Proteomics

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Proteomics analysis of TDP-43 aggregates derived from HEK293A

ABSTRACT: 97% of sporadic ALS patients exhibit pathology and aggregation of a global RNA regulator protein, transactive response DNA binding protein of 43 kDa (TDP-43). The goal of this study was to optimize and characterize a novel immuno-purification platform for ALS-associated TDP-43 aggregates using a scalable HEK293A culture model. Proteomics analysis was used to profile disease-associated post-translational modifications and TDP-43 co-aggregating proteins. Our findings support use of this protocol to generate pathologically relevant TDP-43 aggregates suitable for mechanistic studies in biochemical and cell-based assays.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Laura Herring  

LAB HEAD: Todd Cohen

PROVIDER: PXD035705 | Pride | 2023-07-20

REPOSITORIES: Pride

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Publications

Tandem detergent-extraction and immunoprecipitation of proteinopathy: Scalable enrichment of ALS-associated TDP-43 aggregates.

Evangelista Baggio A BA   Cahalan Shannon R SR   Ragusa Joey V JV   Mordant Angie A   Necarsulmer Julie C JC   Perna Robert J RJ   Ajit Tejazaditya T   White Kristen K   Barker Natalie K NK   Tian Xu X   Cohen Sarah S   Meeker Rick R   Herring Laura E LE   Cohen Todd J TJ  

iScience 20230411 5

Transactive response DNA-binding protein of 43 kDa (TDP-43) is a highly conserved, ubiquitously expressed nucleic acid-binding protein that regulates DNA/RNA metabolism. Genetics and neuropathology studies have linked TDP-43 to several neuromuscular and neurological disorders including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Under pathological conditions, TDP-43 mislocalizes to the cytoplasm where it forms insoluble, hyper-phosphorylated aggregates durin  ...[more]

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