Authors
Rodrigo Gallardo, Meine Ramakers, Frederik De Smet, Filip Claes, Ladan Khodaparast, Laleh Khodaparast, José R Couceiro, Tobias Langenberg, Maxime Siemons, Sofie Nyström, Laurence J Young, Romain F Laine, Lydia Young, Enrico Radaelli, Iryna Benilova, Manoj Kumar, An Staes, Matyas Desager, Manu Beerens, Petra Vandervoort, Aernout Luttun, Kris Gevaert, Guy Bormans, Mieke Dewerchin, Johan Van Eldere, Peter Carmeliet, Greetje Vande Velde, Catherine Verfaillie, Clemens F Kaminski, Bart De Strooper, Per Hammarström, K Peter R Nilsson, Louise Serpell, Joost Schymkowitz, Frederic Rousseau
Publication date
2016/11/11
Journal
Science
Volume
354
Issue
6313
Pages
aah4949
Publisher
American Association for the Advancement of Science
Description
INTRODUCTION
It has been shown that most proteins possess amyloidogenic segments. However, only about 30 human proteins are known to be involved in amyloid-associated pathologies, and it is still not clear what determines amyloid toxicity in these diseases. We investigated whether an endogenously expressed protein that contains sequences with known amyloidogenic segments, but is not known to aggregate either under normal or pathological conditions, can be induced to do so by seeding it with a peptide comprising the protein’s own amyloidogenic fragment. We chose to target the protein vascular endothelial growth factor receptor 2 (VEGFR2) because it has well-characterized biological function and so could provide a model system with which to investigate the relationship between protein loss of function and amyloid toxicity in different cellular contexts.
RATIONALE
The capacity of the amyloid …
Scholar articles
R Gallardo, M Ramakers, F De Smet, F Claes… - Science, 2016