Journal Article

Phosphatidylethanolamine plasmalogen enhances the inhibiting effect of phosphatidylethanolamine on γ-secretase activity

Tomoko Onodera, Eugene Futai, Eiichiro Kan, Naoki Abe, Takafumi Uchida, Yoshiyuki Kamio and Jun Kaneko

in The Journal of Biochemistry

Volume 157, issue 5, pages 301-309
Published in print May 2015 | ISSN: 0021-924X
Published online November 2014 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/jb/mvu074
Phosphatidylethanolamine plasmalogen enhances the inhibiting effect of phosphatidylethanolamine on γ-secretase activity

Show Summary Details

Preview

Plasmalogens (Pls) are widely distributed in the biological membrane of animals and certain anaerobic bacteria, but their functions in the cell membrane are still poorly understood. Decrease of phosphatidylethanolamine plasmalogen (PEPls) in the brain tissue of patients with Alzheimer's disease prompted us to investigate the effect of the membrane phosphorus lipid composition on the activity of γ-secretase that produces amyloid-beta protein (Aβ). To clarify the effect of phospholipids, including PEPls, on Aβ production, γ-secretase activity was measured in an in vitro assay using yeast microsomes and reconstituted liposomes. The presence of ethanolamine phospholipids in the proteoliposome weakened γ-secretase activity. In addition, increased PEPls content in total ethanolamine phospholipids further decreased the enzyme activity, indicating that γ-secretase activity is affected by the membrane phospholipid PEPls/PE ratio. Furthermore, PEPls from anaerobic bacterial cell membrane induced the same effect on γ-secretase activity.

Keywords: Alzheimer's disease; amyloid-beta; γ-secretase activity; phosphatidylethanolamine plasmalogen; yeast microsomes

Journal Article.  4797 words.  Illustrated.

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content. subscribe or login to access all content.