메뉴 건너뛰기




Volumn 104, Issue 6, 2010, Pages 1093-1098

Endocytic receptor for pro-coagulant factor VIII: Relevance to inhibitor formation

Author keywords

Allo immunisation; Antigen presenting cells; Endocytic receptors; Factor VIII; Haemophilia A

Indexed keywords

ASIALOGLYCOPROTEIN RECEPTOR; BLOOD CLOTTING FACTOR 8; CELL RECEPTOR; ENDOCYTIC RECEPTOR; GLYCAN DERIVATIVE; IMMUNOGLOBULIN G; LOW DENSITY LIPOPROTEIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MANNOSE RECEPTOR; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PROCOAGULANT; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

EID: 78649726401     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH10-05-0294     Document Type: Review
Times cited : (8)

References (72)
  • 2
    • 0023274159 scopus 로고
    • Factor VIII inhibitor IgG sub-class and FVIII polypeptide specificity determined by immunoblotting
    • Fulcher CA, de Graaf Mahoney S, Zimmerman TS. Factor VIII inhibitor IgG sub-class and FVIII polypeptide specificity determined by immunoblotting. Blood 1987; 69: 1475-1480.
    • (1987) Blood , vol.69 , pp. 1475-1480
    • Fulcher, C.A.1    De Graaf Mahoney, S.2    Zimmerman, T.S.3
  • 4
    • 0028837315 scopus 로고
    • The Nijmegen modification of the Bethesda assay for Factor VIII: C inhibitors: improved specificity and reliability
    • Verbruggen B, Novakova I, Wessels H, et al. The Nijmegen modification of the Bethesda assay for Factor VIII: C inhibitors: improved specificity and reliability. Thromb Haemost 1995; 73: 247-251.
    • (1995) Thromb Haemost , vol.73 , pp. 247-251
    • Verbruggen, B.1    Novakova, I.2    Wessels, H.3
  • 5
    • 0024451521 scopus 로고
    • Localization of epitopes for human factor VIII inhibitor antibodies by immunoblotting and antibody neutralization
    • Scandella D, Mattingly M, de Graaf S, et al. Localization of epitopes for human factor VIII inhibitior antibodies by immunoblotting and antibody neutralization. Blood 1989; 74: 1618-1626. (Pubitemid 19251538)
    • (1989) Blood , vol.74 , Issue.5 , pp. 1618-1626
    • Scandella, D.1    Mattingly, M.2    De Graaf, S.3    Fulcher, C.A.4
  • 6
    • 0035169521 scopus 로고    scopus 로고
    • Antigenicity of putative phospholipid membrane-binding residues in factor VIII
    • DOI 10.1182/blood.V97.1.169
    • Barrow R, Healey J, Jacquemin M, et al. Antigenicity of putative phospholipid membrane-binding residues in factor VIII. Blood 2001; 97: 169-174. (Pubitemid 32061257)
    • (2001) Blood , vol.97 , Issue.1 , pp. 169-174
    • Barrow, R.T.1    Healey, J.F.2    Jacquemin, M.G.3    Saint-Remy, J.-M.R.4    Lollar, P.5
  • 8
    • 0344776562 scopus 로고
    • Epitope mapping of human factor VIII inhibitor antibodies by deletion analysis of factor VIII fragments expressed in Escherichia coli
    • Scandella D, De Graaf Mahoney S, Mattingly M, et al. Epitope mapping of human factor VIII inhibitor antibodies by deletion analysis of factor VIII fragments expressed in Escherichia coli. Proc Natl Acad Sci USA 1988; 85: 6152-6156.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6152-6156
    • Scandella, D.1    De Graaf Mahoney, S.2    Mattingly, M.3
  • 9
    • 0036625005 scopus 로고    scopus 로고
    • A novel mechanism of factor VIII protection by von Willebrand factor from activated protein C-catalyzed inactivation
    • Nogami K, Shima M, Nishiya K, et al. A novel mechanism of factor VIII protection by von Willebrand factor from activated protein C-catalyzed inactivation. Blood 2002; 99: 3993-3998.
    • (2002) Blood , vol.99 , pp. 3993-3998
    • Nogami, K.1    Shima, M.2    Nishiya, K.3
  • 10
    • 0025297357 scopus 로고
    • Synthetic factor VIII peptides with amino acid sequences contained within the C2 domain of factor VIII inhibit factor VIII binding to phosphatidylserine
    • Foster PA, Fulcher CA, Huoghten RA, et al. Synthetic factor VIII peptides with amino acid sequences contained within the C2 domain of factor VIII inhibit factor VIII binding to phosphatidylserine. Blood 1990; 75: 1999-2004.
    • (1990) Blood , vol.75 , pp. 1999-2004
    • Foster, P.A.1    Fulcher, C.A.2    Huoghten, R.A.3
  • 11
    • 34547523962 scopus 로고    scopus 로고
    • Relationship between the binding sites for von Willebrand factor, phospholipid, and human factor VIII C2 inhibitor alloantibodies within the factor VIII C2 domain
    • DOI 10.1532/IJH97.06192
    • Nogami K, Shima M, Giddings JC, et al. Relationship between the binding sites for von Willebrand factor, phospholipid, and human factor VIII C2 inhibitor alloantibodies within the factor VIII C2 domain. Int J Hematol 2007; 85: 317-322. (Pubitemid 47182058)
    • (2007) International Journal of Hematology , vol.85 , Issue.4 , pp. 317-322
    • Nogami, K.1    Shima, M.2    Giddings, J.C.3    Takeyama, M.4    Tanaka, I.5    Yoshioka, A.6
  • 12
    • 0032882449 scopus 로고    scopus 로고
    • Epitope specificity and inactivation mechanisms of factor VIII inhibitor antibodies
    • Scandella D. Epitope specificity and inactivation mechanisms of factor VIII inhibitor antibodies. Vox Sang 1999; 77 (Suppl 1): 17-20. (Pubitemid 29469249)
    • (1999) Vox Sanguinis , vol.77 , Issue.SUPPL. 1 , pp. 17-20
    • Scandella, D.1
  • 13
    • 0028863147 scopus 로고
    • Common inhibitory effects of human anti-C2 domain inhibitor alloantibodies on factor VIII binding to von Willebrand factor
    • Shima M, Nakai H, Scandella D, et al. Common inhibitory effects of human anti-C2 domain inhibitor alloantibodies on factor VIII binding to von Willebrand factor. Br J Haematol 1995; 91: 714-721.
    • (1995) Br J Haematol , vol.91 , pp. 714-721
    • Shima, M.1    Nakai, H.2    Scandella, D.3
  • 14
    • 0027250069 scopus 로고
    • A recombinant factor VIII A2 domain polypeptide quantitatively neutralizes human inhibitor antibodies that bind to A2
    • Scandella D, Mattingly M, Prescott R. A recombinant Factor VIII A2 domain polypeptide quantitatively neutralizes human inhibitor antibodies that bind to A2. Blood 1993; 82: 1767-1775. (Pubitemid 23278767)
    • (1993) Blood , vol.82 , Issue.6 , pp. 1767-1775
    • Scandella, D.1    Mattingly, M.2    Prescott, R.3
  • 15
    • 0032127414 scopus 로고    scopus 로고
    • Some human inhibitor antibodies interfere with factor VIII binding to factor IX
    • Zhong D, Saenko EL, Shima M, et al. Some human inhibitor antibodies interfere with factor VIII binding to Factor IX. Blood 1998; 92: 136-142. (Pubitemid 28303185)
    • (1998) Blood , vol.92 , Issue.1 , pp. 136-142
    • Zhong, D.1    Saenko, E.L.2    Shima, M.3    Felch, M.4    Scandella, D.5
  • 16
    • 0033570089 scopus 로고    scopus 로고
    • Human inhibitor antibodies specific for the factor VIII A2 domain disrupt the interaction between the subunit and factor IXa
    • DOI 10.1074/jbc.274.42.29826
    • Fay PJ, Scandella D. Human inhibitor antibodies specific for the factor VIII A2 domain disrupt the interaction between the subunit and factor IXa. J Biol Chem 1999; 274: 29826-29830. (Pubitemid 29483358)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.42 , pp. 29826-29830
    • Fay, P.J.1    Scandella, D.2
  • 18
    • 0018876848 scopus 로고
    • Circulating immune complexes containing anti-FVIII antibodies in multitransfused patients with haemophilia A
    • Kazatchkine MD, Sultan Y, Burton-Kee EJ, et al. Circulating immune complexes containing anti-FVIII antibodies in multitransfused patients with haemophilia A. Clin Exp Immunol 1980; 39: 315-320.
    • (1980) Clin Exp Immunol , vol.39 , pp. 315-320
    • Kazatchkine, M.D.1    Sultan, Y.2    Burton-Kee, E.J.3
  • 19
    • 20244363765 scopus 로고    scopus 로고
    • Catalytic activity of antibodies against factor VIII in patients with hemophilia A
    • Lacroix-Desmazes S, Moreau A, Sooryanarayana, et al. Catalytic activity of antibodies against factor VIII in patients with hemophilia A. Nat Med 1999; 5: 1044-1047.
    • (1999) Nat Med , vol.5 , pp. 1044-1047
    • Lacroix-Desmazes, S.1    Moreau, A.2    Sooryanarayana3
  • 20
    • 0037186916 scopus 로고    scopus 로고
    • The prevalence of proteolytic anti-bodies against factor VIII in hemophilia A
    • Lacroix-Desmazes S, Bayry J, Misra N, et al. The prevalence of proteolytic anti-bodies against factor VIII in hemophilia A. N Engl J Med 2002; 346: 662-667.
    • (2002) N Engl J Med , vol.346 , pp. 662-667
    • Lacroix-Desmazes, S.1    Bayry, J.2    Misra, N.3
  • 21
    • 33745869467 scopus 로고    scopus 로고
    • Catalytic IgG from patients with hemophilia a inactivate therapeutic factor VIII
    • Lacroix-Desmazes S, Wootla B, Dasgupta S, et al. Catalytic IgG from patients with hemophilia A inactivate therapeutic factor VIII. J Immunol 2006; 177: 1355-1363.
    • (2006) J Immunol , vol.177 , pp. 1355-1363
    • Lacroix-Desmazes, S.1    Wootla, B.2    Dasgupta, S.3
  • 22
    • 0037441590 scopus 로고    scopus 로고
    • CD4+ T-cell clones specific for wild-type factor VIII: A molecular mechanism responsible for a higher incidence of inhibitor formation in mild/moderate hemophilia A
    • Jacquemin M, Vantomme V, Buhot C, et al. CD4+ T-cell clones specific for wild-type factor VIII: a molecular mechanism responsible for a higher incidence of inhibitor formation in mild/moderate hemophilia A. Blood 2003; 101: 1351-1358.
    • (2003) Blood , vol.101 , pp. 1351-1358
    • Jacquemin, M.1    Vantomme, V.2    Buhot, C.3
  • 23
    • 0030035721 scopus 로고    scopus 로고
    • T lymphocyte proliferative responses induced by recombinant factor VIII in hemophilia A patients with inhibitors
    • Singer ST, Addiego JE, Jr., Reason DC, et al. T lymphocyte proliferative responses induced by recombinant factor VIII in hemophilia A patients with inhibitors. Thromb Haemost 1996; 76: 17-22.
    • (1996) Thromb Haemost , vol.76 , pp. 17-22
    • Singer, S.T.1    Addiego Jr., J.E.2    Reason, D.C.3
  • 24
    • 0032725319 scopus 로고    scopus 로고
    • CD4+ T cell response to factor VIII in hemophilia A, acquired hemophilia, and healthy subjects
    • Reding MT, Wu H, Krampf M, et al. CD4+ T cell response to factor VIII in hemophilia A, acquired hemophilia, and healthy subjects. Thromb Haemost 1999; 82: 509-515.
    • (1999) Thromb Haemost , vol.82 , pp. 509-515
    • Reding, M.T.1    Wu, H.2    Krampf, M.3
  • 25
    • 0033786760 scopus 로고    scopus 로고
    • Sensitization of CD4+ T cells to coagulation factor VIII: Response in congenital and acquired hemophilia patients and in healthy subjects
    • Reding M, Wu H, Krampf M, et al. Sensitization of CD4+ T cells to coagulation factor VIII: response in congenital and acquired hemophilia patients and in healthy subjects. Thromb Haemost 2000; 84: 643-652.
    • (2000) Thromb Haemost , vol.84 , pp. 643-652
    • Reding, M.1    Wu, H.2    Krampf, M.3
  • 26
    • 0036797443 scopus 로고    scopus 로고
    • Distribution of Th1- And Th2-induced Anti-factor VIII IgG Subclasses in Congenital and Acquired Hemophilia Patients
    • Reding MT, Lei S, Lei H, et al. Distribution of Th1- and Th2-induced Anti-factor VIII IgG Subclasses in Congenital and Acquired Hemophilia Patients. Thromb Haemost 2002; 88: 568-575.
    • (2002) Thromb Haemost , vol.88 , pp. 568-575
    • Reding, M.T.1    Lei, S.2    Lei, H.3
  • 27
    • 1642295197 scopus 로고    scopus 로고
    • Human CD4+ T-cell epitope repertoire on the C2 domain of coagulation factor VIII
    • Reding MT, Okita DK, Diethelm-Okita BM, et al. Human CD4+ T-cell epitope repertoire on the C2 domain of coagulation factor VIII. J Thromb Haemost 2003; 1: 1777-1784.
    • (2003) J Thromb Haemost , vol.1 , pp. 1777-1784
    • Reding, M.T.1    Okita, D.K.2    Diethelm-Okita, B.M.3
  • 28
    • 36349021392 scopus 로고    scopus 로고
    • T-cell responses over time in a mild hemophilia A inhibitor subject: Epitope identification and transient immunogenicity of the corresponding self-peptide
    • James EA, Kwok WW, Ettinger RA, et al. T-cell responses over time in a mild hemophilia A inhibitor subject: epitope identification and transient immunogenicity of the corresponding self-peptide. J Thromb Haemost 2007; 5: 2399-2407.
    • (2007) J Thromb Haemost , vol.5 , pp. 2399-2407
    • James, E.A.1    Kwok, W.W.2    Ettinger, R.A.3
  • 29
    • 70349328358 scopus 로고    scopus 로고
    • Lineages of human T-cell clones, including T helper 17/T helper 1 cells, isolated at different stages of anti-factor VIII immune responses
    • Ettinger RA, James EA, Kwok WW, et al. Lineages of human T-cell clones, including T helper 17/T helper 1 cells, isolated at different stages of anti-factor VIII immune responses. Blood 2009; 114: 1423-1428.
    • (2009) Blood , vol.114 , pp. 1423-1428
    • Ettinger, R.A.1    James, E.A.2    Kwok, W.W.3
  • 30
    • 10744226043 scopus 로고    scopus 로고
    • Restricted BV gene usage by factor VIII-reactive CD4+ T cells in inhibitor-positive patients with severe hemophilia A
    • Misra N, Bayry J, Pashov A, et al. Restricted BV gene usage by factor VIII-reactive CD4+ T cells in inhibitor-positive patients with severe hemophilia A. Thromb Haemost 2003; 90: 813-822.
    • (2003) Thromb Haemost , vol.90 , pp. 813-822
    • Misra, N.1    Bayry, J.2    Pashov, A.3
  • 31
    • 0023901449 scopus 로고
    • Disappearance of a high response factor VIII inhibitor in a hemophiliac with AIDS
    • Leyva WH, Knutsen AP, Joist JH. Disappearance of a high response factor VIII inhibitor in a hemophiliac with AIDS. Am J Clin Pathol 1988; 89: 414-418.
    • (1988) Am J Clin Pathol , vol.89 , pp. 414-418
    • Leyva, W.H.1    Knutsen, A.P.2    Joist, J.H.3
  • 32
    • 0024379471 scopus 로고
    • Disappearance of inhibitor to factor VIII in HIV-infected hemophiliacs with progression to AIDS or severe ARC
    • Ragni MV, Bontempo FA, Lewis JH. Disappearance of inhibitor to factor VIII in HIV-infected hemophiliacs with progression to AIDS or severe ARC. Transfusion 1989; 29: 447-449.
    • (1989) Transfusion , vol.29 , pp. 447-449
    • Ragni, M.V.1    Bontempo, F.A.2    Lewis, J.H.3
  • 33
    • 0027408194 scopus 로고
    • Loss of high-responder inhibitors in patients with severe hemophilia a and human immunodeficiency virus type 1 infection: A report from the Multi-Center Hemophilia Cohort Study
    • Bray GL, Kroner BL, Arkin S, et al. Loss of high-responder inhibitors in patients with severe hemophilia A and human immunodeficiency virus type 1 infection: a report from the Multi-Center Hemophilia Cohort Study. Am J Hematol 1993; 42: 375-379.
    • (1993) Am J Hematol , vol.42 , pp. 375-379
    • Bray, G.L.1    Kroner, B.L.2    Arkin, S.3
  • 34
    • 0033825674 scopus 로고    scopus 로고
    • Role of CD154 in the secondary immune response: The reduction of pre-existing splenic germinal centers and anti-factor VIII inhibitor titer
    • Qian J, Burkly L, Smith E, et al. Role of CD154 in the secondary immune response: the reduction of pre-existing splenic germinal centers and anti-factor VIII inhibitor titer. Eur J Immunol 2000; 30: 2548-2554.
    • (2000) Eur J Immunol , vol.30 , pp. 2548-2554
    • Qian, J.1    Burkly, L.2    Smith, E.3
  • 35
    • 0034651552 scopus 로고    scopus 로고
    • Prevention and treatment of factor VIII inhibitors in murine hemophilia A
    • Qian J, Collins M, Sharpe AH, et al. Prevention and treatment of factor VIII inhibitors in murine hemophilia A. Blood 2000; 95: 1324-1329.
    • (2000) Blood , vol.95 , pp. 1324-1329
    • Qian, J.1    Collins, M.2    Sharpe, A.H.3
  • 36
    • 0035655711 scopus 로고    scopus 로고
    • Blockade of CD40/CD40 ligand interactions prevents induction of factor VIII inhibitors in hemophilic mice but does not induce lasting immune tolerance
    • Reipert BM, Sasgary M, Ahmad RU, et al. Blockade of CD40/CD40 ligand interactions prevents induction of factor VIII inhibitors in hemophilic mice but does not induce lasting immune tolerance. Thromb Haemost 2001; 86: 1345-1352.
    • (2001) Thromb Haemost , vol.86 , pp. 1345-1352
    • Reipert, B.M.1    Sasgary, M.2    Ahmad, R.U.3
  • 37
    • 0035353196 scopus 로고    scopus 로고
    • Long-term induction of immune tolerance after blockade of CD40-CD40L interaction in a mouse model of hemophilia A
    • Rossi G, Sarkar J, Scandella D. Long-term induction of immune tolerance after blockade of CD40-CD40L interaction in a mouse model of hemophilia A. Blood 2001; 97: 2750-2757.
    • (2001) Blood , vol.97 , pp. 2750-2757
    • Rossi, G.1    Sarkar, J.2    Scandella, D.3
  • 38
    • 3042835164 scopus 로고    scopus 로고
    • Preventing restimulation of memory B cells in hemophilia a: A potential new strategy for the treatment of antibody-dependent immune disorders
    • Hausl C, Ahmad RU, Schwarz HP, et al. Preventing restimulation of memory B cells in hemophilia A: a potential new strategy for the treatment of antibody-dependent immune disorders. Blood 2004; 104: 115-122.
    • (2004) Blood , vol.104 , pp. 115-122
    • Hausl, C.1    Ahmad, R.U.2    Schwarz, H.P.3
  • 40
    • 11144296197 scopus 로고    scopus 로고
    • How do follicular dendritic cells interact intimately with B cells in the germinal centre?
    • Park CS, Choi YS. How do follicular dendritic cells interact intimately with B cells in the germinal centre? Immunology 2005; 114: 2-10.
    • (2005) Immunology , vol.114 , pp. 2-10
    • Park, C.S.1    Choi, Y.S.2
  • 41
    • 0036668676 scopus 로고    scopus 로고
    • Human follicular dendritic cells: Function, origin and development
    • van Nierop K, de Groot C. Human follicular dendritic cells: function, origin and development. Semin Immunol 2002; 14: 251-257.
    • (2002) Semin Immunol , vol.14 , pp. 251-257
    • Van Nierop, K.1    De Groot, C.2
  • 42
    • 70449431508 scopus 로고    scopus 로고
    • Splenic marginal zone antigen-presenting cells are critical for the primary allo-immune response to therapeutic factor VIII in hemophilia A
    • Navarrete A, Dasgupta S, Delignat S, et al. Splenic marginal zone antigen-presenting cells are critical for the primary allo-immune response to therapeutic factor VIII in hemophilia A. J Thromb Haemost 2009; 7: 1816-1823.
    • (2009) J Thromb Haemost , vol.7 , pp. 1816-1823
    • Navarrete, A.1    Dasgupta, S.2    Delignat, S.3
  • 43
    • 52649093281 scopus 로고    scopus 로고
    • Macrophages contribute to the cellular uptake of von Willebrand factor and factor VIII in vivo
    • van Schooten CJ, Shahbazi S, Groot E, et al. Macrophages contribute to the cellular uptake of von Willebrand factor and factor VIII in vivo. Blood 2008; 112: 1704-1712.
    • (2008) Blood , vol.112 , pp. 1704-1712
    • Van Schooten, C.J.1    Shahbazi, S.2    Groot, E.3
  • 44
    • 47649092909 scopus 로고    scopus 로고
    • Dynamics of factor VIII interactions determine its immunologic fate in hemophilia A
    • Lacroix-Desmazes S, Navarrete AM, Andre S, et al. Dynamics of factor VIII interactions determine its immunologic fate in hemophilia A. Blood 2008; 112: 240-249.
    • (2008) Blood , vol.112 , pp. 240-249
    • Lacroix-Desmazes, S.1    Navarrete, A.M.2    Andre, S.3
  • 45
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz J, Strickland DK. LRP: a multifunctional scavenger and signaling receptor. J Clin Invest 2001; 108: 779-784.
    • (2001) J Clin Invest , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 46
    • 4544310501 scopus 로고    scopus 로고
    • Clearance of coagulation factor VIII in very low-density lipoprotein receptor knockout mice
    • Bovenschen N, van Dijk KW, Havekes LM, et al. Clearance of coagulation factor VIII in very low-density lipoprotein receptor knockout mice. Br J Haematol 2004; 126: 722-725.
    • (2004) Br J Haematol , vol.126 , pp. 722-725
    • Bovenschen, N.1    Van Dijk, K.W.2    Havekes, L.M.3
  • 47
    • 77449091890 scopus 로고    scopus 로고
    • Inhibitors in hemophilia A: Advances in elucidation of inhibitory mechanisms and in inhibitor management with bypassing agents
    • Ananyeva NM, Lee TK, Jain N, et al. Inhibitors in hemophilia A: advances in elucidation of inhibitory mechanisms and in inhibitor management with bypassing agents. Semin Thromb Hemost 2009; 35: 735-751.
    • (2009) Semin Thromb Hemost , vol.35 , pp. 735-751
    • Ananyeva, N.M.1    Lee, T.K.2    Jain, N.3
  • 48
    • 0033588163 scopus 로고    scopus 로고
    • The light chain of factor VIII comprises a binding site for low density lipoprotein receptor-related protein
    • Lenting P, Neels J, van den Berg B, et al. The light chain of factor VIII comprises a binding site for low density lipoprotein receptor-related protein. J Biol Chem 1999; 274: 23734-23739.
    • (1999) J Biol Chem , vol.274 , pp. 23734-23739
    • Lenting, P.1    Neels, J.2    Van Den Berg, B.3
  • 49
    • 0033621486 scopus 로고    scopus 로고
    • Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism
    • Saenko E, Yakhyaev A, Mikhailenko I, et al. Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism. J Biol Chem 1999; 274: 37685-37692.
    • (1999) J Biol Chem , vol.274 , pp. 37685-37692
    • Saenko, E.1    Yakhyaev, A.2    Mikhailenko, I.3
  • 50
    • 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: 3933-3939.
    • (2003) Blood , vol.101 , pp. 3933-3939
    • Bovenschen, N.1    Herz, J.2    Grimbergen, J.M.3
  • 51
    • 0035853843 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans participate in factor viii catabolism mediated by low density lipoprotein receptor- Related protein
    • Sarafanov A, Ananyeva N, Shima M, et al. Cell surface heparan sulfate proteoglycans participate in factor viii catabolism mediated by low density lipoprotein receptor- related protein. J Biol Chem 2001; 276: 11970-11979.
    • (2001) J Biol Chem , vol.276 , pp. 11970-11979
    • Sarafanov, A.1    Ananyeva, N.2    Shima, M.3
  • 52
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • Srivastava P. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu Rev Immunol 2002; 20: 395-425.
    • (2002) Annu Rev Immunol , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 53
    • 38549178456 scopus 로고    scopus 로고
    • Factor VIII bypasses CD91/LRP for endocytosis by dendritic cells leading to T-cell activation
    • Dasgupta S, Navarrete AM, Andre S, et al. Factor VIII bypasses CD91/LRP for endocytosis by dendritic cells leading to T-cell activation. Haematologica 2008; 93: 83-89.
    • (2008) Haematologica , vol.93 , pp. 83-89
    • Dasgupta, S.1    Navarrete, A.M.2    Andre, S.3
  • 54
    • 0032402122 scopus 로고    scopus 로고
    • The life cycle of coagulation factor VIII in view of its structure and function
    • Lenting PJ, van Mourik JA, Mertens K. The life cycle of coagulation factor VIII in view of its structure and function. Blood 1998; 92: 3983-3996.
    • (1998) Blood , vol.92 , pp. 3983-3996
    • Lenting, P.J.1    Van Mourik, J.A.2    Mertens, K.3
  • 55
    • 0021677942 scopus 로고
    • Structure of human factor VIII
    • Vehar GA, Keyt B, Eaton DH, et al. Structure of human factor VIII. Nature 1984; 312: 337-342.
    • (1984) Nature , vol.312 , pp. 337-342
    • Vehar, G.A.1    Keyt, B.2    Eaton, D.H.3
  • 56
    • 0023918719 scopus 로고
    • Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells
    • Kaufman RJ, Wasley LC, Dorner AJ. Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells. J Biol Chem 1988; 263: 6352-6362.
    • (1988) J Biol Chem , vol.263 , pp. 6352-6362
    • Kaufman, R.J.1    Wasley, L.C.2    Dorner, A.J.3
  • 57
    • 0026733430 scopus 로고
    • Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells
    • Hironaka T, Furukawa K, Esmon PC, et al. Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells. J Biol Chem 1992; 267: 8012-8020.
    • (1992) J Biol Chem , vol.267 , pp. 8012-8020
    • Hironaka, T.1    Furukawa, K.2    Esmon, P.C.3
  • 58
    • 0031241505 scopus 로고    scopus 로고
    • Structural characterization of site-specific N-glycosylation of recombinant human factor VIII by reversed-phase high-performance liquid chromatography-electrospray ionization mass spectrometry
    • Medzihradszky KF, Besman MJ, Burlingame AL. Structural characterization of site-specific N-glycosylation of recombinant human factor VIII by reversed-phase high-performance liquid chromatography-electrospray ionization mass spectrometry. Anal Chem 1997; 69: 3986-3994.
    • (1997) Anal Chem , vol.69 , pp. 3986-3994
    • Medzihradszky, K.F.1    Besman, M.J.2    Burlingame, A.L.3
  • 59
    • 24944580953 scopus 로고    scopus 로고
    • The B domain of coagulation factor VIII interacts with the asialoglycoprotein receptor
    • Bovenschen N, Rijken DC, Havekes LM, et al. The B domain of coagulation factor VIII interacts with the asialoglycoprotein receptor. J Thromb Haemost 2005; 3: 1257-1265.
    • (2005) J Thromb Haemost , vol.3 , pp. 1257-1265
    • Bovenschen, N.1    Rijken, D.C.2    Havekes, L.M.3
  • 60
    • 34547430130 scopus 로고    scopus 로고
    • A role for exposed mannosylations in presentation of human therapeutic self-proteins to CD4+ T lymphocytes
    • Dasgupta S, Navarrete AM, Bayry J, et al. A role for exposed mannosylations in presentation of human therapeutic self-proteins to CD4+ T lymphocytes. Proc Natl Acad Sci USA 2007; 104: 8965-8970.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8965-8970
    • Dasgupta, S.1    Navarrete, A.M.2    Bayry, J.3
  • 61
    • 0037276262 scopus 로고    scopus 로고
    • The safety and efficacy of B-domain deleted recombinant factor VIII concentrate in patients with severe haemophilia A
    • Lusher JM, Lee CA, Kessler CM, et al. The safety and efficacy of B-domain deleted recombinant factor VIII concentrate in patients with severe haemophilia A. Haemophilia 2003; 9: 38-49.
    • (2003) Haemophilia , vol.9 , pp. 38-49
    • Lusher, J.M.1    Lee, C.A.2    Kessler, C.M.3
  • 62
    • 36348949128 scopus 로고    scopus 로고
    • Comparison of the immunogenicity of different therapeutic preparations of human factor VIII in the murine model of hemophilia A
    • Delignat S, Dasgupta S, Andre S, et al. Comparison of the immunogenicity of different therapeutic preparations of human factor VIII in the murine model of hemophilia A. Haematologica 2007; 92: 1423-1426.
    • (2007) Haematologica , vol.92 , pp. 1423-1426
    • Delignat, S.1    Dasgupta, S.2    Andre, S.3
  • 63
    • 33846244931 scopus 로고    scopus 로고
    • VWF protects FVIII from endocytosis by dendritic cells and subsequent presentation to immune effectors
    • Dasgupta S, Repesse Y, Bayry J, et al. VWF protects FVIII from endocytosis by dendritic cells and subsequent presentation to immune effectors. Blood 2007; 109: 610-612.
    • (2007) Blood , vol.109 , pp. 610-612
    • Dasgupta, S.1    Repesse, Y.2    Bayry, J.3
  • 64
    • 0029148878 scopus 로고
    • Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products
    • Sallusto F, Cella M, Danieli C, et al. Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products. J Exp Med 1995; 182: 389-400.
    • (1995) J Exp Med , vol.182 , pp. 389-400
    • Sallusto, F.1    Cella, M.2    Danieli, C.3
  • 65
    • 73349085222 scopus 로고    scopus 로고
    • Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII
    • Kosloski MP, Miclea RD, Balu-Iyer SV. Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII. AAPS J 2009; 11: 424-431.
    • (2009) AAPS J , vol.11 , pp. 424-431
    • Kosloski, M.P.1    Miclea, R.D.2    Balu-Iyer, S.V.3
  • 66
    • 38949168866 scopus 로고    scopus 로고
    • The tertiary structure and domain organization of coagulation factor VIII
    • Shen BW, Spiegel PC, Chang CH, et al. The tertiary structure and domain organization of coagulation factor VIII. Blood 2008; 111: 1240-1247.
    • (2008) Blood , vol.111 , pp. 1240-1247
    • Shen, B.W.1    Spiegel, P.C.2    Chang, C.H.3
  • 68
    • 0025608606 scopus 로고
    • Molecular characterization of the human macrophage mannose receptor: Demonstration of multiple carbohydrate recognition- Like domains and phagocytosis of yeasts in Cos-1 cells
    • Ezekowitz RA, Sastry K, Bailly P, et al. Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition- like domains and phagocytosis of yeasts in Cos-1 cells. J Exp Med 1990; 172: 1785-1794.
    • (1990) J Exp Med , vol.172 , pp. 1785-1794
    • Ezekowitz, R.A.1    Sastry, K.2    Bailly, P.3
  • 69
    • 0025362207 scopus 로고
    • Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains
    • Taylor ME, Conary JT, Lennartz MR, et al. Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains. J Biol Chem 1990; 265: 12156-12162.
    • (1990) J Biol Chem , vol.265 , pp. 12156-12162
    • Taylor, M.E.1    Conary, J.T.2    Lennartz, M.R.3
  • 70
    • 0032005288 scopus 로고    scopus 로고
    • The mannose receptor is a pattern recognition receptor involved in host defense
    • Stahl PD, Ezekowitz RA. The mannose receptor is a pattern recognition receptor involved in host defense. Curr Opin Immunol 1998; 10: 50-55.
    • (1998) Curr Opin Immunol , vol.10 , pp. 50-55
    • Stahl, P.D.1    Ezekowitz, R.A.2
  • 71
    • 0037040350 scopus 로고    scopus 로고
    • Mannose receptor-mediated regulation of serum glycoprotein homeostasis
    • Lee SJ, Evers S, Roeder D, et al. Mannose receptor-mediated regulation of serum glycoprotein homeostasis. Science 2002; 295: 1898-1901.
    • (2002) Science , vol.295 , pp. 1898-1901
    • Lee, S.J.1    Evers, S.2    Roeder, D.3
  • 72
    • 23044478501 scopus 로고    scopus 로고
    • LDL receptor cooperates with LDL receptor- Related protein in regulating plasma levels of coagulation factor VIII in vivo
    • Bovenschen N, Mertens K, Hu L, et al. LDL receptor cooperates with LDL receptor- related protein in regulating plasma levels of coagulation factor VIII in vivo. Blood 2005; 106: 906-912.
    • (2005) Blood , vol.106 , pp. 906-912
    • Bovenschen, N.1    Mertens, K.2    Hu, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.