| Molecular Brain | 卷:10 |
| Propagation of Tau aggregates | |
| Maria Grazia Spillantini1  Michel Goedert2  | |
| [1] Department of Clinical Neurosciences, Clifford Allbutt Building, University of Cambridge; | |
| [2] MRC Laboratory of Molecular Biology; | |
| 关键词: Alzheimer’s disease; Amyloid; Cell-to-cell spreading; Disease propagation; Prion-like; Protein strains; | |
| DOI : 10.1186/s13041-017-0298-7 | |
| 来源: DOAJ | |
【 摘 要 】
Abstract Since 2009, evidence has accumulated to suggest that Tau aggregates form first in a small number of brain cells, from where they propagate to other regions, resulting in neurodegeneration and disease. Propagation of Tau aggregates is often called prion-like, which refers to the capacity of an assembled protein to induce the same abnormal conformation in a protein of the same kind, initiating a self-amplifying cascade. In addition, prion-like encompasses the release of protein aggregates from brain cells and their uptake by neighbouring cells. In mice, the intracerebral injection of Tau inclusions induced the ordered assembly of monomeric Tau, followed by its spreading to distant brain regions. Short fibrils constituted the major species of seed-competent Tau. The existence of several human Tauopathies with distinct fibril morphologies has led to the suggestion that different molecular conformers (or strains) of aggregated Tau exist.
【 授权许可】
Unknown