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PL‐03‐03: Prion‐like properties of assembled tau protein
Author(s) -
Goedert Michel,
Clavaguera Florence,
Tolnay Markus
Publication year - 2011
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2011.05.2356
Subject(s) - tauopathy , progressive supranuclear palsy , tau protein , corticobasal degeneration , gene isoform , genetically modified mouse , neocortex , neuroscience , mutant , biology , locus coeruleus , hippocampal formation , cerebral cortex , chemistry , neurodegeneration , transgene , pathology , alzheimer's disease , biochemistry , central nervous system , medicine , disease , gene
The soluble microtubule-associated protein tau becomes hyperphosphorylated, insoluble and filamentous in a number of neurodegenerative diseases collectively referred to as tauopathies. In Alzheimer’s disease (AD), tau pathology develops in a stereotypical manner, with the first lesions appearing in the locus coeruleus and the transentorhinal cortex, from where they appear to spread to the entorhinal cortex, the hippocampus and the neocortex. The staging of tau pathology has also been described in argyrophilic grain disease (AGD), where tau lesions spread stereotypically throughout the limbic system. The isoform composition and morphology of tau filaments differ between diseases, suggesting the possible existence of different tau strains, reminiscent of prion strains. Prion diseases result from the misfolding of the cellular prion protein that can occur sporadically, as the result of dominantly inherited mutations or following infection. Recent experimental work has shown that prion-like mechanisms are also at work in the tauopathies.