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Abstract Title:

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

Abstract Source:

FEBS Lett. 2009 Nov 19;583(22):3569-76. Epub 2009 Oct 25. PMID: 19861125

Abstract Author(s):

Nelson Ferreira, Isabel Cardoso, Maria Rosário Domingues, Rui Vitorino, Margarida Bastos, Guangyue Bai, Maria João Saraiva, Maria Rosário Almeida

Article Affiliation:

Grupo de Neurobiologia Molecular, Instituto de Biologia Molecular e Celular, 4150-180 Porto, Portugal.

Abstract:

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.

Study Type : Review

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Sayer Ji
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