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

• Tipo: Artigo em Revista Científica Internacional
• Data: 2009

Autores

Nelson Ferreira (Autor) Outra; Isabel Cardoso (Autor) Outra; Maria Rosario Domingues (Autor) Outra; Rui Vitorino (Autor) Outra; Margarida Bastos (Autor) FCUP; Guangyue Y Bai (Autor) Outra; Maria Joao Saraiva (Autor) ICBAS; Maria Rosario Almeida (Autor) ICBAS

Revista

Título: FEBS Letters

Vol. 583 Nº 22

Páginas: 3569-3576

ISSN: 0014-5793

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 112 Citações

Scopus - 114 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-003-EAZ

DOI: 10.1016/j.febslet.2009.10.062

Abstract (EN): 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)

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 8