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Palmitoylation of Amyloid Precursor Protein Regulates Amyloidogenic Processing in Lipid Rafts

Bhattacharyya, R., Barren, C., Kovacs, D. M.·2013·Journal of Neuroscience
DOI 10.1523/jneurosci.4704-12.2013
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  • ACAT inhibition significantly reduces palmitoylated APP in lipid rafts, thus reducing APP processing.

    “ACAT inhibition significantly reduces palmitoylated APP in lipid rafts, thus reducing APP processing [75–77, 105, 131].”

    From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [131]

    In the Results section (Fig. 9F), ACAT1 inhibition reduced lipid raft-bound palAPP by 76.15 ± 8.9%, alongside reduced APP cleavage-product levels. The paper says the palAPP reduction *likely* resulted in decreased amyloidogenic APP processing; the claim presents that causal link as established. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Cholesterol regulates the formation of lipid clusters and the affinity of proteins to lipid clusters, including β-secretase and γ-secretase.

    “In cellular membranes, cholesterol regulates the formation of lipid clusters (also known as lipid rafts) and the affinity of proteins to lipid clusters (7), including β-secretase and γ-secretase (8–10).”

    From Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterol (2021) · cites this paper as [10]

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Sorted by citations

Metadata

Authors
Bhattacharyya, R., Barren, C., & Kovacs, D. M.
Venue
Journal of Neuroscience
Publisher
Society for Neuroscience
Published
2013-07-03
Volume
33
Issue
27
Pages
11169-11183
ISSN
  • 0270-6474
  • 1529-2401
DOI
10.1523/jneurosci.4704-12.2013
Cited by
171
References
5
Language
en

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