Cited by 356Alzheimer's disease research and treatmentsLipid Membrane Structure and BehaviorLysosomal Storage Disorders Research

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Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein

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Cordy, Joanna M., Hussain, Ishrut, Dingwall, Colin, Hooper, Nigel M., Turner, Anthony J.·2003·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1635130100PMC PMC208827

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Abstract

β-Secretase (BACE, Asp-2) is a transmembrane aspartic proteinase responsible for cleaving the amyloid precursor protein (APP) to generate the soluble ectodomain sAPPβ and its C-terminal fragment CTFβ. CTFβ is subsequently cleaved by γ-secretase to produce the neurotoxic/synaptotoxic amyloid-β peptide (Aβ) that accumulates in Alzheimer's disease. Indirect evidence has suggested that amyloidogenic APP processing may preferentially occur in lipid rafts. Here, we show that relatively little wild-type BACE is found in rafts prepared from a human neuroblastoma cell line (SH-SY5Y) by using Triton X-100 as detergent. To investigate further the significance of lipid rafts in APP processing, a glycosylphosphatidylinositol (GPI) anchor has been added to BACE, replacing the transmembrane and C-terminal domains. The GPI anchor targets the enzyme exclusively to lipid raft domains. Expression of GPIBACE substantially up-regulates the secretion of both sAPPβ and amyloid-β peptide over levels observed from cells overexpressing wild-type BACE. This effect was reversed when the lipid rafts were disrupted by depleting cellular cholesterol levels. These results suggest that processing of APP to the amyloid-β peptide occurs predominantly in lipid rafts and that BACE is the rate-limiting enzyme in this process. The processing of the APP 695 isoform by GPI-BACE was up-regulated 20-fold compared with wild-type BACE, whereas only a 2-fold increase in the processing of APP 751/770 was seen, implying a differential compartmentation of the APP isoforms. Changes in the local membrane environment during aging may facilitate the cosegregation of APP and BACE leading to increased β-amyloid production.

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Authors: Cordy, J. M., Hussain, I., Dingwall, C., Hooper, N. M., & Turner, A. J.
Affiliations: University of Leeds (GB)
ORCID: Hooper, Nigel M.
Turner, Anthony J.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2003-09-22
Volume: 100
Issue: 20
Pages: 11735-11740
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1635130100
PMC: PMC208827
OpenAlex: W2160524771
Cited by: 356
References: 36
Citations by year: 2026: 3 · 2025: 10 · 2024: 7 · 2023: 6 · 2022: 8 · 2021: 7 · 2020: 10 · 2019: 4 · 2018: 5 · 2017: 10 · 2016: 9 · 2015: 5 · 2014: 12 · 2013: 16 · 2012: 30
FWCI: 12.29
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Research Portal (King's College London) (submittedVersion)
Newcastle University ePrints (Newcastle Univesity)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
Keywords: beta-secretase, BACE, amyloid precursor protein, lipid rafts, GPI anchoring, amyloid-beta production, APP processing, cholesterol depletion, APP isoforms, Alzheimer's disease, SH-SY5Y cells
MeSH terms: Amino Acid Sequence, Cholesterol, Humans, Hydrolysis, Molecular Sequence Data, Endopeptidases, Protein Processing, Post-Translational, Tumor Cells, Cultured, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Glycosylphosphatidylinositols, Lipid Metabolism, Amyloid Precursor Protein Secretases

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Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein

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