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000139668 037__ $$aDZNE-2020-05990
000139668 041__ $$aEnglish
000139668 082__ $$a570
000139668 1001_ $$0P:(DE-2719)2811001$$aGroh, Nicole$$b0$$eFirst author$$udzne
000139668 245__ $$aMethods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans.
000139668 260__ $$aNew Delhi$$bJoVE124831$$c2017
000139668 264_1 $$2Crossref$$3online$$bMyJove Corporation$$c2017-11-26
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000139668 520__ $$aIn the last decades, the prevalence of neurodegenerative disorders, such as Alzheimer's disease (AD) and Parkinson's disease (PD), has grown. These age-associated disorders are characterized by the appearance of protein aggregates with fibrillary structure in the brains of these patients. Exactly why normally soluble proteins undergo an aggregation process remains poorly understood. The discovery that protein aggregation is not limited to disease processes and instead part of the normal aging process enables the study of the molecular and cellular mechanisms that regulate protein aggregation, without using ectopically expressed human disease-associated proteins. Here we describe methodologies to examine inherent protein aggregation in Caenorhabditis elegans through complementary approaches. First, we examine how to grow large numbers of age-synchronized C. elegans to obtain aged animals and we present the biochemical procedures to isolate highly-insoluble-large aggregates. In combination with a targeted genetic knockdown, it is possible to dissect the role of a gene of interest in promoting or preventing age-dependent protein aggregation by using either a comprehensive analysis with quantitative mass spectrometry or a candidate-based analysis with antibodies. These findings are then confirmed by in vivo analysis with transgenic animals expressing fluorescent-tagged aggregation-prone proteins. These methods should help clarify why certain proteins are prone to aggregate with age and ultimately how to keep these proteins fully functional.
000139668 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000139668 650_7 $$2NLM Chemicals$$aCaenorhabditis elegans Proteins
000139668 650_7 $$2NLM Chemicals$$aProtein Aggregates
000139668 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000139668 650_2 $$2MeSH$$aAge Factors
000139668 650_2 $$2MeSH$$aAnimals
000139668 650_2 $$2MeSH$$aAnimals, Genetically Modified
000139668 650_2 $$2MeSH$$aCaenorhabditis elegans: chemistry
000139668 650_2 $$2MeSH$$aCaenorhabditis elegans: genetics
000139668 650_2 $$2MeSH$$aCaenorhabditis elegans: metabolism
000139668 650_2 $$2MeSH$$aCaenorhabditis elegans Proteins: chemistry
000139668 650_2 $$2MeSH$$aCaenorhabditis elegans Proteins: genetics
000139668 650_2 $$2MeSH$$aCaenorhabditis elegans Proteins: metabolism
000139668 650_2 $$2MeSH$$aModels, Animal
000139668 650_2 $$2MeSH$$aProtein Aggregates
000139668 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000139668 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000139668 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000139668 7001_ $$0P:(DE-2719)2811903$$aGallotta, Ivan$$b1$$udzne
000139668 7001_ $$0P:(DE-2719)2810617$$aLechler, Marie C$$b2$$udzne
000139668 7001_ $$0P:(DE-2719)2811852$$aHuang, Chaolie$$b3$$udzne
000139668 7001_ $$0P:(DE-2719)2811479$$aJung, Raimund$$b4$$udzne
000139668 7001_ $$0P:(DE-2719)2810353$$aDavid, Della C$$b5$$eLast author$$udzne
000139668 77318 $$2Crossref$$3journal-article$$a10.3791/56464$$b : MyJove Corporation, 2017-11-26$$n129$$tJournal of Visualized Experiments$$x1940-087X$$y2017
000139668 773__ $$0PERI:(DE-600)2975337-5$$a10.3791/56464$$gno. 129, p. 56464$$n129$$p56464$$q:129<56464$$tJoVE journal$$vBiology$$x1940-087X$$y2017
000139668 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5755480
000139668 8564_ $$uhttps://pub.dzne.de/record/139668/files/DZNE-2020-05990_Restricted.pdf
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