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Physiological levels of amyloid peptides stimulate the angiogenic response through FGF‐2
Author(s) -
Cantara Silvia,
Donnini Sandra,
Morbidelli Lucia,
Giachetti Antonio,
Schulz Richard,
Memo Maurizio,
Ziche Marina
Publication year - 2004
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.04-2114fje
Subject(s) - angiogenesis , fibroblast growth factor , amyloid (mycology) , chemistry , microbiology and biotechnology , in vivo , amyloid beta , peptide , cancer research , biochemistry , biology , receptor , inorganic chemistry
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.