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O-GlcNAcylation increases non-amyloidogenic processing of the amyloid-beta precursor protein (APP)
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- Jacobsen, Kristin T. (author)
- Stockholms universitet,Institutionen för neurokemi
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- Iverfeldt, Kerstin (author)
- Stockholms universitet,Institutionen för neurokemi
- (creator_code:org_t)
- Elsevier BV, 2011
- 2011
- English.
- In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 404:3, s. 882-886
- Journal article (peer-reviewed)
Abstract
Subject headings
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- The amyloid-beta precursor protein (APP) was shown to be O-GlcNAcylated 15 years ago, but the effect of this modification on APP processing and formation of the Alzheimer's disease associated amyloid-beta (A beta) peptide has so far not been investigated. Here, we demonstrate with pharmacological tools or siRNA that O-GlcNAcase and O-GlcNAc transferase regulate the level of O-GlcNAcylated APP. We also show that O-GlcNAcylation increases non-amyloidogenic alpha-secretase processing, resulting in increased levels of the neuroprotective sAPP alpha fragment and decreased A beta secretion. Our results implicate O-GlcNAcylation as a potential therapeutic target for Alzheimer's disease.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Alzheimer's disease
- Amyloid-beta
- APP processing
- O-linked glycosylation
- alpha-Secretase
Publication and Content Type
- ref (subject category)
- art (subject category)
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