메뉴 건너뛰기




Volumn 121, Issue 11, 2013, Pages 2108-2116

A novel B-domain O-glycoPEGylated FVIII (N8-GP) demonstrates full efficacy and prolonged effect in hemophilic mice models

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; MACROGOL; RECOMBINANT BLOOD CLOTTING FACTOR 8; THROMBIN; VON WILLEBRAND FACTOR; BLOOD CLOTTING FACTOR 8; MACROGOL DERIVATIVE; N8 GP COMPOUND; N8-GP COMPOUND;

EID: 84877623981     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2012-01-407494     Document Type: Article
Times cited : (117)

References (36)
  • 1
    • 56649103608 scopus 로고    scopus 로고
    • Primary prophylaxis in children with haemophilia
    • Coppola A, Di Capua M, De Simone C. Primary prophylaxis in children with haemophilia. Blood Transfus. 2008;6:(suppl 2):s4-s11.
    • (2008) Blood Transfus , vol.6 , pp. s4-s11
    • Coppola, A.1    Di Capua, M.2    De Simone, C.3
  • 2
    • 34447127750 scopus 로고    scopus 로고
    • Prophylaxis in adults with haemophilia
    • Hay CR. Prophylaxis in adults with haemophilia. Haemophilia. 2007;13:(suppl 2):10-15.
    • (2007) Haemophilia , vol.13 , pp. 10-15
    • Hay, C.R.1
  • 3
    • 34547757915 scopus 로고    scopus 로고
    • Prophylaxis versus episodic treatment to prevent joint disease in boys with severe hemophilia
    • Manco-Johnson MJ, Abshire TC, Shapiro AD, et al. Prophylaxis versus episodic treatment to prevent joint disease in boys with severe hemophilia. N Engl J Med. 2007;357(6):535-544.
    • (2007) N Engl J Med , vol.357 , Issue.6 , pp. 535-544
    • Manco-Johnson, M.J.1    Abshire, T.C.2    Shapiro, A.D.3
  • 4
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • Harris JM, Chess RB. Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov. 2003; 2(3):214-221.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.3 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 5
    • 64749101544 scopus 로고    scopus 로고
    • Peg-modified biopharmaceuticals
    • Bailon P, Won CY. PEG-modified biopharmaceuticals. Expert Opin Drug Deliv. 2009;6(1):1-16.
    • (2009) Expert Opin Drug Deliv , vol.6 , Issue.1 , pp. 1-16
    • Bailon, P.1    Won, C.Y.2
  • 6
    • 79960942844 scopus 로고    scopus 로고
    • Polymer therapeutics as nanomedicines: New perspectives
    • Duncan R. Polymer therapeutics as nanomedicines: new perspectives. Curr Opin Biotechnol. 2011;22(4):492-501.
    • (2011) Curr Opin Biotechnol , vol.22 , Issue.4 , pp. 492-501
    • Duncan, R.1
  • 7
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of pegylation: Balancing pd with pk to generate novel therapeutics
    • Fishburn CS. The pharmacology of PEGylation: balancing PD with PK to generate novel therapeutics. J Pharm Sci. 2008;97(10): 4167-4183.
    • (2008) J Pharm Sci , vol.97 , Issue.10 , pp. 4167-4183
    • Fishburn, C.S.1
  • 8
    • 77955492929 scopus 로고    scopus 로고
    • Rational design of a fully active, long-acting pegylated factor viii for hemophilia a treatment
    • Mei B, Pan C, Jiang H, et al. Rational design of a fully active, long-acting PEGylated factor VIII for hemophilia A treatment. Blood. 2010;116(2): 270-279.
    • (2010) Blood , vol.116 , Issue.2 , pp. 270-279
    • Mei, B.1    Pan, C.2    Jiang, H.3
  • 9
    • 84855413310 scopus 로고    scopus 로고
    • Pioneering designs for recombinant coagulation factors
    • Schulte S. Pioneering designs for recombinant coagulation factors. Thromb Res. 2011;128:(suppl 1):S9-S12.
    • (2011) Thromb Res , vol.128 , pp. S9-S12
    • Schulte, S.1
  • 10
    • 33744937065 scopus 로고    scopus 로고
    • Monomeric fc fusions: Impact on pharmacokinetic and biological activity of protein therapeutics
    • Dumont JA, Low SC, Peters RT, et al. Monomeric Fc fusions: impact on pharmacokinetic and biological activity of protein therapeutics. BioDrugs. 2006;20(3):151-160.
    • (2006) Biodrugs , vol.20 , Issue.3 , pp. 151-160
    • Dumont, J.A.1    Low, S.C.2    Peters, R.T.3
  • 11
    • 84859197329 scopus 로고    scopus 로고
    • Safety and prolonged activity of recombinant factor viii fc fusion protein in hemophilia a patients
    • Powell JS, Josephson NC, Quon D, et al. Safety and prolonged activity of recombinant factor VIII Fc fusion protein in hemophilia A patients. Blood. 2012;119(13):3031-3037.
    • (2012) Blood , vol.119 , Issue.13 , pp. 3031-3037
    • Powell, J.S.1    Josephson, N.C.2    Quon, D.3
  • 12
    • 33748689917 scopus 로고    scopus 로고
    • Glycopegylation of recombinant therapeutic proteins produced in escherichia coli
    • DeFrees S, Wang ZG, Xing R, et al. GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli. Glycobiology. 2006;16(9):833-843.
    • (2006) Glycobiology , vol.16 , Issue.9 , pp. 833-843
    • DeFrees, S.1    Wang, Z.G.2    Xing, R.3
  • 13
    • 55549105470 scopus 로고    scopus 로고
    • Generation and biochemical characterization of glycopegylated factor viia derivatives
    • Stennicke HR, Ostergaard H, Bayer RJ, et al. Generation and biochemical characterization of glycoPEGylated factor VIIa derivatives. Thromb Haemost. 2008;100(5):920-928.
    • (2008) Thromb Haemost , vol.100 , Issue.5 , pp. 920-928
    • Stennicke, H.R.1    Ostergaard, H.2    Bayer, R.J.3
  • 14
    • 77950245746 scopus 로고    scopus 로고
    • Purification and characterization of a new recombinant factor Viii (n8)
    • Thim L, Vandahl B, Karlsson J, et al. Purification and characterization of a new recombinant factor VIII (N8). Haemophilia. 2010;16(2):349-359.
    • (2010) Haemophilia , vol.16 , Issue.2 , pp. 349-359
    • Thim, L.1    Vandahl, B.2    Karlsson, J.3
  • 15
    • 84857936508 scopus 로고    scopus 로고
    • Bioequivalence between two serum-free recombinant factor viii preparations (n8 and advate®) — An open-label, sequential dosing pharmacokinetic study in patients with severe haemophilia a
    • Martinowitz U, Bjerre J, Brand B, et al. Bioequivalence between two serum-free recombinant factor VIII preparations (N8 and ADVATE®) — an open-label, sequential dosing pharmacokinetic study in patients with severe haemophilia A. Haemophilia. 2011;17(6):854-859.
    • (2011) Haemophilia , vol.17 , Issue.6 , pp. 854-859
    • Martinowitz, U.1    Bjerre, J.2    Brand, B.3
  • 16
    • 83355173939 scopus 로고    scopus 로고
    • Requirements for immune recognition and processing of factor viii by antigen-presenting cells
    • van Haren SD, Wroblewska A, Fischer K, et al. Requirements for immune recognition and processing of factor VIII by antigen-presenting cells. Blood Rev. 2012;26(1):43-49.
    • (2012) Blood Rev , vol.26 , Issue.1 , pp. 43-49
    • Van Haren, S.D.1    Wroblewska, A.2    Fischer, K.3
  • 17
    • 20544472044 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a sialidase gene from arthrobacter ureafaciens
    • Christensen S, Egebjerg J. Cloning, expression and characterization of a sialidase gene from Arthrobacter ureafaciens. Biotechnol Appl Biochem. 2005;41(pt 3):225-231.
    • (2005) Biotechnol Appl Biochem , vol.41 , pp. 225-231
    • Christensen, S.1    Egebjerg, J.2
  • 18
    • 0027933180 scopus 로고
    • Nmr solution structure of the recombinant tick anticoagulant protein (rtap), a factor xa inhibitor from the tick ornithodoros moubata
    • Antuch W, Güntert P, Billeter M, et al. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata. FEBS Lett. 1994;352(2):251-257.
    • (1994) FEBS Lett , vol.352 , Issue.2 , pp. 251-257
    • Antuch, W.1    Güntert, P.2    Billeter, M.3
  • 19
    • 0028936409 scopus 로고
    • Nmr structure determination of tick anticoagulant peptide (tap)
    • Lim-Wilby MS, Hallenga K, de Maeyer M, et al. NMR structure determination of tick anticoagulant peptide (TAP). Protein Sci. 1995;4(2):178-186.
    • (1995) Protein Sci , vol.4 , Issue.2 , pp. 178-186
    • Lim-Wilby, M.S.1    Hallenga, K.2    De Maeyer, M.3
  • 20
    • 0032483024 scopus 로고    scopus 로고
    • A mouse model of severe von willebrand disease: Defects in hemostasis and thrombosis
    • Denis C, Methia N, Frenette PS, et al. A mouse model of severe von Willebrand disease: defects in hemostasis and thrombosis. Proc Natl Acad Sci USA. 1998;95(16):9524-9529.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.16 , pp. 9524-9529
    • Denis, C.1    Methia, N.2    Frenette, P.S.3
  • 21
    • 0029957538 scopus 로고    scopus 로고
    • Further characterization of factor viii-deficient mice created by gene targeting: Rna and protein studies
    • Bi L, Sarkar R, Naas T, et al. Further characterization of factor VIII-deficient mice created by gene targeting: RNA and protein studies. Blood. 1996;88(9):3446-3450.
    • (1996) Blood , vol.88 , Issue.9 , pp. 3446-3450
    • Bi, L.1    Sarkar, R.2    Naas, T.3
  • 23
    • 43749094984 scopus 로고    scopus 로고
    • Hemostatic effect of recombinant factor viia, nn1731 and recombinant factor viii on needle-induced joint bleeding in hemophilia a mice
    • Ovlisen K, Kristensen AT, Valentino LA, et al. Hemostatic effect of recombinant factor VIIa, NN1731 and recombinant factor VIII on needle-induced joint bleeding in hemophilia A mice. J Thromb Haemost. 2008;6(6):969-975.
    • (2008) J Thromb Haemost , vol.6 , Issue.6 , pp. 969-975
    • Ovlisen, K.1    Kristensen, A.T.2    Valentino, L.A.3
  • 24
    • 78049285783 scopus 로고    scopus 로고
    • Functional characteristics of n8, a new recombinant Fviii
    • Christiansen ML, Balling KW, Persson E, et al. Functional characteristics of N8, a new recombinant FVIII. Haemophilia. 2010;16(6): 878-887.
    • (2010) Haemophilia , vol.16 , Issue.6 , pp. 878-887
    • Christiansen, M.L.1    Balling, K.W.2    Persson, E.3
  • 25
    • 84355162247 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of a new recombinant fviii (n8) in haemophilia a mice
    • Elm T, Karpf DM, Øvlisen K, et al. Pharmacokinetics and pharmacodynamics of a new recombinant FVIII (N8) in haemophilia A mice. Haemophilia. 2012;18(1):139-145.
    • (2012) Haemophilia , vol.18 , Issue.1 , pp. 139-145
    • Elm, T.1    Karpf, D.M.2    Øvlisen, K.3
  • 26
    • 73949088476 scopus 로고    scopus 로고
    • A ferric chloride induced arterial injury model used as haemostatic effect model
    • Møller F, Tranholm M. A ferric chloride induced arterial injury model used as haemostatic effect model. Haemophilia. 2010;16(1):e216-e222.
    • (2010) Haemophilia , vol.16 , Issue.1 , pp. e216-e222
    • Møller, F.1    Tranholm, M.2
  • 27
    • 0018706876 scopus 로고
    • Enzymatic properties of neuraminidases from arthrobacter ureafaciens
    • Uchida Y, Tsukada Y, Sugimori T. Enzymatic properties of neuraminidases from Arthrobacter ureafaciens. J Biochem. 1979;86(5):1573-1585.
    • (1979) J Biochem , vol.86 , Issue.5 , pp. 1573-1585
    • Uchida, Y.1    Tsukada, Y.2    Sugimori, T.3
  • 28
    • 0037926885 scopus 로고    scopus 로고
    • Elevated plasma factor viii in a mouse model of low-density lipoprotein receptor-related protein deficiency
    • Bovenschen N, Herz J, Grimbergen JM, et al. Elevated plasma factor VIII in a mouse model of low-density lipoprotein receptor-related protein deficiency. Blood. 2003;101(10):3933-3939.
    • (2003) Blood , vol.101 , Issue.10 , pp. 3933-3939
    • Bovenschen, N.1    Herz, J.2    Grimbergen, J.M.3
  • 29
    • 0033588163 scopus 로고    scopus 로고
    • The light chain of factor viii comprises a binding site for low density lipoprotein receptor-related protein
    • Lenting PJ, Neels JG, van den Berg BM, et al. The light chain of factor VIII comprises a binding site for low density lipoprotein receptor-related protein. J Biol Chem. 1999;274(34):23734-23739.
    • (1999) J Biol Chem , vol.274 , Issue.34 , pp. 23734-23739
    • Lenting, P.J.1    Neels, J.G.2    Van Den Berg, B.M.3
  • 30
    • 0033621486 scopus 로고    scopus 로고
    • Role of the low density lipoprotein-related protein receptor in mediation of factor viii catabolism
    • Saenko EL, Yakhyaev AV, Mikhailenko I, et al. Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism. J Biol Chem. 1999;274(53):37685-37692.
    • (1999) J Biol Chem , vol.274 , Issue.53 , pp. 37685-37692
    • Saenko, E.L.1    Yakhyaev, A.V.2    Mikhailenko, I.3
  • 31
    • 84856486915 scopus 로고    scopus 로고
    • Uptake of blood coagulation factor viii by dendritic cells is mediated via its c1 domain
    • Herczenik E, van Haren SD, Wroblewska A, et al. Uptake of blood coagulation factor VIII by dendritic cells is mediated via its C1 domain. J Allergy Clin Immunol. 2012;129(2):501-509, 509.e1-e5.
    • (2012) J Allergy Clin Immunol , vol.129 , Issue.2
    • Herczenik, E.1    Van Haren, S.D.2    Wroblewska, A.3
  • 32
    • 67449124634 scopus 로고    scopus 로고
    • Efficacy and safety of certolizumab pegol plus methotrexate in active rheumatoid arthritis: The rapid 2 study. A randomised controlled trial
    • Smolen J, Landewé RB, Mease P, et al. Efficacy and safety of certolizumab pegol plus methotrexate in active rheumatoid arthritis: the RAPID 2 study. A randomised controlled trial. Ann Rheum Dis. 2009;68(6):797-804.
    • (2009) Ann Rheum Dis , vol.68 , Issue.6 , pp. 797-804
    • Smolen, J.1    Landewé, R.B.2    Mease, P.3
  • 33
    • 0029858896 scopus 로고    scopus 로고
    • Shear-dependent changes in the three-dimensional structure of human von willebrand factor
    • Siedlecki CA, Lestini BJ, Kottke-Marchant KK, et al. Shear-dependent changes in the three-dimensional structure of human von Willebrand factor. Blood. 1996;88(8):2939-2950.
    • (1996) Blood , vol.88 , Issue.8 , pp. 2939-2950
    • Siedlecki, C.A.1    Lestini, B.J.2    Kottke-Marchant, K.K.3
  • 34
    • 85023182997 scopus 로고    scopus 로고
    • Glycopegylation of fviii reduces cellular uptake in the liver, but does not alter in vivo distribution
    • Appa RS, Oie CI, Kristensen JB, et al. GlycoPEGylation of FVIII reduces cellular uptake in the liver, but does not alter in vivo distribution. J Thromb Haemost. 2011;9:(suppl s2):567-568.
    • (2011) J Thromb Haemost , vol.9 , pp. 567-568
    • Appa, R.S.1    Oie, C.I.2    Kristensen, J.B.3
  • 35
    • 33846244931 scopus 로고    scopus 로고
    • Vwf protects fviii from endocytosis by dendritic cells and subsequent presentation to immune effectors
    • Dasgupta S, Repessé Y, Bayry J, et al. VWF protects FVIII from endocytosis by dendritic cells and subsequent presentation to immune effectors. Blood. 2007;109(2):610-612.
    • (2007) Blood , vol.109 , Issue.2 , pp. 610-612
    • Dasgupta, S.1    Repessé, Y.2    Bayry, J.3
  • 36
    • 84861896973 scopus 로고    scopus 로고
    • Modification of an exposed loop in the c1 domain reduces immune responses to factor viii in hemophilia a mice
    • Wroblewska A, van Haren SD, Herczenik E, et al. Modification of an exposed loop in the C1 domain reduces immune responses to factor VIII in hemophilia A mice. Blood. 2012;119(22): 5294-5300.
    • (2012) Blood , vol.119 , Issue.22 , pp. 5294-5300
    • Wroblewska, A.1    Van Haren, S.D.2    Herczenik, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.