Understanding of molecular pathogenesis of Alzheimer's disease. Implications for drug development.
-
- TAKEDA Masatoshi
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
-
- SHINOSAKI Kazuhiro
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
-
- NISHIKAWA Takashi
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
-
- TANAKA Toshihisa
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
-
- KUDO Takashi
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
-
- NAKAMURA Yu
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
-
- KASHIWAGI Yujiro
- Psychiatry, Department of Clinical Neuroscience, Osaka University Graduate School of Medicine
Bibliographic Information
- Other Title
-
- アルツハイマー病の分子病態と治療薬開発への指針
- アルツハイマービョウ ノ ブンシ ビョウタイ ト チリョウヤク カイハツ エ ノ シシン
Search this article
Abstract
Recent advances in the knowledge about Alzheimer pathogenesis indicate several tactics for the development of drugs to treat Alzheimer's disease. Firstly, the function of presenilin, the causative gene for most familial Alzheimer's disease, has been demonstrated to be the protease in the Notch signaling system. Pre-senilin cleaves the transmembrane domain of the C-terminal fragment of the Notch-1 molecule, which is generated by proteolysis by furin-like proteases. APP is also cleaved by presenilin at the γcut site, implying that presenilin is γ-secretase itself or at least closely functioning with γ-secretase. A recent paper has demonstrated that immunization of APP transgenic mouse with amyloid β42 may decrease and prevent amyloid deposition in brain tissue. This unique and novel approach may open the new tactics for developing anti-dementia drugs. Another important finding comes from the identification of the function of prolyl isomerase. It is demonstrated that pin 1, intra-nuclear prolyl isomerase, can restore the microtubule binding capacity of phosphorylated tau, which clearly shows a solid strategy for developing drugs for preventing neuronal degeneration.
Journal
-
- Folia Pharmacologica Japonica
-
Folia Pharmacologica Japonica 115 (2), 79-88, 2000
The Japanese Pharmacological Society
- Tweet
Details 詳細情報について
-
- CRID
- 1390282679250039040
-
- NII Article ID
- 10005705525
-
- NII Book ID
- AN00198335
-
- COI
- 1:CAS:528:DC%2BD3cXpsVChtQ%3D%3D
-
- ISSN
- 13478397
- 00155691
-
- NDL BIB ID
- 4974745
-
- PubMed
- 10876794
-
- Text Lang
- ja
-
- Data Source
-
- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
-
- Abstract License Flag
- Disallowed