Huang, C; Wagner-Valladolid, S; Stephens, AD; Jung, R; Poudel, C; Sinnige, T; Lechler, MC; ... David, DC; + view all Huang, C; Wagner-Valladolid, S; Stephens, AD; Jung, R; Poudel, C; Sinnige, T; Lechler, MC; Schlörit, N; Lu, M; Laine, RF; Michel, CH; Vendruscolo, M; Kaminski, CF; Kaminski Schierle, GS; David, DC; - view fewer (2019) Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans. Elife , 8 , Article e43059. 10.7554/eLife.43059.

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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 aggregation accelerates the functional decline of different tissues in C. elegans. Together, these findings imply that amyloid-like aggregates contribute to the aging process and therefore could be important targets for strategies designed to maintain physiological functions in the late stages of life.

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