메뉴 건너뛰기




Volumn 48, Issue 30, 2009, Pages 7201-7208

Two families of synthetic peptides that enhance fibrin turbidity and delay fibrinolysis by different mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

C-DOMAIN; CLOT TURBIDITY; DIFFERENT MECHANISMS; FIBRIN CLOTS; IN-VITRO; PENTAPEPTIDES; POSITIVELY CHARGED PEPTIDES; SYNTHETIC PEPTIDE;

EID: 70350722262     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi900647g     Document Type: Article
Times cited : (15)

References (36)
  • 2
    • 33644513725 scopus 로고    scopus 로고
    • Binding of synthetic B knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin
    • Doolittle, R. F., and Pandi, L. (2006) Binding of synthetic B knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin. Biochemistry 45, 2657-2667.
    • (2006) Biochemistry , vol.45 , pp. 2657-2667
    • Doolittle, R.F.1    Pandi, L.2
  • 3
    • 34548490739 scopus 로고    scopus 로고
    • Probing the β-chain hole of fibrinogen with synthetic peptides that differ at their amino termini
    • DOI 10.1021/bi7010916
    • Doolittle, R. F., and Pandi, L. (2007) Probing the β-chain holes of fibrinogen with synthetic peptides that differ at their amino termini. Biochemistry 46, 10033-10038. (Pubitemid 47378594)
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 10033-10038
    • Doolittle, R.F.1    Pandi, L.2
  • 5
    • 48249103964 scopus 로고    scopus 로고
    • Searching for Differences between Fibrinogen and Fibrin That Affect the Initiation of Fibrinolysis
    • Doolittle, R. F. (2008) Searching for Differences Between Fibrinogen and Fibrin That Affect the Initiation of Fibrinolysis. Cardiovasc. Hematol. Agents Med. Chem. 6, 181-189.
    • (2008) Cardiovasc. Hematol. Agents Med. Chem. , vol.6 , pp. 181-189
    • Doolittle, R.F.1
  • 8
    • 1542746446 scopus 로고    scopus 로고
    • Fibrinogen C-terminal peptidic sequences (Haptides) modulate fibrin polymerization
    • Marx, G., Ben-Moshe, M., Magdassi, S., and Gorodetsky, R. (2004) Fibrinogen C-terminal peptide sequences (Haptides) modulate fibrin polymerization. Thromb. Haemostasis 91, 43-51. (Pubitemid 38111219)
    • (2004) Thrombosis and Haemostasis , vol.91 , Issue.1 , pp. 43-51
    • Marx, G.1    Ben-Moshe, M.2    Magdassi, S.3    Gorodetsky, R.4
  • 10
    • 0014057783 scopus 로고
    • Amino acid sequence studies on artiodactyls fibrinopeptides. I. Dromedary camel, mule deer and Cape Buffalo
    • Doolittle, R. F., Schubert, D., and Schwartz, S. A. (1967) Amino acid sequence studies on artiodactyls fibrinopeptides. I. Dromedary camel, mule deer and Cape Buffalo. Arch. Biochem. Biophys. 118, 456-467.
    • (1967) Arch. Biochem. Biophys. , vol.118 , pp. 456-467
    • Doolittle, R.F.1    Schubert, D.2    Schwartz, S.A.3
  • 11
    • 0002039318 scopus 로고
    • Heterogeneity of human fibrinogen
    • Finlayson, J. S., and Mosesson, M. W. (1963) Heterogeneity of human fibrinogen. Biochemistry 2, 42-46.
    • (1963) Biochemistry , vol.2 , pp. 42-46
    • Finlayson, J.S.1    Mosesson, M.W.2
  • 12
    • 0015523610 scopus 로고
    • Human fibrinogen heterogeneities. I. Structural and related studies of plasma fibrinogens which are high solubility catabolic intermediates
    • Mosesson, M. W., Finlayson, J. S., Umfleet, R. A., and Galanakis, D. (1972) Human fibrinogen heterogeneities. 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.4
  • 13
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • DOI 10.1038/38947
    • Spraggon, G., Everse, S. J., and Doolittle, R. F. (1997) Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 389, 455-462. (Pubitemid 27435313)
    • (1997) Nature , vol.389 , Issue.6650 , pp. 455-462
    • Spraggon, G.1    Everse, S.J.2    Doollttle, R.F.3
  • 14
    • 0014932863 scopus 로고
    • Plasminogen: Purification from human plasma by affinity chromatography
    • Deutsch, D. G., and Mertz, E. T. (1970) Plasminogen: Purification from human plasma by affinity chromatography. Science 170, 1095-1096.
    • (1970) Science , vol.170 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2
  • 15
    • 0017910967 scopus 로고
    • Size and density of fibrin fibers from turbidity
    • Carr, M. E., and Herman, J. (1978) Size and density of fibrin fibers from turbidity. Macromolecules 11, 46-50.
    • (1978) Macromolecules , vol.11 , pp. 46-50
    • Carr, M.E.1    Herman, J.2
  • 16
    • 0018180318 scopus 로고
    • The wavelength dependence of the turbidity of solutions of macromolecules
    • Camerini-Otero, R. D., and Day, L. A. (1978) The wavelength dependence of turbidity of solutions of macromolecules. Biopolymers 17, 2241-2249. (Pubitemid 9015233)
    • (1978) Biopolymers , vol.17 , Issue.9 , pp. 2241-2249
    • Camerini-Otero, R.D.1    Day, L.A.2
  • 17
    • 0001204684 scopus 로고
    • Dextran-induced changes in fibrin fiber size and density based on wavelength dependence of gel turbidity
    • Carr, M. E., and Gabriel, D. A. (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
  • 18
    • 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
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AmoRe
    • Navaza, J. (2001) Implementation of molecular replacement in AmoRe. Acta Crystallogr. D57, 1367-1372.
    • (2001) Acta Crystallogr. , vol.D57 , pp. 1367-1372
    • Navaza, J.1
  • 21
    • 0028103275 scopus 로고
    • CollaborativeComputational Project Number 4
    • CollaborativeComputational Project Number 4 (1994) . Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building proteins in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building proteins in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0016770029 scopus 로고
    • Plasminogen-plasmin system IX. Specific binding of tranexamic acid to plasmin
    • Iwamoto, M. (1975) Plasminogen-plasmin system IX. Specific binding of tranexamic acid to plasmin. Thromb. Diath. Haemorrh. 33, 573-585.
    • (1975) Thromb. Diath. Haemorrh. , vol.33 , pp. 573-585
    • Iwamoto, M.1
  • 28
    • 0018800309 scopus 로고
    • The binding of tranexamic acid to native (Glu) and modified (Lys) human plasminogen and its effect on conformation
    • Markus, G., Priore, R. L., and Wissler, F. C. (1979) The binding of tranexamic acid to native (Glu) and modified (Lys) human plasminogen and its effect on conformation. J. Biol. Chem. 254, 1211-1216.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1211-1216
    • Markus, G.1    Priore, R.L.2    Wissler, F.C.3
  • 29
    • 0033537698 scopus 로고    scopus 로고
    • Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide
    • Everse, S. J., Spraggon, G., Veerapandian, L., and Doolittle, R. F. (1999) Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry 38, 2941-2946.
    • (1999) Biochemistry , vol.38 , pp. 2941-2946
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Doolittle, R.F.4
  • 30
    • 33947443359 scopus 로고
    • The conversion of human fibrinogen to fibrin under various conditions
    • Ferry, J. D., and Morrison, P. R. (1947) 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
  • 31
    • 0026491075 scopus 로고
    • The effect of fibrin structure on fibrinolysis
    • Gabriel, D. A., Muga, K., and Boothroyd, E. M. (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
  • 32
    • 0029100827 scopus 로고
    • Effect of fibrin structure on plasmin-mediated dissolution of plasma clots
    • Carr, M., and Alving, B. M. (1995) Effect of fibrin structure on plasmin-mediated dissolution of plasma clots. Blood Coagulation Fibrinolysis 6, 567-573.
    • (1995) Blood Coagulation Fibrinolysis , vol.6 , pp. 567-573
    • Carr, M.1    Alving, B.M.2
  • 33
    • 34250172106 scopus 로고    scopus 로고
    • The relative kinetics of clotting and lysis provide a biochemical rationale for the correlation between elevated fibrinogen and cardiovascular disease
    • DOI 10.1111/j.1538-7836.2007.02426.x
    • Kim, P. Y., Stewart, R. J., Lipson, S. M., and Nesheim, M. E. (2007) The relative kinetics of clotting and lysis provide a biochemical rationale for the correlation between elevated fibrinogen and cardiovascular disease. J. Thromb. Haemostasis 5, 1250-1256. (Pubitemid 46902128)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.6 , pp. 1250-1256
    • Kim, P.Y.1    Stewart, R.J.2    Lipson, S.M.3    Nesheim, M.E.4
  • 34
    • 0038353228 scopus 로고    scopus 로고
    • Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots
    • DOI 10.1074/jbc.M212734200
    • Collet, J.-P., Lesty, C., Montalescot, G., and Weisel, J. W. (2003) Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots. J. Biol. Chem. 278, 21331-21335. (Pubitemid 36792527)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21331-21335
    • Collet, J.-P.1    Lesty, C.2    Montalescot, G.3    Weisel, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.