Abstract
The role of ubiquitinated TDP-43 in amyotrophic lateral sclerosis
Highlights
Amyotrophic lateral sclerosis (ALS) is a disease of progressive degeneration of motor neurons with an insidious onset
Following the discovery of superoxidase dismutase 1 (SOD1) mutation in familial ALS[1], TAR DNAbinding protein 43 inclusions have been found in ALS to be related to familial ALS[2]
RNAbinding protein prion-like domains have no homology or sequence similarity to the human prion protein that forms infectious protein aggregates in new variant Creutzfeldt-Jakob disease, many of these proteins have been identified as the major components of cytoplasmic inclusions associated with subtypes of ALS and frontotemporal dementia (FTD)
Summary
Amyotrophic lateral sclerosis (ALS) is a disease of progressive degeneration of motor neurons with an insidious onset. TDP-43 protein, as an intracellular ubiquitin inclusion, has been identified in sporadic ALS patients[3,4]. Pathological TDP-43 mediated neuronal death is mainly caused by neurotoxicity and loss of TDP-43 function[17]. The overexpression of the full-length protein of TDP-43 and its aggregation can be detected in high expression of tardbp CTFs cells.
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