The Liver X Receptor Ligand T0901317 Decreases Amyloid β Production in Vitro and in a Mouse Model of Alzheimer's Disease
Open accessAbstract
Recent studies indicate that oxysterols, which are ligands for the nuclear hormone liver X receptors (LXR), decrease amyloid beta (Abeta) secretion in vitro. The effect was attributed primarily to the ATP-binding cassette transporter A1 (ABCA1) transcriptionally up-regulated by ligand-activated LXRs. We now examined the effect of the synthetic LXR ligand T0901317, which can be used in vivo, on Abeta production in vitro and in APP23 transgenic mice. T0901317 applied to a variety of in vitro models, including immortalized fibroblasts from Tangier patients, and primary embryonic mouse neurons caused a concentration-dependent decrease in Abeta secretion, and this effect was increased by the addition of apolipoprotein A-I. The inhibition of Abeta production by T0901317 was cell-type specific, being more prominent in primary neurons than in non-neuronal cells. Tangier fibroblasts lacking a functional ABCA1 secreted more Abeta than control fibroblasts, thus demonstrating the role of ABCA1 in amyloid precursor protein (APP) processing and Abeta generation. T0901317 treatment of 11-week-old APP23 mice for 6 days showed a significant increase in ABCA1 expression and a decrease in the ratio of soluble APP (sAPP)beta- to sAPPalpha-cleavage products. Most importantly, the treatment caused a statistically significant reduction in the levels of soluble Abeta40 and of Abeta42 in the brain these mice. Our experiments demonstrate that T0901317 decreases amyloidogenic processing of APP in vitro and in vivo, thus supporting the search for potent and specific LXR ligands with properties allowing therapeutic application.
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LXR agonists increase murine CNS apoE levels and decrease Aβ levels in APP transgenic mice.
“dosing of APP transgenic mice with LXR agonists, which increase murine CNS apoE levels, also decrease A levels (Koldamova et al., 2005;Burns et al., 2006;Riddell et al., 2007).”
From Impact of Apolipoprotein E (ApoE) Polymorphism on Brain ApoE Levels (2008) · cites this paper as Koldamova et al., 2005
The in vivo results report reduced soluble Aβ40 and Aβ42 in T0901317-treated APP23 mice (Fig. 7). But the in vivo APP23 results (Fig. 6D) and Discussion explicitly report no significant change in brain apoE protein after treatment, contrary to the claimed increase in murine CNS apoE. (LLM, conf=0.90)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredLXR agonist treatment alleviates AD-like pathology in mouse models of amyloidosis, possibly by inducing Abca1 expression.
“LXR agonist treatment alleviates AD-like pathology in mouse models of amyloidosis, possibly by inducing Abca1 expression (29, 43–48).”
From The E3 ubiquitin ligase Idol controls brain LDL receptor expression, ApoE clearance, and Aβ amyloidosis (2015) · cites this paper as [45]
The In Vivo LXR Ligand Treatment section reports increased brain ABCA1 expression and significantly decreased soluble Aβ40 and Aβ42 after T0901317 treatment in young APP23 mice. The Discussion proposes ABCA1 as a possible mediator. The study supports reduced amyloidogenic processing in one mouse model, but does not show that established AD-like pathology was alleviated. (LLM, conf=0.84)
Experimental — accuracy not yet measuredABCA1 induction decreases Aβ levels in cells by inhibiting both β- and γ-cleavage of APP.
“Koldamova et al. and Sun et al. reported that ABCA1 induction decreases Aβ levels in cells by inhibiting both β- and γ-cleavage of APP [62-64].”
From MicroRNAs in brain cholesterol metabolism and their implications for Alzheimer's disease (2016) · cites this paper as [63]
The ABCA1 Overexpression section and Figure 4 report reduced Aβ secretion from cells overexpressing ABCA1. The APP23 Mice results report a lower ratio of β- to α-cleavage products after LXR-ligand treatment, but they do not establish that ABCA1 induction inhibits both β- and γ-cleavage in cells. The claimed two-cleavage mechanism is therefore not supported by this paper. (LLM, conf=0.88)
Experimental — accuracy not yet measuredABCA1 gene ablation in mice decreases APOE lipidation and levels and increases Aβ accumulation in APP transgenic mouse models.
“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 [63]
The Discussion (page unavailable) reports markedly lower brain and cerebrospinal-fluid apoE levels in ABCA1-knockout mice, but its statement about abnormal lipidation concerns HDL, not specifically apoE. It does not report increased Aβ accumulation after ABCA1 ablation in APP-transgenic mice; instead, it says the effect of ABCA1 loss on the Alzheimer’s disease phenotype is difficult to predict. (LLM, conf=0.88)
Experimental — accuracy not yet measuredLXR agonists decrease Aβ deposition in the brain while modestly increasing apoE expression.
“LXR agonists have been shown to decrease A deposition in the brain while modestly increasing apoE expression (Koldamova et al., 2005;Zelcer et al., 2007;Fitz et al., 2010).”
From Anti-ApoE Antibody Given after Plaque Onset Decreases Aβ Accumulation and Improves Brain Function in a Mouse Model of Aβ Amyloidosis (2014) · cites this paper as Koldamova et al., 2005
The in vivo results report reduced soluble Aβ40 and Aβ42 in the brains of T0901317-treated APP23 mice, but do not establish reduced Aβ deposition. The in vivo results and Discussion report no significant change in brain apoE protein, rather than a modest increase. Page numbers are unavailable in our copy. (LLM, conf=0.89)
Experimental — accuracy not yet measured
Several genes expressed in the liver including liver X receptors (LXRs) have been suggested as potential therapeutic targets for AD.
“Interestingly, several genes expressed in the liver including liver X receptors (LXRs) have been suggested as potential therapeutic targets for AD [189–191].”
From Genetic architecture of Alzheimer's disease (2020) · cites this paper as [191]
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Self-citation
- Authors
- Koldamova, R. P., Lefterov, I. M., Staufenbiel, M., Wolfe, D., Huang, S., Glorioso, J. C., Walter, M., Roth, M. G., & Lazo, J. S.
- Affiliations
- University of Pittsburgh (US)
- Novartis Institutes for BioMedical Research (CH)
- University of Münster (DE)
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Koldamova, Radosveta P.
- Lefterov, Iliya M.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 280
- Issue
- 6
- Pages
- 4079-4088
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1996457468
- Cited by
- 279
- References
- 55
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 4 · 2023: 5 · 2022: 10 · 2021: 11 · 2020: 12 · 2019: 8 · 2018: 6 · 2017: 11 · 2016: 13 · 2015: 15 · 2014: 17 · 2013: 22 · 2012: 15
- FWCI
- 8.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- University of Pittsburgh
- National Institutes of Health
- National Institute on Aging (AG 18558, AG 23304, R03AG023304)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- liver X receptor, T0901317, amyloid-beta, Alzheimer's disease, ABCA1, oxysterols, APP processing, APP23 transgenic mice, apolipoprotein A-I, soluble APP alpha, cell type specificity, LXR ligands
- MeSH terms
- Liver X Receptors, Benzenesulfonamides, Alzheimer Disease, Animals, Anticholesteremic Agents, Brain, Cloning, Molecular, Disease Models, Animal, DNA-Binding Proteins, Enzyme-Linked Immunosorbent Assay, Fibroblasts, Fluorocarbons, Humans, Hydrocarbons, Fluorinated, Ligands, Mice, Inbred C57BL, Mice, Transgenic, Neurons, Protein Binding, Sulfonamides, Time Factors, Transcription, Genetic, Transfection, Blotting, Western, Up-Regulation, Amyloid beta-Protein Precursor, Apolipoprotein A-I, DNA, Complementary, Simplexvirus, Receptors, Cytoplasmic and Nuclear, Immunoprecipitation, Mice, Orphan Nuclear Receptors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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