Clearance of extracellular misfolded proteins in systemic amyloidosis: Experience with transthyretin

• Tipo: Outra Publicação em Revista Científica Internacional
• Data: 2012

Autores

Maria Rosario Almeida (Autor) ICBAS; Maria Joao Saraiva (Autor) ICBAS

Revista

Título: FEBS Letters

Vol. 586

Páginas: 2891-2896

ISSN: 0014-5793

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 22 Citações

Scopus - 24 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-002-6T0

DOI: 10.1016/j.febslet.2012.07.029

Abstract (EN): Increasing evidence indicates that accumulation of misfolded proteins in the form of oligomers, protofibrils or amyloid fibrils, and their consequences in triggering intracellular signaling cascades with toxic consequences represent unifying events in many of slowly progressive neurodegenerative disorders. Studies with small compounds or molecules, known to recognize and disrupt amyloidogenic structures, have proven efficient in promoting clearance of protein aggregates in experimental models of systemic and localized forms of amyloidoses. Doxycycline and EGCG were efficient in removing aggregates in pre-clinical studies in a transgenic mouse model for transthyretin (TTR) systemic amyloidosis and represent an opportunity to address mechanisms and key players in deposit removal. Extracellular chaperones, such as clusterin and metalloproteinases play an important role in this process.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6