Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity

被引：115

作者：

Ferreira, Nelson ^{[1
,2
]}

Cardoso, Isabel ^{[1
]}

Domingues, Maria Rosario ^{[3
]}

Vitorino, Rui ^{[3
]}

Bastos, Margarida ^{[4
]}

Bai, Guangyue ^{[4
]}

Saraiva, Maria Joao ^{[1
,2
]}

Almeida, Maria Rosario ^{[1
,2
]}

机构：

[1] IBMC, Grp Neurobiol Mol, P-4150180 Oporto, Portugal

[2] Univ Porto, Dept Biol Mol, ICBAS, P-4099003 Oporto, Portugal

[3] Univ Aveiro, Dept Quim, Ctr Espectrometria Massa, P-3810193 Aveiro, Portugal

[4] Univ Porto, Fac Ciencias, Dept Quim, CIQ UP, P-4169007 Oporto, Portugal

来源：

FEBS LETTERS | 2009年 / 583卷 / 22期

关键词：

Transthyretin; (-)-Epigallocatechin-3-gallate; Amyloid; Aggregation; FAMILIAL AMYLOIDOTIC POLYNEUROPATHY; IN-VITRO; (-)-EPIGALLOCATECHIN-3-GALLATE; PROTEIN; SERUM; PHARMACOKINETICS; FIBRILLOGENESIS; INHIBITORS; VARIANTS; ALBUMIN;

D O I：

10.1016/j.febslet.2009.10.062

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

More than 100 transthyretin (TTR) variants are associated with hereditary amyloidosis. Approaches for TTR amyloidosis that interfere with any step of the cascade of events leading to fibril formation have therapeutic potential. In this study we tested (-)-epigallocatechin-3-gallate (EGCG), the most abundant catechin of green tea, as an inhibitor of TTR amyloid formation. We demonstrate that EGCG binds to TTR "in vitro" and "ex vivo" and that EGCG inhibits TTR aggregation "in vitro" and in a cell culture system. These findings together with the low toxicity of the compound raise the possibility of using EGCG in a therapeutic approach for familial amyloidotic polyneuropathy, the most frequent form of hereditary TTR amyloidosis. Structured summary: MINT-7294529: TTR (uniprotkb:P02766) and TTR (uniprotkb:P02766) bind (MI:0407) by comigration in non-denaturing gel electrophoresis (MI:0404) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3569 / 3576

页数：8

共 32 条

[1]

Almeida M. R., 2005, Current Drug Targets - CNS and Neurological Disorders, V4, P587, DOI 10.2174/156800705774322076

[2] Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative [J].

Almeida, MR ;

Macedo, B ;

Cardoso, I ;

Alves, I ;

Valencia, G ;

Arsequell, G ;

Planas, A ;

Saraiva, MJ .

BIOCHEMICAL JOURNAL, 2004, 381 :351-356

[3]

Altland K, 1999, ELECTROPHORESIS, V20, P1349, DOI 10.1002/(SICI)1522-2683(19990601)20:7<1349::AID-ELPS1349>3.0.CO

[4]

2-5

[5] Thermodynamics of the interaction between a hydrophobically modified polyelectrolyte and sodium dodecyl sulfate in aqueous solution [J].

Bai, GY ;

Santos, LMNBF ;

Nichifor, M ;

Lopes, A ;

Bastos, M .

JOURNAL OF PHYSICAL CHEMISTRY B, 2004, 108 (01) :405-413

[6] FAST TITRATION EXPERIMENTS USING HEAT-CONDUCTION MICROCALORIMETERS [J].

BASTOS, M ;

HAGG, S ;

LONNBRO, P ;

WADSO, I .

JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS, 1991, 23 (03) :255-258

[7] Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid [J].

Baures, PW ;

Oza, VB ;

Peterson, SA ;

Kelly, JW .

BIOORGANIC & MEDICINAL CHEMISTRY, 1999, 7 (07) :1339-1347

[8] The molecular biology and clinical features of amyloid neuropathy [J].

Benson, Merrill D. ;

Kincaid, John C. .

MUSCLE & NERVE, 2007, 36 (04) :411-423

[9] STRUCTURE OF PRE-ALBUMIN - SECONDARY, TERTIARY AND QUATERNARY INTERACTIONS DETERMINED BY FOURIER REFINEMENT AT 1.8-A [J].

BLAKE, CCF ;

GEISOW, MJ ;

OATLEY, SJ ;

RERAT, B ;

RERAT, C .

JOURNAL OF MOLECULAR BIOLOGY, 1978, 121 (03) :339-356

[10] Transthyretin fibrillogenesis entails the assembly of monomers:: A molecular model for in vitro assembled transthyretin amyloid-like fibrils [J].

Cardoso, I ;

Goldsbury, CS ;

Müller, SA ;

Olivieri, V ;

Wirtz, S ;

Damas, AM ;

Aebi, U ;

Saraiva, MJ .

JOURNAL OF MOLECULAR BIOLOGY, 2002, 317 (05) :683-695

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