Although it can be understood that TDP-43 has both a toxic gain of function and loss of function, it has yet to be fully determined as to what may be the cause of the toxicity within the cell. According to Lagier-Tourenne et al. animal models tested provide concrete evidence that supports the idea that as ALS progresses, there seems to be an increase in localization of TDP-43 throughout the cytoplasm of neurons found in the brains and spinal cords of patients.
When examining patients, those who had endured sporadic ALS for any duration between 10-20 years showed lower number of inclusions of ubiquitinated TDP-43 when compared to an average patient with ALS (Lee et al 2012). This allows for one to speculate that when there are fewer inclusions due to the aggregation of ubiquitinated TDP-43, ALS may be less severe in the fact that the neurodegeneration of the patient does not occur as rapidly. This also suggests that these inclusions may be effects brought upon by the disease rather than a cause of the disease. It was discovered that within that same study, patients displayed TDP-43 protein aggregates located in the a...
... middle of paper ...
...ron et al. 2010; Lagier-Tourenne et al. 2010). According to Lagier-Tourenne et al., Caspase-3 is known protease that is considered to be an ‘executioner caspase’ which not only activates imminent cell death but also creates a downregulation of the secreted growth factor progranulin disrupting different aspects of growth within the cell (2010).
In a recent study published in 2015, Mitchell et al. suggested that mislocalization and aggregation of the mutant protein seeds recruit wild-type TDP-43 and rapidly accelerates the disease processes in a mice model. Mitchell et al. believes that this is potentially groundbreaking research. This research stemmed Walker et al. to examine clearing the cytoplasmic TDP-43 in the mouse models. Following the clearance of the cytoplasmic TDP-43, it was found that there was functional recovery in the mouse models (Walker et al. 2015).
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