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Volumn 7, Issue 9, 2012, Pages

Stability of the Transthyretin Molecule as a Key Factor in the Interaction with A-Beta Peptide - Relevance in Alzheimer's Disease

Author keywords

[No Author keywords available]

Indexed keywords

2 (3,5 DICHLOROPHENYL)AMINO; 4 (3,5 DIFLUOROPHENYL); AMYLOID BETA PROTEIN; FLUFENAMIC ACID; GENISTEIN; PREALBUMIN; THYROXINE; UNCLASSIFIED DRUG;

EID: 84866460552     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0045368     Document Type: Article
Times cited : (39)

References (46)
  • 2
    • 0028856460 scopus 로고
    • An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde"
    • Alzheimer A, Stelzmann RA, Schnitzlein HN, Murtagh FR, (1995) An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde". Clinical anatomy 8: 429-431.
    • (1995) Clinical Anatomy , vol.8 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Schnitzlein, H.N.3    Murtagh, F.R.4
  • 3
    • 0037126952 scopus 로고    scopus 로고
    • Increased tau phosphorylation but absence of formation of neurofibrillary tangles in mice double transgenic for human tau and Alzheimer mutant (M146L) presenilin-1
    • Boutajangout A, Leroy K, Touchet N, Authelet M, Blanchard V, et al. (2002) Increased tau phosphorylation but absence of formation of neurofibrillary tangles in mice double transgenic for human tau and Alzheimer mutant (M146L) presenilin-1. Neuroscience letters 318: 29-33.
    • (2002) Neuroscience Letters , vol.318 , pp. 29-33
    • Boutajangout, A.1    Leroy, K.2    Touchet, N.3    Authelet, M.4    Blanchard, V.5
  • 6
    • 40149086952 scopus 로고    scopus 로고
    • Transthyretin binding to A-Beta peptide-impact on A-Beta fibrillogenesis and toxicity
    • Costa R, Goncalves A, Saraiva MJ, Cardoso I, (2008) Transthyretin binding to A-Beta peptide-impact on A-Beta fibrillogenesis and toxicity. FEBS letters 582: 936-942.
    • (2008) FEBS Letters , vol.582 , pp. 936-942
    • Costa, R.1    Goncalves, A.2    Saraiva, M.J.3    Cardoso, I.4
  • 7
    • 51449096179 scopus 로고    scopus 로고
    • Transthyretin protects against A-beta peptide toxicity by proteolytic cleavage of the peptide: a mechanism sensitive to the Kunitz protease inhibitor
    • Costa R, Ferreira-da-Silva F, Saraiva MJ, Cardoso I, (2008) Transthyretin protects against A-beta peptide toxicity by proteolytic cleavage of the peptide: a mechanism sensitive to the Kunitz protease inhibitor. PLoS One 3: e2899.
    • (2008) PLoS One , vol.3
    • Costa, R.1    Ferreira-da-Silva, F.2    Saraiva, M.J.3    Cardoso, I.4
  • 8
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation
    • Lashuel HA, Lai Z, Kelly JW, (1998) Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 37: 17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 9
    • 0015218747 scopus 로고
    • Evidence for multiple thyroxine-binding sites in human prealbumin
    • Nilsson SF, Peterson PA, (1971) Evidence for multiple thyroxine-binding sites in human prealbumin. The Journal of biological chemistry 246: 6098-6105.
    • (1971) The Journal of Biological Chemistry , vol.246 , pp. 6098-6105
    • Nilsson, S.F.1    Peterson, P.A.2
  • 11
    • 0029062667 scopus 로고
    • Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
    • Monaco HL, Rizzi M, Coda A, (1995) Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science 268: 1039-1041.
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 12
    • 0027363264 scopus 로고
    • Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
    • McCutchen SL, Colon W, Kelly JW, (1993) Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32: 12119-12127.
    • (1993) Biochemistry , vol.32 , pp. 12119-12127
    • McCutchen, S.L.1    Colon, W.2    Kelly, J.W.3
  • 13
    • 0031684499 scopus 로고    scopus 로고
    • Discovering transthyretin amyloid fibril inhibitors by limited screening
    • Baures PW, Peterson SA, Kelly JW, (1998) Discovering transthyretin amyloid fibril inhibitors by limited screening. Bioorganic & medicinal chemistry 6: 1389-1401.
    • (1998) Bioorganic & Medicinal Chemistry , vol.6 , pp. 1389-1401
    • Baures, P.W.1    Peterson, S.A.2    Kelly, J.W.3
  • 14
    • 0037122698 scopus 로고    scopus 로고
    • Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors
    • Oza VB, Smith C, Raman P, Koepf EK, Lashuel HA, et al. (2002) Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors. Journal of medicinal chemistry 45: 321-332.
    • (2002) Journal of Medicinal Chemistry , vol.45 , pp. 321-332
    • Oza, V.B.1    Smith, C.2    Raman, P.3    Koepf, E.K.4    Lashuel, H.A.5
  • 15
    • 0025825160 scopus 로고
    • Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP)
    • Furuya H, Saraiva MJ, Gawinowicz MA, Alves IL, Costa PP, et al. (1991) Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP). Biochemistry 30: 2415-2421.
    • (1991) Biochemistry , vol.30 , pp. 2415-2421
    • Furuya, H.1    Saraiva, M.J.2    Gawinowicz, M.A.3    Alves, I.L.4    Costa, P.P.5
  • 16
    • 0030885583 scopus 로고    scopus 로고
    • Thyroxine binding to transthyretin Met 119. Comparative studies of different heterozygotic carriers and structural analysis
    • Almeida MR, Damas AM, Lans MC, Brouwer A, Saraiva MJ, (1997) Thyroxine binding to transthyretin Met 119. Comparative studies of different heterozygotic carriers and structural analysis. Endocrine 6: 309-315.
    • (1997) Endocrine , vol.6 , pp. 309-315
    • Almeida, M.R.1    Damas, A.M.2    Lans, M.C.3    Brouwer, A.4    Saraiva, M.J.5
  • 18
    • 3242807241 scopus 로고    scopus 로고
    • Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative
    • Almeida MR, Macedo B, Cardoso I, Alves I, Valencia G, et al. (2004) Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative. The Biochemical journal 381: 351-356.
    • (2004) The Biochemical Journal , vol.381 , pp. 351-356
    • Almeida, M.R.1    Macedo, B.2    Cardoso, I.3    Alves, I.4    Valencia, G.5
  • 20
    • 84988113204 scopus 로고
    • Demonstration of human prealbumin by double one-dimensional slab gel electrophoresis
    • Altland K, Rauh S, Hacker R, (1981) Demonstration of human prealbumin by double one-dimensional slab gel electrophoresis. Electrophoresis 2: 148-155.
    • (1981) Electrophoresis , vol.2 , pp. 148-155
    • Altland, K.1    Rauh, S.2    Hacker, R.3
  • 21
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Molecular neurodegeneration 2: 18.
    • (2007) Molecular Neurodegeneration , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5
  • 22
    • 36348960658 scopus 로고    scopus 로고
    • Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design
    • Cardoso I, Almeida MR, Ferreira N, Arsequell G, Valencia G, et al. (2007) Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design. The Biochemical journal 408: 131-138.
    • (2007) The Biochemical Journal , vol.408 , pp. 131-138
    • Cardoso, I.1    Almeida, M.R.2    Ferreira, N.3    Arsequell, G.4    Valencia, G.5
  • 23
    • 79960910835 scopus 로고    scopus 로고
    • Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation
    • Ferreira N, Saraiva MJ, Almeida MR, (2011) Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS letters 585: 2424-2430.
    • (2011) FEBS Letters , vol.585 , pp. 2424-2430
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 24
    • 0033044803 scopus 로고    scopus 로고
    • Prealbumin measurement as a screening tool for protein calorie malnutrition in emergency hospital admissions: a pilot study
    • Potter MA, Luxton G, (1999) Prealbumin measurement as a screening tool for protein calorie malnutrition in emergency hospital admissions: a pilot study. Clinical and investigative medicine Medecine clinique et experimentale 22: 44-52.
    • (1999) Clinical and Investigative Medicine Medecine Clinique Et Experimentale , vol.22 , pp. 44-52
    • Potter, M.A.1    Luxton, G.2
  • 26
    • 0030864769 scopus 로고    scopus 로고
    • Cerebrospinal fluid transthyretin: aging and late onset Alzheimer's disease
    • Serot JM, Christmann D, Dubost T, Couturier M, (1997) Cerebrospinal fluid transthyretin: aging and late onset Alzheimer's disease. Neurosurg Psychiatry 63(4): 506-508.
    • (1997) Neurosurg Psychiatry , vol.63 , Issue.4 , pp. 506-508
    • Serot, J.M.1    Christmann, D.2    Dubost, T.3    Couturier, M.4
  • 28
    • 0030329641 scopus 로고    scopus 로고
    • Interaction of transthyretin with amyloid beta-protein: binding and inhibition of amyloid formation
    • Schwarzman AL, Goldgaber D, (1996) Interaction of transthyretin with amyloid beta-protein: binding and inhibition of amyloid formation. Ciba Found Symp 199: 146-160.
    • (1996) Ciba Found Symp , vol.199 , pp. 146-160
    • Schwarzman, A.L.1    Goldgaber, D.2
  • 29
    • 0036759157 scopus 로고    scopus 로고
    • Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways
    • Stein TD, Johnson JA, (2002) Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways. The Journal of neuroscience: the official journal of the Society for Neuroscience 22: 7380-7388.
    • (2002) The Journal of Neuroscience: The Official Journal of the Society for Neuroscience , vol.22 , pp. 7380-7388
    • Stein, T.D.1    Johnson, J.A.2
  • 32
    • 11144228259 scopus 로고    scopus 로고
    • The crystal structure of transthyretin in complex with diethylstilbestrol: a promising template for the design of amyloid inhibitors
    • Morais-de-Sa E, Pereira PJ, Saraiva MJ, Damas AM, (2004) The crystal structure of transthyretin in complex with diethylstilbestrol: a promising template for the design of amyloid inhibitors. The Journal of biological chemistry 279: 53483-53490.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 53483-53490
    • Morais-de-Sa, E.1    Pereira, P.J.2    Saraiva, M.J.3    Damas, A.M.4
  • 33
    • 0032970177 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid
    • Baures PW, Oza VB, Peterson SA, Kelly JW, (1999) Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid. Bioorganic & medicinal chemistry 7: 1339-1347.
    • (1999) Bioorganic & Medicinal Chemistry , vol.7 , pp. 1339-1347
    • Baures, P.W.1    Oza, V.B.2    Peterson, S.A.3    Kelly, J.W.4
  • 35
    • 0036544598 scopus 로고    scopus 로고
    • Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization
    • Raghu P, Reddy GB, Sivakumar B, (2002) Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization. Archives of biochemistry and biophysics 400: 43-47.
    • (2002) Archives of Biochemistry and Biophysics , vol.400 , pp. 43-47
    • Raghu, P.1    Reddy, G.B.2    Sivakumar, B.3
  • 36
    • 77952671938 scopus 로고    scopus 로고
    • Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding
    • Trivella DB, Bleicher L, Palmieri L C, Wiggers HJ, Montanari CA, et al. (2010) Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding. Journal of structural biology 170: 522-531.
    • (2010) Journal of Structural Biology , vol.170 , pp. 522-531
    • Trivella, D.B.1    Bleicher, L.2    Palmieri, L.C.3    Wiggers, H.J.4    Montanari, C.A.5
  • 37
    • 33745601361 scopus 로고    scopus 로고
    • Genistein and other soya isoflavones are potent ligands for transthyretin in serum and cerebrospinal fluid
    • Radovic B, Mentrup B, Kohrle J, (2006) Genistein and other soya isoflavones are potent ligands for transthyretin in serum and cerebrospinal fluid. The British journal of nutrition 95: 1171-1176.
    • (2006) The British Journal of Nutrition , vol.95 , pp. 1171-1176
    • Radovic, B.1    Mentrup, B.2    Kohrle, J.3
  • 38
    • 77954988796 scopus 로고    scopus 로고
    • Synergy of combined doxycycline/TUDCA treatment in lowering Transthyretin deposition and associated biomarkers: studies in FAP mouse models
    • Cardoso I, Martins D, Ribeiro T, Merlini G, Saraiva MJ, (2010) Synergy of combined doxycycline/TUDCA treatment in lowering Transthyretin deposition and associated biomarkers: studies in FAP mouse models. Journal of translational medicine 8: 74.
    • (2010) Journal of Translational Medicine , vol.8 , pp. 74
    • Cardoso, I.1    Martins, D.2    Ribeiro, T.3    Merlini, G.4    Saraiva, M.J.5
  • 39
    • 49349097870 scopus 로고    scopus 로고
    • Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of Familial Amyloidotic Polyneuropathy
    • Macedo B, Batista AR, Ferreira N, Almeida MR, Saraiva MJ, (2008) Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of Familial Amyloidotic Polyneuropathy. Biochimica et biophysica acta 1782: 517-522.
    • (2008) Biochimica Et Biophysica Acta , vol.1782 , pp. 517-522
    • Macedo, B.1    Batista, A.R.2    Ferreira, N.3    Almeida, M.R.4    Saraiva, M.J.5
  • 40
    • 71749085436 scopus 로고    scopus 로고
    • Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity
    • Ferreira N, Cardoso I, Domingues MR, Vitorino R, Bastos M, et al. (2009) Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity. FEBS letters 583: 3569-3576.
    • (2009) FEBS Letters , vol.583 , pp. 3569-3576
    • Ferreira, N.1    Cardoso, I.2    Domingues, M.R.3    Vitorino, R.4    Bastos, M.5
  • 41
    • 84855650426 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: "in vivo" evidence from FAP mice models
    • Ferreira N, Saraiva MJ, Almeida MR, (2012) Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: "in vivo" evidence from FAP mice models. PLoS One 7: e29933.
    • (2012) PLoS One , vol.7
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 42
    • 77954847105 scopus 로고    scopus 로고
    • The crystal structure of the green tea polyphenol (-)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site
    • Miyata M, Sato T, Kugimiya M, Sho M, Nakamura T, et al. (2010) The crystal structure of the green tea polyphenol (-)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site. Biochemistry 49: 6104-6114.
    • (2010) Biochemistry , vol.49 , pp. 6104-6114
    • Miyata, M.1    Sato, T.2    Kugimiya, M.3    Sho, M.4    Nakamura, T.5
  • 43
    • 64249132020 scopus 로고    scopus 로고
    • Substrate specificity of transthyretin: identification of natural substrates in the nervous system
    • Liz MA, Fleming CE, Nunes AF, Almeida MR, Mar FM, et al. (2009) Substrate specificity of transthyretin: identification of natural substrates in the nervous system. Biochem J 419(2): 467-474.
    • (2009) Biochem J , vol.419 , Issue.2 , pp. 467-474
    • Liz, M.A.1    Fleming, C.E.2    Nunes, A.F.3    Almeida, M.R.4    Mar, F.M.5
  • 44
    • 0023930090 scopus 로고
    • Serum prealbumin and retinol-binding protein concentrations in Japanese-type familial amyloid polyneuropathy
    • Shoji S, Nakagawa S, (1988) Serum prealbumin and retinol-binding protein concentrations in Japanese-type familial amyloid polyneuropathy. European neurology 28: 191-193.
    • (1988) European Neurology , vol.28 , pp. 191-193
    • Shoji, S.1    Nakagawa, S.2
  • 45
    • 0034113564 scopus 로고    scopus 로고
    • Use of the retinol-binding protein: transthyretin ratio for assessment of vitamin A status during the acute-phase response
    • Filteau SM, Willumsen JF, Sullivan K, Simmank K, Gamble M, (2000) Use of the retinol-binding protein: transthyretin ratio for assessment of vitamin A status during the acute-phase response. The British journal of nutrition 83: 513-520.
    • (2000) The British Journal of Nutrition , vol.83 , pp. 513-520
    • Filteau, S.M.1    Willumsen, J.F.2    Sullivan, K.3    Simmank, K.4    Gamble, M.5


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