Pathogenic Aggregates

Amyloid-β – Amyloid precursor protein (APP) is cleaved by enzymes like secretase into various species of amyloid-β (Aβ) peptides, which may have physiological roles in infection defense, blood-brain barrier repair, and brain injury recovery. Under healthy conditions, Aβ is quickly cleared from extracellular space and the cerebrospinal fluid, but genetic and environmental factors can cause the aberrant accumulation of Aβ. This leads to Aβ aggregation and the formation of higher-order structures (oligomers, fibrils, and plaques) that are associated with Alzheimer’s disease.

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Tau – Microtubules are critical for the transport of cellular cargo through axons, and are therefore in a constant state of polymerization and depolymerization. Stabilizing proteins like Tau help assemble and regulate microtubules in neurons and glial cells. Misfolded and hyperphosphorylated Tau proteins, however, will form self-propagating aggregates called neurofibrillary tangles (NFTs) which are unable to perform their normal role in microtubule stabilization. This results in loss of neuronal function, and can lead to neurodegenerative diseases like frontotemporal dementia (FTD), Pick’s disease, and Alzheimer’s disease.

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α-Synuclein – α-Synuclein is a protein that is primarily found in the central nervous system (CNS), but is expressed at low levels in a variety of other tissues. It is predominantly localized to presynaptic terminals of neurons and plays a role in regulating membrane vesicle trafficking. Mutations and modifications of α-Synuclein can lead to its aggregation and the formation of Lewy bodies, which can cause Parkinson’s disease, multiple system atrophy, and Lewy body dementia.

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Prion – Cellular prion protein (PrP^C) is expressed on the surface of cells in different tissues, with the highest expression in the nervous system. In neurons, it is localized to pre- and postsynaptic structures, suggesting a role for PrP^C in regulating synaptic function. The pathogenic and misfolded form of the prion protein, PrP^Sc, can spontaneously arise or be transmitted, and will catalyze the transformation of PrP^C into PrP^Sc. This leads to PrP^Sc aggregation and development of neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD), Kuru, and scrapie.

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