What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?

Neuropathology : Official Journal of the Japanese Society of Neuropathology
Richard A ArmstrongNigel J Cairns

Abstract

Abnormal protein aggregates, in the form of either extracellular plaques or intracellular inclusions, are an important pathological feature of the majority of neurodegenerative disorders. The major molecular constituents of these lesions, viz., beta-amyloid (Abeta), tau, and alpha-synuclein, have played a defining role in the diagnosis and classification of disease and in studies of pathogenesis. The molecular composition of a protein aggregate, however, is often complex and could be the direct or indirect consequence of a pathogenic gene mutation, be the result of cell degeneration, or reflect the acquisition of new substances by diffusion and molecular binding to existing proteins. This review examines the molecular composition of the major protein aggregates found in the neurodegenerative diseases including the Abeta and prion protein (PrP) plaques found in Alzheimer's disease (AD) and prion disease, respectively, and the cellular inclusions found in the tauopathies and synucleinopathies. The data suggest that the molecular constituents of a protein aggregate do not directly cause cell death but are largely the consequence of cell degeneration or are acquired during the disease process. These findings are discussed in relati...Continue Reading

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Citations

Sep 22, 2009·Neurological Sciences : Official Journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology·Richard A Armstrong, Nigel J Cairns
Jun 25, 2013·Neurochemistry International·Sushil SharmaManuchair Ebadi
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Apr 22, 2020·ACS Chemical Neuroscience·Himanshu ChaudharyChristofer Lendel

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