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The neuropathology of different neurodegenerative diseases begins in different brain regions, and involves distinct brain networks. Evidence indicates that transcellular propagation of protein aggregation, which is the basis of prion disease, might underlie the progression of pathology in neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. The prion model predicts specific patterns of neuronal vulnerability and network involvement on the basis of the conformation of pathological proteins. Indeed, evidence indicates that self-propagating aggregate conformers, or so-called strains, are associated with distinct neuropathological syndromes. The extension of this hypothesis to our understanding of common neurodegenerative disorders can suggest new therapeutic approaches, such as immunotherapy and small molecules, to block transcellular propagation, and new diagnostic tools to detect early evidence of disease.
A pathological hallmark of many neurodegenerative diseases is the aggregation of misfolded proteins.1 To prevent accumulation of misfolded protein, constant intracellular clearance through the proteasome and lysosomal and autophagic systems, and extracellular removal through the immune system are crucial,3 but these clearance mechanisms seem to fall short under pathological conditions. What triggers the disease cascade in the brain, why protein removal systems fail in some individuals and not others, and whether neurodegenerative diseases, apart from prion disorders like Creutzfeldt–Jakob disease, are communicable are questions that remain unanswered.