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

• Type: Article in International Scientific Journal
• Date: 2006

Authors

Filipe Monteiro (Author) Other; Cardoso, I (Author) Other; Monica M Sousa (Author) ICBAS; Maria Joao Saraiva (Author) ICBAS

Journal

Title: FEBS Letters

Vol. 580

Pages: 3451-3456

ISSN: 0014-5793

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 21 Citations

Scopus - 24 Citations

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6