Show simple item record

Mild/moderate haemophilia A: new insights into molecular mechanisms and inhibitor development

dc.contributor.authorD’oiron, R.en_US
dc.contributor.authorPipe, Steven W.en_US
dc.contributor.authorJacquemin, M.en_US
dc.date.accessioned2010-06-01T19:51:19Z
dc.date.available2010-06-01T19:51:19Z
dc.date.issued2008-07en_US
dc.identifier.citationD’OIRON, R.; PIPE, S. W.; JACQUEMIN, M. (2008). "Mild/moderate haemophilia A: new insights into molecular mechanisms and inhibitor development." Haemophilia 14(s3 State of the Art. XXVIII International Congress of the World Federation of Hemophilia ): 138-146. <http://hdl.handle.net/2027.42/72987>en_US
dc.identifier.issn1351-8216en_US
dc.identifier.issn1365-2516en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/72987
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=18510534&dopt=citationen_US
dc.format.extent138326 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rights© 2008 Blackwell Publishing Ltden_US
dc.subject.otherFactor VIIIen_US
dc.subject.otherGenotypeen_US
dc.subject.otherInhibitoren_US
dc.subject.otherMild/Moderate Haemophilia Aen_US
dc.subject.otherT-cell Epitopeen_US
dc.titleMild/moderate haemophilia A: new insights into molecular mechanisms and inhibitor developmenten_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelOncology and Hematologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationum† Department of Pediatrics, University of Michigan, Ann Arbor, MI USAen_US
dc.contributor.affiliationother* Centre de traitement pour HÉmophiles AP-HP HÔpital BicÊtre, UniversitÉ Paris XI, Le Kremlin-BicÊtre Cedex, Franceen_US
dc.contributor.affiliationother† Center for Molecular and Vascular Biology, University of Leuven, Leuven, Belgiumen_US
dc.identifier.pmid18510534en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/72987/1/j.1365-2516.2008.01730.x.pdf
dc.identifier.doi10.1111/j.1365-2516.2008.01730.xen_US
dc.identifier.sourceHaemophiliaen_US
dc.identifier.citedreferenceMannucci PM. Desmopressin (DDAVP) in the treatment of bleeding disorders: the first twenty years. Haemophilia 2000; 6 ( Suppl. 1 ): 60 – 67.en_US
dc.identifier.citedreferenceKemball-Cook G, Tuddenham EG, Wacey AI. The factor VIII structure and mutation resource site: HAMSTeRS version 4. Nucleic Acids Res 1998; 26: 216 – 9. Available at http://europium.csc.mrc.ac.uk/ accessed January 2008.en_US
dc.identifier.citedreferenceFay PJ, Jenkins PV. Mutating factor VIII: lessons from structure to function. Blood Rev 2005; 19: 15 – 27.en_US
dc.identifier.citedreferenceShen BW, Spiegel PC, Chang CH et al. The tertiary structure and domain organization of coagulation factor VIII. Blood 2008; 111: 1240 – 7.en_US
dc.identifier.citedreferenceHay CRM, Ludlam CA, Colvin BT et al. Factor VIII inhibitors in mild and moderate-severity haemophilia A. Thromb Haemost 1998; 79: 762 – 6.en_US
dc.identifier.citedreferenceOldenburg J, El-Maarri O, Schwaab R. Inhibitor development in correlation to factor VIII genotypes. Haemophilia 2002; 8: 23 – 29.en_US
dc.identifier.citedreferenceFijnvandraat K, Turenhout EAM, van den Brink EN et al. The missense mutation Arg 593 → Cys is related to antibody formation in a patient with mild hemophilia A. Blood 1997; 89: 4371 – 7.en_US
dc.identifier.citedreferencePeerlinck K, Jacquemin M. Inhibitors to factor VIII-mild and moderate hemophilia. In: Lee CA, Berntorp EE, Hoots WK, eds. Textbook of Hemophilia Oxford: Blackwell Publishing, 2005: 71 – 73.en_US
dc.identifier.citedreferenceSantagostino E, Gringeri A, Tagliavacca L, Mannucci PM. Inhibitors to factor VIII in a family with mild hemophilia: molecular characterization and response to factor VIII and desmopressin. Thromb Haemost 1995; 74: 619 – 21.en_US
dc.identifier.citedreferenceFranchini M, Girelli D, Olivieri O et al. Tyr2105Cys mutation in exon 22 of FVIII gene is a risk factor for the development of inhibitors in patients with mild/moderate haemophilia A. Haemophilia 2006; 12: 448 – 51.en_US
dc.identifier.citedreferenceThompson AR, Murphy MEP, Liu ML et al. Loss of tolerance to exogenous and endogenous factor VIII in a mild hemophilia A patient with an Arg 593 to Cys mutation. Blood 1997; 90: 1902 – 10.en_US
dc.identifier.citedreferenceJacquemin M, Lavendhomme R, Benhida A et al. Rupture of tolerance to self factor VIII in mild/moderate hemophilia A. Blood 2004; 104: 11 ( abstract 3076 ).en_US
dc.identifier.citedreferenceBril WS, Turenhout EAM, Kaijen PHP et al. Analysis of factor VIII inhibitors in a haemophilia A patient with an Arg 593 →Cys mutation using phage display. Br J Haematol 2002; 119: 393 – 6.en_US
dc.identifier.citedreferenceJacquemin M, Benhida A, Peerlinck K et al. A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor. Blood 2000; 95: 156 – 63.en_US
dc.identifier.citedreferencevan den Brink EN, Timmermans SM, Turenhout EA et al. Longitudinal analysis of factor VIII inhibitors in a previously untreated mild haemophilia A patient with an Arg 593 → Cys substitution. Thromb Haemost 1999; 81: 723 – 6.en_US
dc.identifier.citedreferenceJacquemin 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 – 8.en_US
dc.identifier.citedreferenceJames EA, Kwok WW, Ettinger RA, Thompson AR, Pratt KP. 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 – 407.en_US
dc.identifier.citedreferenceBogdanova N, Markoff A, Eisert R et al. Spectrum of molecular defects and mutation detection rate in patients with mild and moderate hemophilia A. Hum Mutat 2007; 28: 54 – 60.en_US
dc.identifier.citedreferencePipe SW, Kaufman RJ. Structural and functional role of the factor VIII B domain. Haematologica 2004; 89: 8 – 13.en_US
dc.identifier.citedreferenceLiu ML, Shen BW, Nakaya S et al. Hemophilic factor VIII C1- and C2-domain missense mutations and their modeling to the 1.5-angstrom human C2-domain crystal structure. Blood 2000; 96: 979 – 87.en_US
dc.identifier.citedreferenceJacquemin M, Lavend’homme R, Benhida A et al. A novel cause of mild/moderate hemophilia A: mutations scattered in the factor VIII C1 domain reduce factor VIII binding to von Willebrand factor. Blood 2000; 96: 958 – 65.en_US
dc.identifier.citedreferenceMichnick DA, Pittman DD, Wise RJ, Kaufman RJ. Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage. J Biol Chem 1994; 269: 20095 – 102.en_US
dc.identifier.citedreferenceMumford AD, Laffan M, O’Donnell J et al. A Tyr346-->Cys substitution in the interdomain acidic region a1 of factor VIII in an individual with factor VIII:C assay discrepancy. Br J Haematol 2002; 118: 589 – 94.en_US
dc.identifier.citedreferenceLyall H, Hill M, Westby J, Grimley C, Dolan G. Tyr346-->Cys mutation results in factor VIII:C assay discrepancy and a normal bleeding phenotype – is this mild haemophilia A? Haemophilia 2008; 14: 78 – 80.en_US
dc.identifier.citedreferenceRudzki Z, Duncan EM, Casey GJ, Neumann M, Favaloro EJ, Lloyd JV. Mutations in a subgroup of patients with mild haemophilia A and a familial discrepancy between the one-stage and two-stage factor VIII:C methods. Br J Haematol 1996; 94: 400 – 6.en_US
dc.identifier.citedreferencePemberton S, Lindley P, Zaitsev V, Card G, Tuddenham EG, Kemball-Cook G. A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 1997; 89: 2413 – 21.en_US
dc.identifier.citedreferenceSchwaab R, Oldenburg J, Kemball-Cook G et al. Assay discrepancy in mild haemophilia A due to a factor VIII missense mutation (Asn694Ile) in a large Danish family. Br J Haematol 2000; 109: 523 – 8.en_US
dc.identifier.citedreferenceGoodeve AC, Peake IR. The molecular basis of hemophilia A: genotype-phenotype relationships and inhibitor development. Semin Thromb Hemost 2003; 29: 23 – 30.en_US
dc.identifier.citedreferenceRodgers SE, Duncan EM, Barbulescu DM, Quinn DM, Lloyd JV. In vitro kinetics of factor VIII activity in patients with mild haemophilia A and a discrepancy between one-stage and two-stage factor VIII assay results. Br J Haematol 2007; 136: 138 – 45.en_US
dc.identifier.citedreferenceCid AR, CasaÑa P, Cabrera N, Haya S, Cortina V, Aznar JA. Inhibitor development in one patient and laboratory discrepancies in several families with both mild haemophilia and Arg531Cys mutation. Haemophilia 2007; 13: 206 – 8.en_US
dc.identifier.citedreferenceWakabayashi H, Zhou Q, Varfaj F, Fay PJ. A3 domain residue Glu1829 contributes to A2 subunit retention in factor VIIIa. J Thromb Haemost 2007; 5: 996 – 1001.en_US
dc.identifier.citedreferencePipe SW, Saenko EL, Eickhorst AN, Kemball-Cook G, Kaufman RJ. Hemophilia A mutations associated with 1-stage/2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor VIIIa. Blood 2001; 97: 685 – 91.en_US
dc.identifier.citedreferenceKeeling DM, Sukhu K, Kemball-Cook G, Waseem N, Bagnall R, Lloyd JV. Diagnostic importance of the two-stage factor VIII:C assay demonstrated by a case of mild haemophilia associated with His1954-->Leu substitution in the factor VIII A3 domain. Br J Haematol 1999; 105: 1123 – 6.en_US
dc.identifier.citedreferencePratt KP, Shen BW, Takeshima K, Davie EW, Fujikawa K, Stoddard BL. Structure of the C2 domain of human factor VIII at 1.5 A resolution. Nature 1999; 402: 439 – 42.en_US
dc.identifier.citedreferenceMacedo-Ribeiro S, Bode W, Huber R et al. Crystal structures of the membrane-binding C2 domain of human coagulation factor V. Nature 1999; 402: 434 – 9.en_US
dc.identifier.citedreferenceStoilova-McPhie S, Villoutreix BO, Mertens K, Kemball-Cook G, Holzenburg A. 3-Dimensional structure of membrane-bound coagulation factor VIII: modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography. Blood 2002; 99: 1215 – 23.en_US
dc.identifier.citedreferenceSpiegel PC, Murphy P, Stoddard BL. Surface-exposed hemophilic mutations across the factor VIII C2 domain have variable effects on stability and binding activities. J Biol Chem 2004; 279: 53691 – 8.en_US
dc.identifier.citedreferenceAmano K, Sarkar R, Pemberton S, Kemball-Cook G, Kazazian HH Jr, Kaufman RJ. The molecular basis for cross-reacting material-positive hemophilia A due to missense mutations within the A2-domain of factor VIII. Blood 1998; 91: 538 – 48.en_US
dc.identifier.citedreferenceJenkins PV, Freas J, Schmidt KM, Zhou Q, Fay PJ. Mutations associated with hemophilia A in the 558-565 loop of the factor VIIIa A2 subunit alter the catalytic activity of the factor Xase complex. Blood 2002; 100: 501 – 8.en_US
dc.identifier.citedreferenced’Oiron R, Lavergne JM, Lavend’homme R et al. Deletion of alanine 2201 in the FVIII C2 domain results in mild hemophilia A by impairing FVIII binding to VWF and phospholipids and destroys a major FVIII antigenic determinant involved in inhibitor development. Blood 2004; 103: 155 – 7.en_US
dc.identifier.citedreferenceNaylor JA, Green PM, Rizza CR, Giannelli F. Analysis of factor VIII mRNA reveals defects in everyone of 28 haemophilia A patients. Hum Mol Genet 1993; 2: 11 – 17.en_US
dc.identifier.citedreferenceKnobe KE, Villoutreix BO, Tengborn LI, Petrini P, Ljung RC. Factor VIII inhibitors in two families with mild haemophilia A: structural analysis of the mutations. Haemostasis 2000; 30: 268 – 79.en_US
dc.identifier.citedreferencePeerlinck K, Jacquemin MG, Arnout J et al. Antifactor VIII antibody inhibiting allogeneic but not autologous factor VIII in patients with mild hemophilia A. Blood 1999; 93: 2267 – 73.en_US
dc.identifier.citedreferenceLiu ML, Nakaya S, Thompson AR. Non-inversion factor VIII mutations in 80 hemophilia A families including 24 with alloimmune responses. Thromb Haemost 2002; 87: 273 – 6.en_US
dc.identifier.citedreferenceFernÁndez-LÓpez O, GarcÍa-Lozano JR, NÚÑez-VÁzquez R, PÉrez-Garrido R, NÚÑez-RoldÁn A. The spectrum of mutations in Southern Spanish patients with hemophilia A and identification of 28 novel mutations. Haematologica 2005; 90: 707 – 10.en_US
dc.identifier.citedreferenceNaylor JA, Green PM, Montandon AJ, Rizza CR, Giannelli F. Detection of three novel mutations in two haemophilia A patients by rapid screening of whole essential region of factor VIII gene. Lancet 1991; 337: 635 – 9.en_US
dc.identifier.citedreferenceCutler JA, Mitchell MJ, Smith MP, Savidge GF. The identification and classification of 41 novel mutations in the factor VIII gene (F8C). Hum Mutat 2002; 19: 274 – 8.en_US
dc.identifier.citedreferencePieneman WC, Deutz-Terlouw PP, Reitsma PH, BriËt E. Screening for mutations in haemophilia A patients by multiplex PCR-SSCP, Southern blotting and RNA analysis: the detection of a genetic abnormality in the factor VIII gene in 30 out of 35 patients. Br J Haematol 1995; 90: 442 – 9.en_US
dc.identifier.citedreferenceAstermark J, Berntorp E, White GC, Kroner BL, The MIBS Study Group. The MalmÖ International Brother Study (MIBS): further support for genetic predisposition to inhibitor development. Haemophilia 2001; 7: 267 – 72.en_US
dc.identifier.citedreferenceBril WS, MacLean PE, Kaijen PH et al. HLA class II genotype and factor VIII inhibitors in mild haemophilia A patients with an Arg593 to Cys mutation. Haemophilia 2004; 10: 509 – 14.en_US
dc.identifier.citedreferenceAstermark J, Oldenburg J, Pavlova A, Berntorp E, Lefvert AK, MIBS Study Group. Polymorphisms in the IL10 but not in the IL1beta and IL4 genes are associated with inhibitor development in patients with hemophilia A. Blood 2006; 107: 3167 – 72.en_US
dc.identifier.citedreferenceOldenburg J, Schroder J, Brackmann HH, Muller-Reible C, Schwaab R, Tuddenham E. Environmental and genetic factors influencing inhibitor development. Semin Hematol 2004; 41 ( Suppl. 1 ): 82 – 88.en_US
dc.identifier.citedreferenceWhite B, Cotter M, Byrne M, O’Shea E, Smith OP. High responding factor VIII inhibitors in mild haemophilia – is there a link with recent changes in clinical practice? Haemophilia 2000; 6: 113 – 5.en_US
dc.identifier.citedreferenceRoussel-Robert V, Torchet MF, Legrand F, Rothschild C, Stieltjes N. Factor VIII inhibitors development following introduction of B-domain-deleted recombinant factor VIII in four hemophilia A previously treated patients. J Thromb Haemost 2003; 1: 2450 – 1.en_US
dc.identifier.citedreferenceSharatkumar A, Lillicrap D, Blanchette VS et al. Intensive exposure to factor VIII is a risk for inhibitor development in mild hemophilia A. J Thromb Haemost 2003; 1: 1228 – 36.en_US
dc.identifier.citedreferencevon Auer Ch, Oldenburg J, von Depka M et al. Inhibitor development in patients with hemophilia A after continuous infusion of FVIII concentrates. Ann N Y Acad Sci 2005; 1051: 498 – 505.en_US
dc.identifier.citedreferenceMatzinger P. The danger model: a renewed sense of self. Science 2002; 296: 301 – 5.en_US
dc.identifier.citedreferenceRobbins D, Kulkarni R, Gera R, Scott-Emuakpor AB, Bosma K, Penner JA. Successful treatment of high titer inhibitors in mild hemophilia A with avoidance of factor VIII and immunosuppressive therapy. Am J Hematol 2001; 68: 184 – 8.en_US
dc.identifier.citedreferenceVlot AJ, Wittebol S, Strengers PF et al. Factor VIII inhibitor in a patient with mild haemophilia A and an Asn618-->Ser mutation responsive to immune tolerance induction and cyclophosphamide. Br J Haematol 2002; 117: 136 – 40.en_US
dc.identifier.citedreferenceWiestner A, Cho HJ, Asch AS, Michells MA, Zeller JA, Peerschke EIB. Rituximab in the treatment of acquired factor VIII inhibitors. Blood 2002; 100: 3426 – 8.en_US
dc.identifier.citedreferenceCarcao M, St Louis J, Poon MC et al. Inhibitor Subcommittee of Association of Hemophilia Clinic Directors of Canada. Rituximab for congenital haemophiliacs with inhibitors: a Canadian experience. Haemophilia 2006; 12: 7 – 18.en_US
dc.identifier.citedreferenceDunkley S, Kershaw G, Young G et al. Rituximab treatment of mild haemophilia A with inhibitors: a proposed treatment protocol. Haemophilia 2006; 12: 663 – 7.en_US
dc.identifier.citedreferenceLeebeek FWG, Kappers-Klunne MC, Jie KSG. Effective and safe use of recombinant factor VIIa (NovoSeven ® ) in elderly mild haemophilia A patients with high-titre antibodies against factor VIII. Haemophilia 2004; 10: 250 – 3.en_US
dc.identifier.citedreferenced’Oiron R, Volot F, Reynaud J et al. Impact of choice of treatment for bleeding episodes on inhibitor outcome in patients with mild/moderate hemophilia A and inhibitors. Semin Hematol 2006; 43: S3 – S9.en_US
dc.identifier.citedreferenceVanderlugt CJ, Miller SD. Epitope spreading. Curr-Opin-Immunol 1996; 8: 831 – 6.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.