Insulin regulates Presenilin 1 localization via PI3K/Akt signaling.

• 木下, 彩栄

• Uemura, Kengo

• Kubota, Masakazu

• Ando, Koichi

• Kuzuya, Akira

• Asada, Megumi

• Kihara, Takeshi

• Kinoshita, Ayae

抄録

Recently, insulin signaling has been highlighted in the pathology of Alzheimer's disease (AD). Although the association between insulin signaling and Tau pathology has been investigated in several studies, the interaction between insulin signaling and Presenilin 1 (PS1), a key molecule of amyloid beta (Abeta) pathology, has not been elucidated so far. In this study, we demonstrated that insulin inhibited PS1 phosphorylation at serine residues (serine 353, 357) via phosphatidylinositol 3-kinase (PI3K)/Akt signal pathway and strengthened the trimeric complex of PS1/N-cadherin/beta-catenin, consequently relocalizing PS1 to the cell surface. Since our recent report suggests that PS1/N-cadherin/beta-catenin complex regulates Abeta production, it is likely that insulin signaling affects Abeta pathology by regulating PS1 localization.

収録刊行物

• Neuroscience letters

  Neuroscience letters 483 (3), 157-161, 2010-10-15

  Elsevier Ireland Ltd

キーワード

• Alzheimer's disease
• Insulin
• Preseninlin 1
• Phosphorylation

詳細情報

• CRID: 1050282810665003264
• NII論文ID: 120002484938
• NII書誌ID: AA00754925
• ISSN: 03043940
• HANDLE: 2433/126716
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles