ゼロから学んで最先端まで理解するタウPETイメージング

抄録

Tau protein is encoded by microtubule–associated protein tau (MAPT), which is located on chromosome 17 in humans, and contributes to microtubule stabilization. Tau protein is abundant in neurons of the central nervous system and is also expressed at very low levels in astrocytes and oligodendrocytes. Tau protein itself is highly soluble ; however, hyperphosphorylated tau protein becomes insoluble and highly aggregated tau fibrils, which accumulate inside and outside the cells and cause neurotoxicity. Such tau lesions are pathognomonic hallmarks observed in the brain of various neurodegenerative diseases collectively referred to as tauopathies, such as Alzheimer disease, progressive supranuclear palsy, corticobasal degeneration, and Pick disease, and are suspected of being related to neurological damage. Recently, the development of tau positron emission tomography (PET) imaging technology using PET and a PET ligand with binding affinity and selectivity for tau lesions has made it possible to visualize tau lesions in vivo, and research on brain pathology using this technology is progressing remarkably. This paper reviews the history of tau PET imaging technology development and the differences in the properties of each ligand, followed by a review of the latest findings of tau PET imaging research in Alzheimer disease and non–Alzheimer's tauopathies. Finally, future prospects for tau PET imaging research are discussed.