fibrinogen at 2.7 A resolution Biochemistry 40, 12515-12523 (Pubitemid 32979704)
    • (2001) Biochemistry , vol.40 , Issue.42 , pp. 12515-12523
    • Zhe, Y.1    Kollman, J.M.2    Pandi, L.3    Doolittle, R.F.4
  • 14
    • 72949124019 scopus 로고    scopus 로고
    • Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X
    • Cardinali, B., Profumo, A., Aprile, A., Byron, O., Morris, G., Harding, S. E., Stafford, W. F., and Rocco, M. (2010) Hydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X Arch. Biochem. Biophys. 493, 157-168
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 157-168
    • Cardinali, B.1    Profumo, A.2    Aprile, A.3    Byron, O.4    Morris, G.5    Harding, S.E.6    Stafford, W.F.7    Rocco, M.8
  • 15
    • 0021995951 scopus 로고
    • A monoclonal antibody, specific for human fibrinogen, fibrinopeptide A-containing fragments and not reacting with free fibrinopeptide A
    • Koppert, P. W., Huijsmans, C. M., and Nieuwenhuizen, W. (1985) A monoclonal antibody, specific for human fibrinogen, fibrinopeptide A-containing fragments and not reacting with free fibrinopeptide A Blood 66, 503-507 (Pubitemid 15230750)
    • (1985) Blood , vol.66 , Issue.3 , pp. 503-507
    • Koppert, P.W.1    Huijsmans, C.M.G.2    Nieuwenhuizen, W.3
  • 16
    • 0026729988 scopus 로고
    • Immunoelectrophoretic and immunohistochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas
    • Valenzuela, R., Shainoff, J. R., DiBello, P. M., Urbanic, D. A., Anderson, J. M., Matsueda, G. R., and Kudryk, B. J. (1992) Immunoelectrophoretic and immunohistochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas Am. J. Pathol. 141, 861-880
    • (1992) Am. J. Pathol. , vol.141 , pp. 861-880
    • Valenzuela, R.1    Shainoff, J.R.2    Dibello, P.M.3    Urbanic, D.A.4    Anderson, J.M.5    Matsueda, G.R.6    Kudryk, B.J.7
  • 18
    • 0027505548 scopus 로고
    • Characterization of purified recombinant fibrinogen: Partial phosphorylation of fibrinopeptide A
    • DOI 10.1021/bi00052a015
    • Binnie, C. G., Hettasch, J. M., Strickland, E., and Lord, S. T. (1993) Characterization of purified recombinant fibrinogen: partial phosphorylation of fibrinopeptide A Biochemistry 32, 107-113 (Pubitemid 23033326)
    • (1993) Biochemistry , vol.32 , Issue.1 , pp. 107-113
    • Binnie, C.G.1    Hettasch, J.M.2    Strickland, E.3    Lord, S.T.4
  • 19
    • 0030998485 scopus 로고    scopus 로고
    • The conversion of fibrinogen to fibrin: Recombinant fibrinogen typifies plasma fibrinogen
    • Gorkun, O. V., Veklich, Y. I., Weisel, J. W., and Lord, S. T. (1997) The conversion of fibrinogen to fibrin: recombinant fibrinogen typifies plasma fibrinogen Blood 89, 4407-4414 (Pubitemid 27260251)
    • (1997) Blood , vol.89 , Issue.12 , pp. 4407-4414
    • Gorkun, O.V.1    Veklich, Y.I.2    Weisel, J.W.3    Lord, S.T.4
  • 20
    • 0030048726 scopus 로고    scopus 로고
    • Strategy for recombinant multichain protein synthesis: Fibrinogen B beta-chain variants as thrombin substrates
    • Lord, S. T., Strickland, E., and Jayjock, E. (1996) Strategy for recombinant multichain protein synthesis: fibrinogen B beta-chain variants as thrombin substrates Biochemistry 35, 2342-2348
    • (1996) Biochemistry , vol.35 , pp. 2342-2348
    • Lord, S.T.1    Strickland, E.2    Jayjock, E.3
  • 21
    • 0034682822 scopus 로고    scopus 로고
    • Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release
    • Mullin, J. L., Gorkun, O. V., Binnie, C. G., and Lord, S. T. (2000) Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release J. Biol. Chem. 275, 25239-25246
    • (2000) J. Biol. Chem. , vol.275 , pp. 25239-25246
    • Mullin, J.L.1    Gorkun, O.V.2    Binnie, C.G.3    Lord, S.T.4
  • 22
    • 0034664089 scopus 로고    scopus 로고
    • Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism
    • DOI 10.1021/bi000045c
    • Mullin, J. L., Gorkun, O. V., and Lord, S. T. (2000) Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism Biochemistry 39, 9843-9849 (Pubitemid 30626832)
    • (2000) Biochemistry , vol.39 , Issue.32 , pp. 9843-9849
    • Mullin, J.L.1    Gorkun, O.V.2    Lord, S.T.3
  • 23
    • 0037161292 scopus 로고    scopus 로고
    • Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that "B-b" interactions have a role in protofibril formation
    • DOI 10.1021/bi011988s
    • Lounes, K. C., Ping, L., Gorkun, O. V., and Lord, S. T. (2002) Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that "B-b" interactions have a role in protofibril formation Biochemistry 41, 5291-5299 (Pubitemid 34411685)
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5291-5299
    • Lounes, K.C.1    Ping, L.2    Gorkun, O.V.3    Lord, S.T.4
  • 24
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 25
    • 0022354752 scopus 로고
    • Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin
    • Lewis, S. D., Shields, P. P., and Shafer, J. A. (1985) Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin J. Biol. Chem. 260, 10192-10199 (Pubitemid 16246553)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.18 , pp. 10192-10199
    • Lewis, S.D.1    Shields, P.P.2    Shafer, J.A.3
  • 26
    • 10044290943 scopus 로고    scopus 로고
    • The hydrodynamic radii of macromolecules and their effect on red blood cell aggregation
    • DOI 10.1529/biophysj.104.047746
    • Armstrong, J. K., Wenby, R. B., Meiselman, H. J., and Fisher, T. C. (2004) The hydrodynamic radii of macromolecules and their effect on red blood cell aggregation Biophys. J. 87, 4259-4270 (Pubitemid 39602928)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 4259-4270
    • Armstrong, J.K.1    Wenby, R.B.2    Meiselman, H.J.3    Fisher, T.C.4
  • 27
    • 0026771894 scopus 로고
    • Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled
    • Weisel, J. W. and Nagaswami, C. (1992) Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled Biophys. J. 63, 111-128
    • (1992) Biophys. J. , vol.63 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 29
    • 0027379584 scopus 로고
    • Carboxyl-terminal portions of the α chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization
    • Veklich, Y. I., Gorkun, O. V., Medved, L. V., Nieuwenhuizen, W., and Weisel, J. W. (1993) Carboxyl-terminal portions of the alpha chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated alpha C fragments on polymerization J. Biol. Chem. 268, 13577-13585 (Pubitemid 23307788)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.18 , pp. 13577-13585
    • Veklich, Y.I.1    Gorkun, O.V.2    Medved, L.V.3    Nieuwenhuizen, W.4    Weisel, J.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.