Special Reviews

Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease

Science  31 Oct 2003:
Vol. 302, Issue 5646, pp. 814-818
DOI: 10.1126/science.1087348

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Abstract

The incidence of Alzheimer's disease (AD) and that of prion disorders (PrD) could not be more different. One-third of octogenarians succumb to AD, whereas Creutzfeldt-Jakob disease typically affects one individual in a million each year. However, these diseases have many common features impinging on the metabolism of neuronal membrane proteins: the amyloid precursor protein APP in the case of AD, and the cellular prion protein PrPC in PrD. APP begets the Aβ peptide, whereas PrPC begets the malignant prion protein PrPSc. Both Aβ and PrPSc are associated with disease, but we do not know what triggers their accumulation and neurotoxicity. A great deal has been learned, however, about protein folding, misfolding, and aggregation; an entirely new class of intramembrane proteases has been identified; and unsuspected roles for the immune system have been uncovered. There is reason to expect that prion research will profit from advances in the understanding of AD, and vice versa.

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