메뉴 건너뛰기




Volumn 23, Issue 2, 2016, Pages 86-97

Novel conformation-specific monoclonal antibodies against amyloidogenic forms of transthyretin

Author keywords

Aggregation; cardiac; clearance; cryptotope; fibrils; immunotherapy; protein misfolding

Indexed keywords

AMYLOID PROTEIN; MONOCLONAL ANTIBODY; PREALBUMIN; ANTIGEN ANTIBODY COMPLEX; EPITOPE; PROTEIN AGGREGATE; RECOMBINANT PROTEIN;

EID: 84961203344     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.3109/13506129.2016.1148025     Document Type: Article
Times cited : (71)

References (45)
  • 1
    • 79955842001 scopus 로고    scopus 로고
    • Amyloidosis: pathogenesis and new therapeutic options
    • G.Merlini, D.C.Seldin, M.A.Gertz Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol 2011;29:1924–33
    • (2011) J Clin Oncol , vol.29 , pp. 1924-1933
    • Merlini, G.1    Seldin, D.C.2    Gertz, M.A.3
  • 2
    • 84907416004 scopus 로고    scopus 로고
    • Recent advances in transthyretin amyloidosis therapy
    • M.Ueda, Y.Ando Recent advances in transthyretin amyloidosis therapy. Transl Neurodegener 2014;3:19
    • (2014) Transl Neurodegener , vol.3 , pp. 19
    • Ueda, M.1    Ando, Y.2
  • 3
    • 84940703039 scopus 로고    scopus 로고
    • Transthyretin (ATTR) amyloidosis: clinical spectrum, molecular pathogenesis and disease-modifying treatments
    • Y.Sekijima Transthyretin (ATTR) amyloidosis: clinical spectrum, molecular pathogenesis and disease-modifying treatments. J Neurol Neurosurg Psychiatry 2015;86:1036–43
    • (2015) J Neurol Neurosurg Psychiatry , vol.86 , pp. 1036-1043
    • Sekijima, Y.1
  • 10
    • 0027312398 scopus 로고
    • Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis
    • G.Holmgren, B.G.Ericzon, C.G.Groth, L.Steen, O.Suhr, O.Andersen, B.G.Wallin,. Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis. Lancet 1993;341:1113–16
    • (1993) Lancet , vol.341 , pp. 1113-1116
    • Holmgren, G.1    Ericzon, B.G.2    Groth, C.G.3    Steen, L.4    Suhr, O.5    Andersen, O.6    Wallin, B.G.7
  • 15
    • 84861451481 scopus 로고    scopus 로고
    • Clinical development of an antisense therapy for the treatment of transthyretin-associated polyneuropathy
    • E.J.Ackermann, S.Guo, S.Booten, L.Alvarado, M.Benson, S.Hughes, B.P.Monia Clinical development of an antisense therapy for the treatment of transthyretin-associated polyneuropathy. Amyloid 2012;19:43–4
    • (2012) Amyloid , vol.19 , pp. 43-44
    • Ackermann, E.J.1    Guo, S.2    Booten, S.3    Alvarado, L.4    Benson, M.5    Hughes, S.6    Monia, B.P.7
  • 16
    • 84860697106 scopus 로고    scopus 로고
    • Methods to evaluate the inhibition of TTR fibrillogenesis induced by small ligands
    • G.Arsequell, A.Planas Methods to evaluate the inhibition of TTR fibrillogenesis induced by small ligands. Curr Med Chem 2012;19:2343–55
    • (2012) Curr Med Chem , vol.19 , pp. 2343-2355
    • Arsequell, G.1    Planas, A.2
  • 17
    • 0014336534 scopus 로고
    • Retinol-binding protein: the transport protein for vitamin A in human plasma
    • M.Kanai, A.Raz, D.S.Goodman Retinol-binding protein: the transport protein for vitamin A in human plasma. J Clin Invest 1968;47:2025–44
    • (1968) J Clin Invest , vol.47 , pp. 2025-2044
    • Kanai, M.1    Raz, A.2    Goodman, D.S.3
  • 18
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • X.Jiang, J.N.Buxbaum, J.W.Kelly The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci USA. 2001;98:14943–8
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 19
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • J.W.Kelly Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 1996;6:11–17
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 20
    • 84907938241 scopus 로고    scopus 로고
    • Antibodies and protein misfolding: from structural research tools to therapeutic strategies
    • E.De Genst, A.Messer, C.M.Dobson Antibodies and protein misfolding: from structural research tools to therapeutic strategies. Biochim Biophys Acta 2014;1844:1907–19
    • (2014) Biochim Biophys Acta , vol.1844 , pp. 1907-1919
    • De Genst, E.1    Messer, A.2    Dobson, C.M.3
  • 21
    • 84871601016 scopus 로고    scopus 로고
    • AL amyloid imaging and therapy with a monoclonal antibody to a cryptic epitope on amyloid fibrils
    • J.S.Wall, S.J.Kennel, A.Williams, T.Richey, A.Stuckey, Y.Huang, S.Macy,. AL amyloid imaging and therapy with a monoclonal antibody to a cryptic epitope on amyloid fibrils. PLoS One 2012;7:e52686
    • (2012) PLoS One , vol.7 , pp. e52686
    • Wall, J.S.1    Kennel, S.J.2    Williams, A.3    Richey, T.4    Stuckey, A.5    Huang, Y.6    Macy, S.7
  • 22
    • 84875244684 scopus 로고    scopus 로고
    • Impact of antibodies against amyloidogenic transthyretin (ATTR) on phenotypes of patients with familial amyloidotic polyneuropathy (FAP) ATTR Valine30Methionine
    • K.Obayashi, M.Tasaki, H.Jono, M.Ueda, S.Shinriki, Y.Misumi, T.Yamashita,. Impact of antibodies against amyloidogenic transthyretin (ATTR) on phenotypes of patients with familial amyloidotic polyneuropathy (FAP) ATTR Valine30Methionine. Clin Chim Acta 2013;419:127–31
    • (2013) Clin Chim Acta , vol.419 , pp. 127-131
    • Obayashi, K.1    Tasaki, M.2    Jono, H.3    Ueda, M.4    Shinriki, S.5    Misumi, Y.6    Yamashita, T.7
  • 24
    • 32844473029 scopus 로고    scopus 로고
    • Immunization in familial amyloidotic polyneuropathy: counteracting deposition by immunization with a Y78F TTR mutant
    • H.Terazaki, Y.Ando, R.Fernandes, K.Yamamura, S.Maeda, M.J.Saraiva Immunization in familial amyloidotic polyneuropathy: counteracting deposition by immunization with a Y78F TTR mutant. Lab Invest 2006;86:23–31
    • (2006) Lab Invest , vol.86 , pp. 23-31
    • Terazaki, H.1    Ando, Y.2    Fernandes, R.3    Yamamura, K.4    Maeda, S.5    Saraiva, M.J.6
  • 25
    • 0028260652 scopus 로고
    • Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations
    • Å.Gustavsson, U.Engström, P.Westermark Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations. Am J Pathol 1994;144:1301–11
    • (1994) Am J Pathol , vol.144 , pp. 1301-1311
    • Gustavsson, Å.1    Engström, U.2    Westermark, P.3
  • 26
    • 0034657815 scopus 로고    scopus 로고
    • Designing transthyretin mutants affecting tetrameric structure: implications in amyloidogenicity
    • C.Redondo, A.M.Damas, M.J.M.Saraiva Designing transthyretin mutants affecting tetrameric structure: implications in amyloidogenicity. Biochem J 2000;348:167–72
    • (2000) Biochem J , vol.348 , pp. 167-172
    • Redondo, C.1    Damas, A.M.2    Saraiva, M.J.M.3
  • 27
    • 84899000210 scopus 로고    scopus 로고
    • Transthyretin aggregate-specific antibodies recognize cryptic epitopes on patient-derived amyloid fibrils
    • M.Phay, V.Blinder, S.Macy, M.J.Greene, D.C.Wooliver, W.Liu, A.Planas,. Transthyretin aggregate-specific antibodies recognize cryptic epitopes on patient-derived amyloid fibrils. Rejuvenation Res 2014;17:97–104
    • (2014) Rejuvenation Res , vol.17 , pp. 97-104
    • Phay, M.1    Blinder, V.2    Macy, S.3    Greene, M.J.4    Wooliver, D.C.5    Liu, W.6    Planas, A.7
  • 30
    • 0034405428 scopus 로고    scopus 로고
    • Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils
    • C.Redondo, A.M.Damas, A.Olofsson, E.Lundgren, M.J.M.Saraiva Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils. J Mol Biol 2000;304:461–70
    • (2000) J Mol Biol , vol.304 , pp. 461-470
    • Redondo, C.1    Damas, A.M.2    Olofsson, A.3    Lundgren, E.4    Saraiva, M.J.M.5
  • 31
    • 46049085810 scopus 로고    scopus 로고
    • Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis
    • A.R.Hurshman Babbes, E.T.Powers, J.W.Kelly Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis. Biochemistry 2008;47:6969–84
    • (2008) Biochemistry , vol.47 , pp. 6969-6984
    • Hurshman Babbes, A.R.1    Powers, E.T.2    Kelly, J.W.3
  • 33
    • 0029087813 scopus 로고
    • Chemical and immunological heterogeneity of fibrillar amyloid in plaques of Alzheimer's disease and Down's syndrome brains revealed by confocal microscopy
    • M.L.Schmidt, K.A.Robinson, V.M.Lee, J.Q.Trojanowski Chemical and immunological heterogeneity of fibrillar amyloid in plaques of Alzheimer's disease and Down's syndrome brains revealed by confocal microscopy. Am J Pathol 1995;147:503–15
    • (1995) Am J Pathol , vol.147 , pp. 503-515
    • Schmidt, M.L.1    Robinson, K.A.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 34
    • 84927556020 scopus 로고    scopus 로고
    • Binding of TDP-43 to the 3'UTR of its cognate mRNA enhances its solubility
    • Y.Sun, P.E.Arslan, A.Won, C.M.Yip, A.Chakrabartty Binding of TDP-43 to the 3'UTR of its cognate mRNA enhances its solubility. Biochemistry 2014;53:5885–94
    • (2014) Biochemistry , vol.53 , pp. 5885-5894
    • Sun, Y.1    Arslan, P.E.2    Won, A.3    Yip, C.M.4    Chakrabartty, A.5
  • 35
    • 18944407388 scopus 로고    scopus 로고
    • Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death
    • M.Wogulis, S.Wright, D.Cunningham, T.Chilcote, K.Powell, R.E.Rydel Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death. J Neurosci 2005;25:1071–80
    • (2005) J Neurosci , vol.25 , pp. 1071-1080
    • Wogulis, M.1    Wright, S.2    Cunningham, D.3    Chilcote, T.4    Powell, K.5    Rydel, R.E.6
  • 36
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • W.-F.Xue, S.W.Homans, S.E.Radford Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc. Natl. Acad. Sci. U.S.A. 2008;105:8926–31
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 8926-8931
    • Xue, W.-F.1    Homans, S.W.2    Radford, S.E.3
  • 39
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid β peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • F.Bard, C.Cannon, R.Barbour, R.-L.Burke, D.Games, H.Grajeda, T.Guido,. Peripherally administered antibodies against amyloid β peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 2000;6:916–19
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.-L.4    Games, D.5    Grajeda, H.6    Guido, T.7
  • 42
    • 84875784710 scopus 로고    scopus 로고
    • Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERAD
    • A.C.Teixeira, M.J.Saraiva Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERAD. J Cell Mol Med 2013;17:429–35
    • (2013) J Cell Mol Med , vol.17 , pp. 429-435
    • Teixeira, A.C.1    Saraiva, M.J.2
  • 44
    • 84963532664 scopus 로고    scopus 로고
    • First in human phase I/II study of NEOD001 in patients with light chain amyloidosis and persistent organ dysfunction
    • [Epub ahead of print]
    • M.Gertz, H.Landau, R.L.Comenzo, D.Seldin, B.Weiss, J.Zonder, G.Merlini,. First in human phase I/II study of NEOD001 in patients with light chain amyloidosis and persistent organ dysfunction. J Clin Oncol 2016; [Epub ahead of print]. DOI: 10.1200/JCO.2015.63.6530
    • (2016) J Clin Oncol
    • Gertz, M.1    Landau, H.2    Comenzo, R.L.3    Seldin, D.4    Weiss, B.5    Zonder, J.6    Merlini, G.7
  • 45
    • 84865849112 scopus 로고    scopus 로고
    • Transthyretin (TTR) cardiac amyloidosis
    • F.L.Ruberg, J.L.Berk Transthyretin (TTR) cardiac amyloidosis. Circulation 2012;126:1286–300
    • (2012) Circulation , vol.126 , pp. 1286-1300
    • Ruberg, F.L.1    Berk, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.