| Autor: |
Marie C. Lechler, Claire H. Michel, G. S. Kaminski Schierle, Chaolie Huang, Raimund Jung, Chetan Poudel, Clemens F. Kaminski, Della C. David, N. Schlörit, A.D. Stephens, Michele Vendruscolo, Romain F. Laine, Tessa Sinnige, Sara Wagner-Valladolid |
| Jazyk: |
angličtina |
| Rok vydání: |
2018 |
| Předmět: |
|
| DOI: |
10.1101/417873 |
| Popis: |
Reduced protein homeostasis and increased protein instability is a common feature of aging. Yet it remains unclear whether protein instability is a cause of aging. In neurodegenerative diseases and amyloidoses, specific proteins self-assemble into amyloid fibrils and accumulate as pathological solid aggregates in a variety of tissues. More recently, widespread protein aggregation has been described during normal aging, in the absence of disease processes. Until now, an extensive characterization of the nature of age-dependent protein aggregation and its consequences for aging has been lacking. Here, we show that age-dependent aggregates are rapidly formed by newly synthesized proteins and contain amyloid-like structures similar to disease-associated protein aggregates. Moreover, we demonstrate that age-dependent protein aggregation accelerates the functional decline of different tissues in C. elegans. Together, these finding reveal that the formation of amyloid aggregates is a generic problem of aging and likely to be an important target for strategies designed to maintain physiological functions in later stages of life. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
