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000140705 1001_ $$0P:(DE-2719)2811852$$aHuang, Chaolie$$b0$$eFirst author$$udzne
000140705 245__ $$aIntrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in Caenorhabditis elegans.
000140705 260__ $$aCambridge$$beLife Sciences Publications$$c2019
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000140705 520__ $$aReduced 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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000140705 542__ $$2Crossref$$i2019-05-03$$uhttps://submit.elifesciences.org/html/elife_author_instructions.html#policies
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000140705 650_2 $$2MeSH$$aAging
000140705 650_2 $$2MeSH$$aAmyloid: metabolism
000140705 650_2 $$2MeSH$$aAnimals
000140705 650_2 $$2MeSH$$aCaenorhabditis elegans: physiology
000140705 650_2 $$2MeSH$$aCaenorhabditis elegans Proteins: metabolism
000140705 650_2 $$2MeSH$$aProtein Aggregates
000140705 7001_ $$0P:(DE-HGF)0$$aWagner-Valladolid, Sara$$b1
000140705 7001_ $$0P:(DE-HGF)0$$aStephens, Amberley D$$b2
000140705 7001_ $$0P:(DE-2719)2811479$$aJung, Raimund$$b3$$udzne
000140705 7001_ $$0P:(DE-HGF)0$$aPoudel, Chetan$$b4
000140705 7001_ $$0P:(DE-HGF)0$$aSinnige, Tessa$$b5
000140705 7001_ $$0P:(DE-2719)2810617$$aLechler, Marie C$$b6$$udzne
000140705 7001_ $$0P:(DE-2719)2811001$$aSchlörit, Nicole$$b7$$udzne
000140705 7001_ $$0P:(DE-HGF)0$$aLu, Meng$$b8
000140705 7001_ $$0P:(DE-HGF)0$$aLaine, Romain F$$b9
000140705 7001_ $$0P:(DE-HGF)0$$aMichel, Claire H$$b10
000140705 7001_ $$0P:(DE-HGF)0$$aVendruscolo, Michele$$b11
000140705 7001_ $$0P:(DE-HGF)0$$aKaminski, Clemens F$$b12
000140705 7001_ $$0P:(DE-HGF)0$$aKaminski Schierle, Gabriele S$$b13$$eCorresponding author
000140705 7001_ $$0P:(DE-2719)2810353$$aDavid, Della C$$b14$$eLast author$$udzne
000140705 77318 $$2Crossref$$3journal-article$$a10.7554/elife.43059$$b : eLife Sciences Publications, Ltd, 2019-05-03$$teLife$$v8$$x2050-084X$$y2019
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