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Neuropathol Appl Neurobiol. 2015 Feb;41(1):47-58. doi: 10.1111/nan.12197.

Invited review: Prion-like transmission and spreading of tau pathology.

Author information

1
Institute of Pathology, University Hospital Basel, Basel, Switzerland.

Abstract

Filaments made of hyperphosphorylated tau protein are encountered in a number of neurodegenerative diseases referred to as 'tauopathies'. In the most prevalent tauopathy, Alzheimer's disease, tau pathology progresses in a stereotypical manner with the first lesions appearing in the locus coeruleus and the entorhinal cortex from where they appear to spread to the hippocampus and neocortex. Propagation of tau pathology is also characteristic of argyrophilic grain disease, where the tau lesions appear to spread throughout distinct regions of the limbic system. These findings strongly implicate neurone-to-neurone propagation of tau aggregates. Isoform composition and morphology of tau filaments can differ between tauopathies suggesting the existence of conformationally diverse tau strains. Altogether, this points to prion-like mechanisms in the pathogenesis of tauopathies.

KEYWORDS:

propagation; tauopathy; transmission

PMID:
25399729
DOI:
10.1111/nan.12197
[Indexed for MEDLINE]

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