메뉴 건너뛰기




Volumn 412, Issue 3, 2008, Pages 545-551

Characterization of an ideal amphipathic peptide as a procoagulant agent

Author keywords

Coagulation; Fibrinolysis; Haemostatic peptide; Ideal amphipathic peptide (IAP); Prothrombinase; Tenase

Indexed keywords

BIOCHEMISTRY;

EID: 45349107140     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071448     Document Type: Article
Times cited : (9)

References (31)
  • 1
    • 0141707881 scopus 로고    scopus 로고
    • Thrombin formation
    • Mann, K. G. (2003) Thrombin formation. Chest 124, 4S-10S
    • (2003) Chest , vol.124
    • Mann, K.G.1
  • 2
    • 2942517677 scopus 로고    scopus 로고
    • Role of tissue factor in hemostasis, thrombosis, and vascular development
    • Mackman, N. (2004) Role of tissue factor in hemostasis, thrombosis, and vascular development. Arterioscler. Thromb. Vasc. Biol. 24, 1015-1022
    • (2004) Arterioscler. Thromb. Vasc. Biol , vol.24 , pp. 1015-1022
    • Mackman, N.1
  • 3
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie, B. and Furie, B. C. (1988) The molecular basis of blood coagulation. Cell 53, 505-518
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 5
    • 0021322174 scopus 로고
    • Comparison of coagulation factor Xa and des-(1-44)factor Xa in the assembly of prothrombinase
    • Skogen, W. F., Esmon, C. T. and Cox, A. C. (1984) Comparison of coagulation factor Xa and des-(1-44)factor Xa in the assembly of prothrombinase. J. Biol. Chem. 259, 2306-2310
    • (1984) J. Biol. Chem , vol.259 , pp. 2306-2310
    • Skogen, W.F.1    Esmon, C.T.2    Cox, A.C.3
  • 6
    • 0027358796 scopus 로고
    • The importance of specific γ-carboxyglutamic acid residues in prothrombin: Evaluation by site-specific mutagenesis
    • Ratcliffe, J. V., Furie, B. and Furie, B. C. (1993) The importance of specific γ-carboxyglutamic acid residues in prothrombin: evaluation by site-specific mutagenesis. J. Biol. Chem. 268, 24339-24345
    • (1993) J. Biol. Chem , vol.268 , pp. 24339-24345
    • Ratcliffe, J.V.1    Furie, B.2    Furie, B.C.3
  • 7
    • 0025317472 scopus 로고
    • Kinetics of coagulation factor X activation by platelet-bound factor IXa
    • Rawala-Sheikh, R., Ahmad, S. S., Ashby, B. and Walsh, P. N. (1990) Kinetics of coagulation factor X activation by platelet-bound factor IXa. Biochemistry 29, 2606-2611
    • (1990) Biochemistry , vol.29 , pp. 2606-2611
    • Rawala-Sheikh, R.1    Ahmad, S.S.2    Ashby, B.3    Walsh, P.N.4
  • 8
    • 0019831499 scopus 로고
    • The role of phospholipid and factor VIIIa in the activation of bovine factor X
    • van Dieijen, G., Tans, G., Rosing, J. and Hemker, H. C. (1981) The role of phospholipid and factor VIIIa in the activation of bovine factor X. J. Biol. Chem. 256, 3433-3442
    • (1981) J. Biol. Chem , vol.256 , pp. 3433-3442
    • van Dieijen, G.1    Tans, G.2    Rosing, J.3    Hemker, H.C.4
  • 9
    • 0021915109 scopus 로고
    • The kinetics of activation of normal and γ-carboxyglutamic acid-deficient prothrombins
    • Malhotra, O. P., Nesheim, M. E. and Mann, K. G. (1985) The kinetics of activation of normal and γ-carboxyglutamic acid-deficient prothrombins. J. Biol. Chem. 260, 279-287
    • (1985) J. Biol. Chem , vol.260 , pp. 279-287
    • Malhotra, O.P.1    Nesheim, M.E.2    Mann, K.G.3
  • 10
    • 0016328156 scopus 로고
    • A plausible mechanism for prothrombin activation by factor Xa, factor Va, phospholipid, and calcium ions
    • Esmon, C. T., Owen, W. G. and Jackson, C. M. (1974) A plausible mechanism for prothrombin activation by factor Xa, factor Va, phospholipid, and calcium ions. J. Biol. Chem. 249, 8045-8047
    • (1974) J. Biol. Chem , vol.249 , pp. 8045-8047
    • Esmon, C.T.1    Owen, W.G.2    Jackson, C.M.3
  • 11
    • 0034601828 scopus 로고    scopus 로고
    • Amphipathic helices support function of blood coagulation factor IXa
    • Blostein, M. D., Rigby, A. C., Furie, B. C., Furie, B. and Gilbert, G. E. (2000) Amphipathic helices support function of blood coagulation factor IXa. Biochemistry 39, 12000-12006
    • (2000) Biochemistry , vol.39 , pp. 12000-12006
    • Blostein, M.D.1    Rigby, A.C.2    Furie, B.C.3    Furie, B.4    Gilbert, G.E.5
  • 12
    • 0028177259 scopus 로고
    • The amphipathic α-helix concept: Application to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin
    • Cornut, I., Buttner, K., Dasseux, J. L. and Dufourcg, J. (1994) The amphipathic α-helix concept: application to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin. FEBS Lett. 349, 29-33
    • (1994) FEBS Lett , vol.349 , pp. 29-33
    • Cornut, I.1    Buttner, K.2    Dasseux, J.L.3    Dufourcg, J.4
  • 13
    • 0032722442 scopus 로고    scopus 로고
    • The plasminogen (fibrinolytic) system
    • Collen, D. (1999) The plasminogen (fibrinolytic) system. Thromb. Haemostasis 82, 259-270
    • (1999) Thromb. Haemostasis , vol.82 , pp. 259-270
    • Collen, D.1
  • 14
    • 4444287581 scopus 로고
    • Nossel, H. L. and Vogel, H. J, eds, Academic Press, New York
    • Nossel, H. L. and Vogel, H. J. (eds) (1982) Pathobiology of the Endothelial Cell, Academic Press, New York
    • (1982) Pathobiology of the Endothelial Cell
  • 15
    • 0032560732 scopus 로고    scopus 로고
    • Hemostatic drugs
    • Mannucci, P. M. (1998) Hemostatic drugs. N. Engl. J. Med. 339, 245-253
    • (1998) N. Engl. J. Med , vol.339 , pp. 245-253
    • Mannucci, P.M.1
  • 17
    • 33645547820 scopus 로고    scopus 로고
    • Incorporation of fragment X into fibrin clots renders them more susceptible to lysis by plasmin
    • Schaefer, A. V., Leslie, B. A., Rischke, J. A., Stafford, A. R., Fredenburgh, J. C. and Weitz, J. I. (2006) Incorporation of fragment X into fibrin clots renders them more susceptible to lysis by plasmin. Biochemistry 45, 4257-4265
    • (2006) Biochemistry , vol.45 , pp. 4257-4265
    • Schaefer, A.V.1    Leslie, B.A.2    Rischke, J.A.3    Stafford, A.R.4    Fredenburgh, J.C.5    Weitz, J.I.6
  • 21
    • 0017071357 scopus 로고
    • Effect of polylysine on the activation of prothrombin: Polylysine substitutes for calcium ions and factor V in the factor Xa catalyzed activation of prothrombin
    • Vogel, C. N., Butkowski, R. J., Mann, K. G. and Lundblad, R. L. (1976) Effect of polylysine on the activation of prothrombin: polylysine substitutes for calcium ions and factor V in the factor Xa catalyzed activation of prothrombin. Biochemistry 15, 3265-3269
    • (1976) Biochemistry , vol.15 , pp. 3265-3269
    • Vogel, C.N.1    Butkowski, R.J.2    Mann, K.G.3    Lundblad, R.L.4
  • 22
    • 0020084791 scopus 로고
    • The acceleration by polylysine of the activation of factor X by factor IXa
    • Lundblad, R. L. and Roberts, H. R. (1982) The acceleration by polylysine of the activation of factor X by factor IXa. Thromb. Res. 25, 319-329
    • (1982) Thromb. Res , vol.25 , pp. 319-329
    • Lundblad, R.L.1    Roberts, H.R.2
  • 23
    • 0038192455 scopus 로고    scopus 로고
    • The antibiotic activity of cationic linear amphipathic peptides: Lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes
    • Beven, L., Castano, S., Dufourcq, J., Wieslander, A. and Wroblewski, H. (2003) The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes. Eur. J. Biochem. 270, 2207-2217
    • (2003) Eur. J. Biochem , vol.270 , pp. 2207-2217
    • Beven, L.1    Castano, S.2    Dufourcq, J.3    Wieslander, A.4    Wroblewski, H.5
  • 25
    • 0037742621 scopus 로고    scopus 로고
    • A novel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice
    • Papo, N., Shahar, M., Eisenbach, L. and Shai, Y. (2003) A novel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice. J. Biol. Chem. 278, 21018-21023
    • (2003) J. Biol. Chem , vol.278 , pp. 21018-21023
    • Papo, N.1    Shahar, M.2    Eisenbach, L.3    Shai, Y.4
  • 26
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462, 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 27
    • 0033066284 scopus 로고    scopus 로고
    • Interactions of α-helices with lipid bilayers: A review of simulation studies
    • Biggin, P. C. and Sansom, M. S. (1999) Interactions of α-helices with lipid bilayers: a review of simulation studies. Biophys. Chem. 76, 161-183
    • (1999) Biophys. Chem , vol.76 , pp. 161-183
    • Biggin, P.C.1    Sansom, M.S.2
  • 28
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe, M., Schumann, M., Wieprecht, T., Winkler, A., Beyermann, M., Krause, E., Matsuzaki, K., Murase, O. and Bienert, M. (1996) Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35, 12612-12622
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 29
    • 17044405174 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant factor VIIa for treatment of severe bleeding: A systematic review
    • Levi, M., Peters, M. and Buller, H. R. (2005) Efficacy and safety of recombinant factor VIIa for treatment of severe bleeding: a systematic review. Crit. Care Med. 33, 883-890
    • (2005) Crit. Care Med , vol.33 , pp. 883-890
    • Levi, M.1    Peters, M.2    Buller, H.R.3
  • 30
    • 24644491444 scopus 로고    scopus 로고
    • Recombinant factor VIIa as adjunctive therapy for bleeding control in severely injured trauma patients: Two parallel randomized, placebo-controlled, double-blind clinical trials
    • Boffard, K. D., Riou, B., Warren, B., Choong, P. I., Rizoli, S., Rossaint, R., Axelsen, M. and Kluger, Y. (2005) Recombinant factor VIIa as adjunctive therapy for bleeding control in severely injured trauma patients: two parallel randomized, placebo-controlled, double-blind clinical trials. J. Trauma 59, 8-15
    • (2005) J. Trauma , vol.59 , pp. 8-15
    • Boffard, K.D.1    Riou, B.2    Warren, B.3    Choong, P.I.4    Rizoli, S.5    Rossaint, R.6    Axelsen, M.7    Kluger, Y.8
  • 31
    • 33645549194 scopus 로고    scopus 로고
    • A special report on the chitosan-based hemostatic dressing: Experience in current combat operations
    • Wedmore, I., McManus, J. G., Pusateri, A. E. and Holcomb, J. B. (2006) A special report on the chitosan-based hemostatic dressing: experience in current combat operations. J. Trauma 60, 655-658
    • (2006) J. Trauma , vol.60 , pp. 655-658
    • Wedmore, I.1    McManus, J.G.2    Pusateri, A.E.3    Holcomb, J.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.