Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in <i>Caenorhabditis elegans</i>.

ABSTRACT: Reduced protein homeostasis leading to increased protein instability is a common molecular feature of aging, but it remains unclear whether this is a cause or consequence of the aging process. In neurodegenerative diseases and other amyloidoses, specific proteins self-assemble into amyloid fibrils and accumulate as pathological aggregates in different tissues. More recently, widespread protein aggregation has been described during normal aging. Until now, an extensive characterization of the nature of age-dependent protein aggregation has been lacking. Here, we show that age-dependent aggregates are rapidly formed by newly synthesized proteins and have an amyloid-like structure resembling that of protein aggregates observed in disease. We then demonstrate that age-dependent protein aggrega

SUBMITTER: Huang C 

PROVIDER: S-EPMC6524967 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature