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Volumn 7, Issue 12, 2012, Pages

AL Amyloid Imaging and Therapy with a Monoclonal Antibody to a Cryptic Epitope on Amyloid Fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID A PROTEIN; ANTIGEN; ASPARTIC ACID; CRYPTIC EPITOPE; EPITOPE; GLUTAMIC ACID; IODINE 131; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 2A4; MONOCLONAL ANTIBODY 2A4 I 131; UNCLASSIFIED DRUG;

EID: 84871601016     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052686     Document Type: Article
Times cited : (69)

References (48)
  • 1
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • Merlini G, Bellotti V, (2003) Molecular mechanisms of amyloidosis. N Engl J Med 349: 583-596.
    • (2003) N Engl J Med , vol.349 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 2
    • 84861480962 scopus 로고    scopus 로고
    • What do I need to know about immunoglobulin light chain (AL) amyloidosis
    • Dispenzieri A, Gertz MA, Buadi F, (2012) What do I need to know about immunoglobulin light chain (AL) amyloidosis? Blood Rev 26: 137-154.
    • (2012) Blood Rev , vol.26 , pp. 137-154
    • Dispenzieri, A.1    Gertz, M.A.2    Buadi, F.3
  • 3
    • 84860643971 scopus 로고    scopus 로고
    • Revised prognostic staging system for light chain amyloidosis incorporating cardiac biomarkers and serum free light chain measurements
    • Kumar S, Dispenzieri A, Lacy MQ, Hayman SR, Buadi FK, et al. (2012) Revised prognostic staging system for light chain amyloidosis incorporating cardiac biomarkers and serum free light chain measurements. J Clin Oncol 30: 989-995.
    • (2012) J Clin Oncol , vol.30 , pp. 989-995
    • Kumar, S.1    Dispenzieri, A.2    Lacy, M.Q.3    Hayman, S.R.4    Buadi, F.K.5
  • 4
    • 77956196131 scopus 로고    scopus 로고
    • Prognosis assessment of cardiac involvement in systemic AL amyloidosis by magnetic resonance imaging
    • Mekinian A, Lions C, Leleu X, Duhamel A, Lamblin N, et al. (2010) Prognosis assessment of cardiac involvement in systemic AL amyloidosis by magnetic resonance imaging. Am J Med 123: 864-868.
    • (2010) Am J Med , vol.123 , pp. 864-868
    • Mekinian, A.1    Lions, C.2    Leleu, X.3    Duhamel, A.4    Lamblin, N.5
  • 8
    • 0037107177 scopus 로고    scopus 로고
    • Non-Fc-mediated mechanisms are involved in clearance of amyloid-beta in vivo by immunotherapy
    • Bacskai BJ, Kajdasz ST, McLellan ME, Games D, Seubert P, et al. (2002) Non-Fc-mediated mechanisms are involved in clearance of amyloid-beta in vivo by immunotherapy. J Neurosci 22: 7873-7878.
    • (2002) J Neurosci , vol.22 , pp. 7873-7878
    • Bacskai, B.J.1    Kajdasz, S.T.2    McLellan, M.E.3    Games, D.4    Seubert, P.5
  • 9
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R, Burke RL, Games D, et al. (2000) Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 6: 916-919.
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5
  • 10
    • 49049089830 scopus 로고    scopus 로고
    • Immunotherapy reduces vascular amyloid-beta in PDAPP mice
    • Schroeter S, Khan K, Barbour R, Doan M, Chen M, et al. (2008) Immunotherapy reduces vascular amyloid-beta in PDAPP mice. J Neurosci 28: 6787-6793.
    • (2008) J Neurosci , vol.28 , pp. 6787-6793
    • Schroeter, S.1    Khan, K.2    Barbour, R.3    Doan, M.4    Chen, M.5
  • 11
    • 40449086748 scopus 로고    scopus 로고
    • Progress in the active immunotherapeutic approach to Alzheimer's disease: clinical investigations into AN1792-associated meningoencephalitis
    • Pride M, Seubert P, Grundman M, Hagen M, Eldridge J, et al. (2008) Progress in the active immunotherapeutic approach to Alzheimer's disease: clinical investigations into AN1792-associated meningoencephalitis. Neurodegener Dis 5: 194-196.
    • (2008) Neurodegener Dis , vol.5 , pp. 194-196
    • Pride, M.1    Seubert, P.2    Grundman, M.3    Hagen, M.4    Eldridge, J.5
  • 12
    • 0033810109 scopus 로고    scopus 로고
    • Antibody-mediated resolution of light chain-associated amyloid deposits
    • Hrncic R, Wall J, Wolfenbarger DA, Murphy CL, Schell M, et al. (2000) Antibody-mediated resolution of light chain-associated amyloid deposits. Am J Pathol 157: 1239-1246.
    • (2000) Am J Pathol , vol.157 , pp. 1239-1246
    • Hrncic, R.1    Wall, J.2    Wolfenbarger, D.A.3    Murphy, C.L.4    Schell, M.5
  • 15
    • 77957707133 scopus 로고    scopus 로고
    • Radioimmunodetection of amyloid deposits in patients with AL amyloidosis
    • Wall JS, Kennel SJ, Stuckey AC, Long MJ, Townsend DW, et al. (2010) Radioimmunodetection of amyloid deposits in patients with AL amyloidosis. Blood 116: 2241-2244.
    • (2010) Blood , vol.116 , pp. 2241-2244
    • Wall, J.S.1    Kennel, S.J.2    Stuckey, A.C.3    Long, M.J.4    Townsend, D.W.5
  • 16
    • 0036931760 scopus 로고    scopus 로고
    • Diagnostic tools for amyloidosis
    • Hachulla E, Grateau G, (2002) Diagnostic tools for amyloidosis. Joint Bone Spine 69: 538-545.
    • (2002) Joint Bone Spine , vol.69 , pp. 538-545
    • Hachulla, E.1    Grateau, G.2
  • 17
    • 0030199312 scopus 로고    scopus 로고
    • Prospective and serial study of primary amyloidosis with serum amyloid P component scintigraphy: from diagnosis to prognosis
    • Hachulla E, Maulin L, Deveaux M, Facon T, Bletry O, et al. (1996) Prospective and serial study of primary amyloidosis with serum amyloid P component scintigraphy: from diagnosis to prognosis. Am J Med 101: 77-87.
    • (1996) Am J Med , vol.101 , pp. 77-87
    • Hachulla, E.1    Maulin, L.2    Deveaux, M.3    Facon, T.4    Bletry, O.5
  • 18
    • 0025025397 scopus 로고
    • Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component
    • Hawkins PN, Lavender JP, Pepys MB, (1990) Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component. N Engl J Med 323: 508-513.
    • (1990) N Engl J Med , vol.323 , pp. 508-513
    • Hawkins, P.N.1    Lavender, J.P.2    Pepys, M.B.3
  • 19
    • 0025694826 scopus 로고
    • Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis
    • Hawkins PN, Wootton R, Pepys MB, (1990) Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis. J Clin Invest 86: 1862-1869.
    • (1990) J Clin Invest , vol.86 , pp. 1862-1869
    • Hawkins, P.N.1    Wootton, R.2    Pepys, M.B.3
  • 20
    • 33645237311 scopus 로고    scopus 로고
    • Diagnostic performance of 123I-labeled serum amyloid P component scintigraphy in patients with amyloidosis
    • Hazenberg BP, van Rijswijk MH, Piers DA, Lub-de Hooge MN, Vellenga E, et al. (2006) Diagnostic performance of 123I-labeled serum amyloid P component scintigraphy in patients with amyloidosis. Am J Med 119: 355 e315-324.
    • (2006) Am J Med , vol.119
    • Hazenberg, B.P.1    van Rijswijk, M.H.2    Piers, D.A.3    Lub-de Hooge, M.N.4    Vellenga, E.5
  • 21
    • 0027518596 scopus 로고
    • Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis
    • Saile R, Deveaux M, Hachulla E, Descamps J, Duquesnoy B, et al. (1993) Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis. Eur J Nucl Med 20: 130-137.
    • (1993) Eur J Nucl Med , vol.20 , pp. 130-137
    • Saile, R.1    Deveaux, M.2    Hachulla, E.3    Descamps, J.4    Duquesnoy, B.5
  • 23
    • 84871540796 scopus 로고    scopus 로고
    • Generation and Characterization of Anti-AA Amyloid-Specific Monoclonal Antibodies
    • Wall JS, Kennel SJ, Richey T, Allen A, Stuckey A, et al. (2011) Generation and Characterization of Anti-AA Amyloid-Specific Monoclonal Antibodies. Front Immunol 2: 32.
    • (2011) Front Immunol , vol.2 , pp. 32
    • Wall, J.S.1    Kennel, S.J.2    Richey, T.3    Allen, A.4    Stuckey, A.5
  • 24
    • 65549097567 scopus 로고    scopus 로고
    • Current perspectives on familial Mediterranean fever
    • Guz G, Kanbay M, Ozturk MA, (2009) Current perspectives on familial Mediterranean fever. Curr Opin Infect Dis 22: 309-315.
    • (2009) Curr Opin Infect Dis , vol.22 , pp. 309-315
    • Guz, G.1    Kanbay, M.2    Ozturk, M.A.3
  • 26
    • 83455173669 scopus 로고    scopus 로고
    • Amyloid A amyloidosis secondary to rheumatoid arthritis: pathophysiology and treatments
    • Nakamura T, (2011) Amyloid A amyloidosis secondary to rheumatoid arthritis: pathophysiology and treatments. Clin Exp Rheumatol 29: 850-857.
    • (2011) Clin Exp Rheumatol , vol.29 , pp. 850-857
    • Nakamura, T.1
  • 27
    • 37649019187 scopus 로고    scopus 로고
    • Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils
    • Habicht G, Haupt C, Friedrich RP, Hortschansky P, Sachse C, et al. (2007) Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils. Proc Natl Acad Sci U S A 104: 19232-19237.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19232-19237
    • Habicht, G.1    Haupt, C.2    Friedrich, R.P.3    Hortschansky, P.4    Sachse, C.5
  • 28
    • 79953891845 scopus 로고    scopus 로고
    • Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils
    • Haupt C, Bereza M, Kumar ST, Kieninger B, Morgado I, et al. (2011) Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils. J Mol Biol 408: 529-540.
    • (2011) J Mol Biol , vol.408 , pp. 529-540
    • Haupt, C.1    Bereza, M.2    Kumar, S.T.3    Kieninger, B.4    Morgado, I.5
  • 29
    • 78650857643 scopus 로고    scopus 로고
    • Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions
    • Haupt C, Morgado I, Kumar ST, Parthier C, Bereza M, et al. (2011) Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions. J Mol Biol 405: 341-348.
    • (2011) J Mol Biol , vol.405 , pp. 341-348
    • Haupt, C.1    Morgado, I.2    Kumar, S.T.3    Parthier, C.4    Bereza, M.5
  • 30
    • 33749507375 scopus 로고    scopus 로고
    • Conformation-dependent anti-amyloid oligomer antibodies
    • Kayed R, Glabe CG, (2006) Conformation-dependent anti-amyloid oligomer antibodies. Methods Enzymol 413: 326-344.
    • (2006) Methods Enzymol , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 31
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R, (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci U S A 99: 1485-1490.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 32
    • 0345426278 scopus 로고    scopus 로고
    • Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity
    • Wall J, Schell M, Murphy C, Hrncic R, Stevens FJ, et al. (1999) Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity. Biochemistry 38: 14101-14108.
    • (1999) Biochemistry , vol.38 , pp. 14101-14108
    • Wall, J.1    Schell, M.2    Murphy, C.3    Hrncic, R.4    Stevens, F.J.5
  • 34
    • 34250335813 scopus 로고    scopus 로고
    • Radioimaging of Light Chain Amyloid with a Fibril-Reactive Monoclonal Antibody
    • Wall JS, Kennel SJ, Paulus M, Gregor J, Richey T, et al. (2006) Radioimaging of Light Chain Amyloid with a Fibril-Reactive Monoclonal Antibody. J Nucl Med 47: 2016-2024.
    • (2006) J Nucl Med , vol.47 , pp. 2016-2024
    • Wall, J.S.1    Kennel, S.J.2    Paulus, M.3    Gregor, J.4    Richey, T.5
  • 35
    • 35548957417 scopus 로고    scopus 로고
    • Eprodisate slows the progression of renal disease in patients with AA amyloidosis
    • Rule AD, Leung N, (2007) Eprodisate slows the progression of renal disease in patients with AA amyloidosis. Nat Clin Pract Nephrol 3: 592-593.
    • (2007) Nat Clin Pract Nephrol , vol.3 , pp. 592-593
    • Rule, A.D.1    Leung, N.2
  • 36
    • 84857772012 scopus 로고    scopus 로고
    • Review of eprodisate for the treatment of renal disease in AA amyloidosis
    • Rumjon A, Coats T, Javaid MM, (2012) Review of eprodisate for the treatment of renal disease in AA amyloidosis. Int J Nephrol Renovasc Dis 5: 37-43.
    • (2012) Int J Nephrol Renovasc Dis , vol.5 , pp. 37-43
    • Rumjon, A.1    Coats, T.2    Javaid, M.M.3
  • 37
    • 6944240027 scopus 로고    scopus 로고
    • Liver transplantation in transthyretin-related familial amyloid polyneuropathy
    • Stangou AJ, Hawkins PN, (2004) Liver transplantation in transthyretin-related familial amyloid polyneuropathy. Curr Opin Neurol 17: 615-620.
    • (2004) Curr Opin Neurol , vol.17 , pp. 615-620
    • Stangou, A.J.1    Hawkins, P.N.2
  • 39
    • 26844534980 scopus 로고    scopus 로고
    • Selective silencing of a mutant transthyretin allele by small interfering RNAs
    • Kurosawa T, Igarashi S, Nishizawa M, Onodera O, (2005) Selective silencing of a mutant transthyretin allele by small interfering RNAs. Biochem Biophys Res Commun 337: 1012-1018.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 1012-1018
    • Kurosawa, T.1    Igarashi, S.2    Nishizawa, M.3    Onodera, O.4
  • 40
    • 78650228593 scopus 로고    scopus 로고
    • Inhibition of pathologic immunoglobulin-free light chain production by small interfering RNA molecules
    • Phipps JE, Kestler DP, Foster JS, Kennel SJ, Donnell R, et al. (2010) Inhibition of pathologic immunoglobulin-free light chain production by small interfering RNA molecules. Exp Hematol 38: 1006-1013.
    • (2010) Exp Hematol , vol.38 , pp. 1006-1013
    • Phipps, J.E.1    Kestler, D.P.2    Foster, J.S.3    Kennel, S.J.4    Donnell, R.5
  • 41
    • 77949300796 scopus 로고    scopus 로고
    • 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: a phase 2, double-blind, placebo-controlled, ascending-dose study
    • Rinne JO, Brooks DJ, Rossor MN, Fox NC, Bullock R, et al. (2010) 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: a phase 2, double-blind, placebo-controlled, ascending-dose study. Lancet Neurol 9: 363-372.
    • (2010) Lancet Neurol , vol.9 , pp. 363-372
    • Rinne, J.O.1    Brooks, D.J.2    Rossor, M.N.3    Fox, N.C.4    Bullock, R.5
  • 42
    • 19944429065 scopus 로고    scopus 로고
    • Abeta vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
    • Masliah E, Hansen L, Adame A, Crews L, Bard F, et al. (2005) Abeta vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease. Neurology 64: 129-131.
    • (2005) Neurology , vol.64 , pp. 129-131
    • Masliah, E.1    Hansen, L.2    Adame, A.3    Crews, L.4    Bard, F.5
  • 43
    • 84857261943 scopus 로고    scopus 로고
    • Neutralization of soluble, synaptotoxic amyloid beta species by antibodies is epitope specific
    • Zago W, Buttini M, Comery TA, Nishioka C, Gardai SJ, et al. (2012) Neutralization of soluble, synaptotoxic amyloid beta species by antibodies is epitope specific. J Neurosci 32: 2696-2702.
    • (2012) J Neurosci , vol.32 , pp. 2696-2702
    • Zago, W.1    Buttini, M.2    Comery, T.A.3    Nishioka, C.4    Gardai, S.J.5
  • 44
    • 78149282151 scopus 로고    scopus 로고
    • Antibodies to human serum amyloid P component eliminate visceral amyloid deposits
    • Bodin K, Ellmerich S, Kahan MC, Tennent GA, Loesch A, et al. (2010) Antibodies to human serum amyloid P component eliminate visceral amyloid deposits. Nature 468: 93-97.
    • (2010) Nature , vol.468 , pp. 93-97
    • Bodin, K.1    Ellmerich, S.2    Kahan, M.C.3    Tennent, G.A.4    Loesch, A.5
  • 46
    • 0033214526 scopus 로고    scopus 로고
    • Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain
    • Davis DP, Khurana R, Meredith S, Stevens FJ, Argon Y, (1999) Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain. J Immunol 163: 3842-3850.
    • (1999) J Immunol , vol.163 , pp. 3842-3850
    • Davis, D.P.1    Khurana, R.2    Meredith, S.3    Stevens, F.J.4    Argon, Y.5
  • 47
    • 0033715831 scopus 로고    scopus 로고
    • Inhibition of amyloid fiber assembly by both BiP and its target peptide
    • Davis PD, Raffen R, Dul LJ, Vogen MS, Williamson KE, et al. (2000) Inhibition of amyloid fiber assembly by both BiP and its target peptide. Immunity 13: 433-442.
    • (2000) Immunity , vol.13 , pp. 433-442
    • Davis, P.D.1    Raffen, R.2    Dul, L.J.3    Vogen, M.S.4    Williamson, K.E.5
  • 48
    • 1942472616 scopus 로고    scopus 로고
    • Freeze-drying of proteins: some emerging concerns
    • Roy I, Gupta MN, (2004) Freeze-drying of proteins: some emerging concerns. Biotechnol Appl Biochem 39: 165-177.
    • (2004) Biotechnol Appl Biochem , vol.39 , pp. 165-177
    • Roy, I.1    Gupta, M.N.2


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