title: "Prion-like" templated misfolding in tauopathies.
abstract: The soluble microtubule-associated protein tau forms hyperphosphorylated, insoluble and filamentous inclusions in a number of neurodegenerative diseases referred to as "tauopathies." In Alzheimer's disease, tau pathology develops in a stereotypical manner, with the first lesions appearing in the locus coeruleus and entorhinal cortex, from where they appear to spread to the hippocampus and neocortex. Propagation of tau pathology is also a characteristic of argyrophilic grain disease, where the tau lesions spread throughout the limbic system. Significantly, isoform composition and morphology of tau filaments can differ between tauopathies, suggesting the existence of distinct tau strains. Extensive experimental findings indicate that prion-like mechanisms underly the pathogenesis of tauopathies.
authors.affiliation: Department of Neuropathology, Institute of Pathology, University Hospital Basel, Basel, Switzerland.
authors.forename: Florence
authors.initials: F
authors.lastname: Clavaguera
authors.forename: Isabelle
authors.initials: I
authors.lastname: Lavenir
authors.forename: Ben
authors.initials: B
authors.lastname: Falcon
authors.forename: Stephan
authors.initials: S
authors.lastname: Frank
authors.forename: Michel
authors.initials: M
authors.lastname: Goedert
authors.forename: Markus
authors.initials: M
authors.lastname: Tolnay
mesh_terms: D000818:Animals; D006801:Humans; D019636:Neurodegenerative Diseases / Q000235:genetics / Q000378:metabolism; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism*; D057165:Proteostasis Deficiencies / Q000235:genetics / Q000378:metabolism* / Q000628:therapy; D024801:Tauopathies / Q000235:genetics / Q000378:metabolism* / Q000628:therapy