Rinsho Shinkeigaku (Clinical Neurology)

The 49th Annual Meeting of the Japanese Society of Neurology

Recent progress and future direction of neurodegenerative disease research

Ryosuke Takahashi, M.D., Ph.D.

Department of Neurology, Kyoto University Graduate School of Medicine

Although the pathogenetic mechanisms underlying neurodegenerative diseases have been long elusive, recent progress in molecular neurogenetics and neurobiology has suggested that accumulation of misfolded protein leads to dysfunction and degeneration of neurons. Misfolded proteins have propensities to form fibrils termed amyloid fibrils. In the process of amyloid fibrils, intermediate forms such as oligomers and protofibrils are produced and thought to have cytotoxic effects to neurons. Neurotoxicity mediated by misfolded proteins are also caused by stress response such as unfolded protein response. Moreover, recent findings indicate that non-neuronal cells surrounding neurons or extracellular misfolded proteins promote neurodegeneration. To eliminate toxic proteins would constitute promising future therapy for neurodegenerative disorders.
Full Text of this Article in Japanese PDF (389K)

(CLINICA NEUROL, 48: 903|905, 2008)
key words: Conformational disease, misfolded protein, oligomer, endoplasmic reticulum (ER) stress, non-cell autonomous

(Received: 16-May-08)