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- CLINICA NEUROL, 41: 1198－1200, 2001
- Vol.41 No.12 contents
The 42nd Annual Meeting of the Japanese Society of Neurology
Topics Seminar II:
β-amyloid protein: recent progress in basic research and therapeutic approaches
Takeshi Iwatsubo, M. D.
Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo
Deposition of amyloid β protein (Aβ ) as senile plaques or cerebrovascular amyloid characterizes the brains of patients with Alzheimer' s disease (AD). Aβ are composed of 40∼ 42 amino acids that are proteolytically produced from its precursor β APP. We have shown that the deposition of Aβ ending at the 42nd residue (Aβ 42) is one of the earliest pathological changes in AD brains. Genetic and cell biological evidence strongly suggests that mutations in β APP or presenilin (PS) 1 and 2 genes cause AD through increase in production of Aβ 42. Recently, PS1 and PS2 are shown to be the catalytic subunits of γ -secretase that cleaves the intramembrane segments of β APP and Notch. β -amyloid hypothesis that emphasizes the primacy of Aβ in the pathogenesis of AD is currently being verified by the new experimental therapeutic approaches, e.g., Aβ vaccine therapy or administration of inhibitors of β - or γ -secretases.
(CLINICA NEUROL, 41: 1198－1200, 2001)
key words: Alzheimer' s disease, amyloid β protein, presenilin, Notch, γ-secretase
(Received: 11-May-01)
