Amyloid β peptides (Aβ) form insoluble aggregates in Alzheimer’s disease. Accumulation of misfolded amyloid fibrils is generally believed to be a key pathogenic event in several brain disorders. Here we show that small amounts of Aβ peptides activate angiogenesis by promoting endothelial cell proliferation and migration as well as pseudocapillary formation. Aβ peptides functionally synergize with fibroblast growth factor (FGF-2) to promote c-Raf and ERK1/2 activation and angiogenesis in vivo. Thus, Aβ peptides at nanomolar concentrations prime FGF- 2 effects on the endothelium, enhancing survival and sustaining angiogenesis. The angiogenesis promoted by Aβ peptides via FGF-2 might have implications for understanding the initial stages of Alzheimer’s disease and for the design of therapies targeting β amyloid.

Cantara, S., Donnini, S., Morbidelli, L., A., G., R., S., M., M., et al. (2004). Physiological levels of amyloid peptides stimulate the angiogenic response through FGF-2. THE FASEB JOURNAL, 18(15), 1943-1945 [10.1096/fj.04-2114fje].

Physiological levels of amyloid peptides stimulate the angiogenic response through FGF-2

CANTARA, SILVIA;DONNINI, SANDRA;MORBIDELLI, LUCIA;ZICHE, MARINA
2004

Abstract

Amyloid β peptides (Aβ) form insoluble aggregates in Alzheimer’s disease. Accumulation of misfolded amyloid fibrils is generally believed to be a key pathogenic event in several brain disorders. Here we show that small amounts of Aβ peptides activate angiogenesis by promoting endothelial cell proliferation and migration as well as pseudocapillary formation. Aβ peptides functionally synergize with fibroblast growth factor (FGF-2) to promote c-Raf and ERK1/2 activation and angiogenesis in vivo. Thus, Aβ peptides at nanomolar concentrations prime FGF- 2 effects on the endothelium, enhancing survival and sustaining angiogenesis. The angiogenesis promoted by Aβ peptides via FGF-2 might have implications for understanding the initial stages of Alzheimer’s disease and for the design of therapies targeting β amyloid.
File in questo prodotto:
File Dimensione Formato  
FasebMZPDF.pdf

non disponibili

Tipologia: PDF editoriale
Licenza: NON PUBBLICO - Accesso privato/ristretto
Dimensione 1.62 MB
Formato Adobe PDF
1.62 MB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/25727
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo