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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder that is marked by fasciculation, spasticity and progressive weakness of muscles, and results in difficulty speaking, swallowing and breathing. ALS is fatal, usually leading to death within a few years from diagnosis, although more slowly progressing forms of the disease exist.
Intermediate-length repeat expansions in ATXN-2 are the strongest genetic risk factor for ALS. Here, the authors combine patient-derived motor neurons and organoids with mouse models to dissect the pathogenic effects of ATXN2 intermediate expansions.
In this work, protein-metal complexes implicated in the pathogenesis of amyotrophic lateral sclerosis were mapped by mass spectrometry imaging. Metal-deficient hSOD1G93A complexes were revealed to be localised with disease pathology in the spinal cord and brain.
The authors proposed ClusTric, a temporal stratification approach to find disease progression groups. Applied to Amyotrophic Lateral Sclerosis, the method identifies four progression groups with distinguished characteristics.
Around 10% of individuals with frontotemporal lobar dementia have amyloid filament inclusions that lack tau and TDP-43 and were thought to contain the protein FUS, but are found instead to contain the FUS homologue TAF15.
Two new studies have provided important mechanistic insights into TDP-43 pathology, a hallmark of neurodegenerative conditions such as amyotrophic lateral sclerosis and frontotemporal lobar degeneration.
