@article{oai:niigata-u.repo.nii.ac.jp:00020335,
 author = {柳澤, 勝彦},
 issue = {2},
 journal = {新潟医学会雑誌, 新潟医学会雑誌},
 month = {Feb},
 note = {Pathological hallmarks of Alzheimer's disease (AD) are neuritic plaques and neurofibrillary tangles (NFT). Biochemical studies on AD have been based on these pathological features. The amyloid fibrils in plaques consist of polymers of a 4 kDa protein subunit, β-protein. The β-protein is a cleaved product from a precursor protein (APP). Neither the cellular origin of the amyloid nor the mechanism of amyloid accumulation is understood. Involvement of fetal type phosphorylation and fetal type cytoskeletal protein in the formation of paired helical filament, component of NFT, is another important aspect, suggesting that there is some regenerating process in AD brains. Recently lack of growth inhibitory activity was found in AD brains. This biochemical finding may be important to unravel the mechanism of regenerating process in AD brains. Altered protein kinase was found in AD brains. The abnormality in phosphorylation may be related to the expression of some biochemical characteristics like amyloid accumulation or PHF formation. The research on AD has been also advanced with molecular genetics. Very recently Hardy and his colleague found point mutation in APP gene. The pathological significance of this mutation will be elucidated in the near future.},
 pages = {111--116},
 title = {3） アルツハイマー病研究の動向(シンポジウム 老年痴呆の諸問題, 第468回新潟医学会)},
 volume = {107},
 year = {1993}
}