ABSTRACT
Protein aggregation is increasingly recognized as a common pathological hallmark of a number of neurodegenerative diseases. Amyotrophic lateral sclerosis (ALS) is no exception. The motor neuron degeneration that is typical of ALS is accompanied by a range of intraneuronal protein aggregates that take the form of inclusions, the most common of which are Bunina bodies, ubiquitinated inclusions and neurofilament-rich ‘‘hyaline conglomerate inclusions’’ (1). Increasingly, however, protein aggregation in non-neuronal cells is observed in both experimental models of ALS and in postmortem ALS tissue. Understanding the genesis of these proteinaceous aggregates and their role in the pathogenesis of motor neuron degeneration in ALS is the primary focus of this chapter.
