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The Absence of ABCA1 Decreases Soluble ApoE Levels but Does Not Diminish Amyloid Deposition in Two Murine Models of Alzheimer Disease
Open accessAbstract
ABCA1, a cholesterol transporter expressed in the brain, has been shown recently to be required to maintain normal apoE levels and lipidation in the central nervous system. In addition, ABCA1 has been reported to modulate beta-amyloid (Abeta) production in vitro. These observations raise the possibility that ABCA1 may play a role in the pathogenesis of Alzheimer disease. Here we report that the deficiency of ABCA1 does not affect soluble or guanidine-extractable Abeta levels in Tg-SwDI/B or amyloid precursor protein/presenilin 1 (APP/PS1) mice, but rather is associated with a dramatic reduction in soluble apoE levels in brain. Although this reduction in apoE was expected to reduce the amyloid burden in vivo, we observed that the parenchymal and vascular amyloid load was increased in Tg-SwDI/B animals and was not diminished in APP/PS1 mice. Furthermore, we observed an increase in the proportion of apoE retained in the insoluble fraction, particularly in the APP/PS1 model. These data suggested that ABCA1-mediated effects on apoE levels and lipidation influenced amyloidogenesis in vivo.
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“In support of this possibility, it was recently demonstrated that ATP-binding cassette transporter A1 (ABCA1)-mediated lipidation of apoE modulates amyloid plaque formation (Hirsch-Reinshagen et al., 2005; Koldamova et al., 2005; Wahrle et al., 2005; Wahrle et al., 2008).”
From Overexpression of Low-Density Lipoprotein Receptor in the Brain Markedly Inhibits Amyloid Deposition and Increases Extracellular Aβ Clearance (2009) · cites this paper as Hirsch-Reinshagen et al., 2005
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“ABCA1 overexpression or LXR/RXR agonist treatment decreased amyloid deposition [66-69].”
From MicroRNAs in brain cholesterol metabolism and their implications for Alzheimer's disease (2016) · cites this paper as [66]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“ABCA1 gene ablation in mice decreased APOE lipidation and levels and increased Aβ accumulation in APP transgenic mouse models.”
From MicroRNAs in brain cholesterol metabolism and their implications for Alzheimer's disease (2016) · cites this paper as [66]
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“We and others demonstrated that modulation of ABCA1 affects Aβ levels and amyloid accumulation in vivo.”
From miR-106b impairs cholesterol efflux and increases Aβ levels by repressing ABCA1 expression (2012) · cites this paper as Hirsch-Reinshagen et al., 2005
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“ABCA1 deficiency leads to an increase in Aβ and amyloid deposition (Hirsch-Reinshagen et al., 2005; Koldamova et al., 2005; Wahrle et al., 2005)”
From miR-106b impairs cholesterol efflux and increases Aβ levels by repressing ABCA1 expression (2012) · cites this paper as Hirsch-Reinshagen et al., 2005
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“However, three independent studies demonstrated that ABCA1 deficiency leads to an increase in both Aβ and amyloid load in the brains of three different transgenic APP mouse models (Hirsch-Reinshagen et al., 2005; Koldamova et al., 2005; Wahrle et al., 2005).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Hirsch-Reinshagen et al., 2005
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“In the context of Aβ pathology, knockout of ABCA1 led to an increase in Aβ plaques (Fig. 2A) [40–42].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [41]
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“This transporter is of prime interest in AD because its impact on brain cholesterol metabolism modulates the brain's amyloid burden.”
From Bexarotene Promotes Cholesterol Efflux and Restricts Apical-to-Basolateral Transport of Amyloid-β Peptides in an In Vitro Model of the Human Blood-Brain Barrier (2015) · cites this paper as [12]
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“Interestingly, deletion of ATP-binding cassette, sub-family A1 (Abca1) and liver x receptor (Lxr) genes decreased apoE levels but increased or had no effect on Aβ deposition (Hirsch-Reinshagen et al.,2005; Koldamova et al., 2005; Wahrle et al., 2005; Zelcer et al., 2007).”
From Haploinsufficiency of Human APOE Reduces Amyloid Deposition in a Mouse Model of Amyloid-β Amyloidosis (2011) · cites this paper as Hirsch-Reinshagen et al.,2005
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“The amyloid load in APP transgenic mice deficient in ABCA1 did not change, or even increased, when ABCA1−/− mice were crossed to various APP transgenic models [40-42].”
From Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling (2012) · cites this paper as [40]
In the citing paper
“Several studies have demonstrated that deletion of ABCA1 expression increases the amyloid burden in murine models of AD [11][12][13]”
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“knock-out of this gene provokes an accumulation of A peptide in the CNS [12,13,56].”
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“Interestingly, deletion of ATP-binding cassette, subfamily A1 (Abca1) and liver x receptor (Lxr) genes decreased apoE levels but increased or had no effect on A deposition (Hirsch-Reinshagen et al., 2005; Koldamova et al., 2005; Wahrle et al., 2005; Zelcer et al., 2007).”
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Metadata
- Authors
- Hirsch-Reinshagen, V., Maia, L. F., Burgess, B. L., Blain, J.-F., Naus, K. E., McIsaac, S. A., Parkinson, P. F., Chan, J. Y., Tansley, G. H., Hayden, M. R., Poirier, J., Van Nostrand, W., & Wellington, C. L.
- Affiliations
- University of British Columbia (CA)
- McGill University Research Centre for Studies in Aging (CA)
- Corresponding author
- Wellington, Cheryl L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-12
- Volume
- 280
- Issue
- 52
- Pages
- 43243-43256
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2151049459
- Cited by
- 233
- References
- 95
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 6 · 2023: 6 · 2022: 11 · 2021: 8 · 2020: 5 · 2019: 9 · 2018: 7 · 2017: 11 · 2016: 10 · 2015: 10 · 2014: 20 · 2013: 13 · 2012: 19
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Funders
- AstraZeneca
- Heart and Stroke Foundation of Canada
- Child and Family Research Institute
- Alzheimer Society
- National Institutes of Health
- Canadian Institutes of Health Research
- National Institute of Neurological Disorders and Stroke (R01NS036645, NS36645)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- ABCA1, apolipoprotein E, amyloid deposition, Alzheimer's disease, amyloid-beta, amyloid precursor protein, presenilin 1, APP/PS1 mice, cholesterol transport, amyloidogenesis
- MeSH terms
- Alzheimer Disease, Amyloid, Animals, Apolipoproteins E, Brain, Cerebral Cortex, Cholesterol, Densitometry, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Hippocampus, Humans, Immunohistochemistry, Lipids, Membrane Proteins, Mice, Inbred C57BL, Blotting, Western, ATP-Binding Cassette Transporters, Transgenes, Guanidine, Mice, Presenilin-1, ATP Binding Cassette Transporter 1
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