In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)

• Tipo: Artigo em Revista Científica Internacional
• Data: 2006

Autores

Filipe Monteiro (Autor) Outra; Cardoso, I (Autor) Outra; Monica M Sousa (Autor) ICBAS; Maria Joao Saraiva (Autor) ICBAS

Revista

Título: FEBS Letters

Vol. 580

Páginas: 3451-3456

ISSN: 0014-5793

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 21 Citações

Scopus - 24 Citações

Outras Informações

ID Authenticus: P-004-K7T

DOI: 10.1016/j.febslet.2006.05.020

Abstract (EN): Familial amyloidotic polyneuropathy is a neurodegenerative disorder characterized by systemic extracellular deposition of transthyretin (TTR) amyloid fibrils. The latter have been proposed to trigger neurodegeneration through engagement of the receptor for advanced glycation end products (RAGE). Here we show that TTR interaction with RAGE is conserved across mouse and human species and is not dependent on RAGE glycosylation. Moreover, strand D of TTR structure seems important for the TTR-RAGE interaction as well as a motif in RAGE (residues 102-118) located within the V-domain; this motif suppressed TTR aggregate-induced cytotoxicity in cell culture.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6