Home > Publications Database > Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans. > print

001     139668
005     20240321220648.0
024 7 _ |a 10.3791/56464
|2 doi
024 7 _ |a pmid:29286457
|2 pmid
024 7 _ |a pmc:PMC5755480
|2 pmc
024 7 _ |a altmetric:31071653
|2 altmetric
037 _ _ |a DZNE-2020-05990
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Groh, Nicole
|0 P:(DE-2719)2811001
|b 0
|e First author
|u dzne
245 _ _ |a Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans.
260 _ _ |a New Delhi
|c 2017
|b JoVE124831
264 _ 1 |3 online
|2 Crossref
|b MyJove Corporation
|c 2017-11-26
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1708439639_6809
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a In 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.
536 _ _ |a 342 - Disease Mechanisms and Model Systems (POF3-342)
|0 G:(DE-HGF)POF3-342
|c POF3-342
|f POF III
|x 0
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a Caenorhabditis elegans Proteins
|2 NLM Chemicals
650 _ 7 |a Protein Aggregates
|2 NLM Chemicals
650 _ 7 |a Recombinant Proteins
|2 NLM Chemicals
650 _ 2 |a Age Factors
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Animals, Genetically Modified
|2 MeSH
650 _ 2 |a Caenorhabditis elegans: chemistry
|2 MeSH
650 _ 2 |a Caenorhabditis elegans: genetics
|2 MeSH
650 _ 2 |a Caenorhabditis elegans: metabolism
|2 MeSH
650 _ 2 |a Caenorhabditis elegans Proteins: chemistry
|2 MeSH
650 _ 2 |a Caenorhabditis elegans Proteins: genetics
|2 MeSH
650 _ 2 |a Caenorhabditis elegans Proteins: metabolism
|2 MeSH
650 _ 2 |a Models, Animal
|2 MeSH
650 _ 2 |a Protein Aggregates
|2 MeSH
650 _ 2 |a Recombinant Proteins: chemistry
|2 MeSH
650 _ 2 |a Recombinant Proteins: genetics
|2 MeSH
650 _ 2 |a Recombinant Proteins: metabolism
|2 MeSH
700 1 _ |a Gallotta, Ivan
|0 P:(DE-2719)2811903
|b 1
|u dzne
700 1 _ |a Lechler, Marie C
|0 P:(DE-2719)2810617
|b 2
|u dzne
700 1 _ |a Huang, Chaolie
|0 P:(DE-2719)2811852
|b 3
|u dzne
700 1 _ |a Jung, Raimund
|0 P:(DE-2719)2811479
|b 4
|u dzne
700 1 _ |a David, Della C
|0 P:(DE-2719)2810353
|b 5
|e Last author
|u dzne
773 1 8 |a 10.3791/56464
|b : MyJove Corporation, 2017-11-26
|n 129
|3 journal-article
|2 Crossref
|t Journal of Visualized Experiments
|y 2017
|x 1940-087X
773 _ _ |a 10.3791/56464
|g no. 129, p. 56464
|0 PERI:(DE-600)2975337-5
|n 129
|q :129<56464
|p 56464
|t JoVE journal
|v Biology
|y 2017
|x 1940-087X
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5755480
856 4 _ |u https://pub.dzne.de/record/139668/files/DZNE-2020-05990_Restricted.pdf
856 4 _ |u https://pub.dzne.de/record/139668/files/DZNE-2020-05990_Restricted.pdf?subformat=pdfa
|x pdfa
909 C O |p VDB
|o oai:pub.dzne.de:139668
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 0
|6 P:(DE-2719)2811001
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 1
|6 P:(DE-2719)2811903
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 2
|6 P:(DE-2719)2810617
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 3
|6 P:(DE-2719)2811852
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 4
|6 P:(DE-2719)2811479
910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
|0 I:(DE-588)1065079516
|k DZNE
|b 5
|6 P:(DE-2719)2810353
913 1 _ |a DE-HGF
|b Gesundheit
|l Erkrankungen des Nervensystems
|1 G:(DE-HGF)POF3-340
|0 G:(DE-HGF)POF3-342
|3 G:(DE-HGF)POF3
|2 G:(DE-HGF)POF3-300
|4 G:(DE-HGF)POF
|v Disease Mechanisms and Model Systems
|x 0
914 1 _ |y 2017
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
|b JOVE-J VIS EXP : 2019
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0320
|2 StatID
|b PubMed Central
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Clarivate Analytics Master Journal List
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1050
|2 StatID
|b BIOSIS Previews
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
|d 2021-05-04
915 _ _ |a IF < 5
|0 StatID:(DE-HGF)9900
|2 StatID
|d 2021-05-04
920 1 _ |0 I:(DE-2719)1210004
|k AG David
|l Protein Aggregation and Aging
|x 0
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-2719)1210004
980 _ _ |a UNRESTRICTED

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21