Apolipoprotein E isoform-dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease

Holtzman, David M.; Bales, Kelly R.; Tenkova, Tanya; Fagan, Anne M.; Parsadanian, Maia; Sartorius, Leah J.; Mackey, Brian; Olney, John; McKeel, Daniel; Wozniak, David; Paul, Steven M.

doi:10.1073/pnas.050004797

Cited by 937Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Apolipoprotein E isoform-dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease

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Holtzman, David M., Bales, Kelly R., Tenkova, Tanya, Fagan, Anne M., Parsadanian, Maia, Sartorius, Leah J., Mackey, Brian, Olney, John +3 more·2000·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.050004797PMC PMC16026

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Abstract

Apolipoprotein E (apoE) alleles determine the age-adjusted relative risk (ɛ4 > ɛ3) for Alzheimer's disease (AD). ApoE may affect AD pathogenesis by promoting deposition of the amyloid-β (Aβ) peptide and its conversion to a fibrillar form. To determine the effect of apoE on Aβ deposition and AD pathology, we compared APP V717F transgenic (TG) mice expressing mouse, human, or no apoE (apoE −/− ). A severe, plaque-associated neuritic dystrophy developed in APP V717F TG mice expressing mouse or human apoE. Though significant levels of Aβ deposition also occurred in APP V717F TG, apoE −/− mice, neuritic degeneration was virtually absent. Expression of apoE3 and apoE4 in APP V717F TG, apoE −/− mice resulted in fibrillar Aβ deposits and neuritic plaques by 15 months of age and substantially (>10-fold) more fibrillar deposits were observed in apoE4-expressing APP V717F TG mice. Our data demonstrate a critical and isoform-specific role for apoE in neuritic plaque formation, a pathological hallmark of AD.

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APOE exerts toxic effects on the cerebrovascular system and neurons and influences Aβ clearance, amyloid deposition, and tau-related neurodegeneration in an allele-dependent manner APOE4 > APOE3 > APOE2.
“APOE exerts toxic effects on the cerebrovascular system (694) and neurons (383, 384) and influences A 𝛃 clearance (60, 64, 98, 135, 256, 266, 278, 294, 315, 693), amyloid deposition (39, 256, 258, 266, 278, 314, 518, 612), and tau-related neurodegeneration (533) in an allele-dependent manner APOE4 > APOE3 > APOE2 .”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [256]
The Results section reports greater Aβ deposition in apoE4-expressing than apoE3-expressing mice, supporting the amyloid-deposition portion for which this paper is cited. The study compares apoE3 and apoE4, not apoE2, so it does not establish the full APOE4 > APOE3 > APOE2 ranking. The other effects in the sentence have separate citations and are not attributed to this paper. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Human apoE isoform-dependent differences in amyloid plaque deposition in APP-transgenic mice follow the pattern E4 > E3 > E2.
“we and others have reported human apoE isoform-dependent differences in amyloid plaque deposition in APP-transgenic mice (E4 > E3 > E2) (10-14).”
From Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance (2011) · cites this paper as [10]
The Results section reports greater Aβ deposition and more fibrillar plaques in apoE4- than apoE3-expressing APP-transgenic mice. The Methods section describes comparisons of apoE3 and apoE4 mice, but not apoE2 mice; this paper therefore supports E4 > E3, not the full E4 > E3 > E2 ranking. Page numbers were not available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Co-deposition of apoE in Aβ plaques is a prerequisite for the occurrence of focal neuritic dystrophy.
“It has been previously demonstrated that co-deposition of apoE in Aβ plaques is a prerequisite for the occurrence of focal neuritic dystrophy [22,29].”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [29]
In Results (‘Neuritic Plaque Formation Requires apoE Expression’; page unavailable), the paper reports that mice lacking apoE developed substantial Aβ deposits but very few to no neuritic plaques. It also notes that apoE colocalizes with fibrillar Aβ. These findings support a role for apoE in plaque-associated dystrophy, but do not establish that apoE co-deposition in each plaque is an absolute prerequisite for focal neuritic dystrophy. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Co-deposition of apoE in Aβ plaques promotes focal neurodegeneration in humans and in AD Tg mice.
“It has also been recognized that co-deposition of apoE in Aβ plaques promotes focal neurodegeneration in humans and in AD Tg mice [22,29,35].”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [29]
The Abstract and Results report that apoE expression is required for extensive plaque-associated neuritic degeneration in AD transgenic mice. The Results also describe apoE in human AD plaques and dystrophic neurites around human fibrillar Aβ deposits, but do not establish that apoE co-deposition promotes degeneration in humans. (LLM, conf=0.86)
Experimental — accuracy not yet measured
In several AD Tg mouse models, lack of apoE is associated with absence of fibrillar Aβ deposits and prevented neurodegeneration.
“Our findings remain consistent with the effects of apoE knock-out noted in several AD Tg mouse models, where lack of apoE was associated with absence of fibrillar Aβ deposits and prevented neurodegeneration [13,29,31,32].”
From Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice (2014) · cites this paper as [29]
The Results section reports that apoE-knockout APPV717F mice had virtually all thioflavine-S-negative Aβ deposits and very few to no neuritic plaques. The Abstract says Aβ-associated neuritic degeneration was virtually absent. This supports the pattern in one transgenic model, but not an absolute absence of fibrillar deposits or prevention of neurodegeneration more broadly. (LLM, conf=0.84)
Experimental — accuracy not yet measured

Apoe knockout mice exhibit markedly reduced amyloid deposition and develop diffuse, amorphous plaques.
“Apoe knockout mice exhibit markedly reduced amyloid deposition and develop diffuse, amorphous plaques. [44–46].”
From Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice (2026) · cites this paper as [45]
The Results section ('Neuritic Plaque Formation Requires apoE Expression'; page unavailable) describes apoE-knockout APPV717F mice as having more diffuse, largely nonfibrillar Aβ deposits, supporting the plaque description. It says average Aβ deposition was only somewhat lower without apoE and was as extensive as in apoE-expressing mice in some animals, so 'markedly reduced amyloid deposition' overstates the finding for total deposition. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Most AD patients have sporadic late-onset AD, in which the APOE gene contains a predominant risk variant.
“Most AD patients have sporadic late-onset AD (LOAD), in which the apolipoprotein E (APOE) gene contains a predominant risk variant6,7.”
From APOE3 - R136S mutation confers resilience against tau pathology via cGAS-STING-IFN inhibition (2024) · cites this paper as [7]
The Discussion (page not available in our copy) identifies the APOE ε4 allele as a genetic risk factor for sporadic AD, supporting the risk-variant portion of the claim. It does not say that most AD patients have sporadic late-onset disease or that ε4 is the predominant risk variant. (LLM, conf=0.85)
Experimental — accuracy not yet measured
ApoE regulates brain amyloid-β deposition in a dose- and isoform-dependent manner (E4>E3>E2).
“ApoE strongly regulates brain amyloid-β (Aβ) deposition in a dose- and isoform-dependent manner (E4>E3>E2) (Bales et al., 1997; Holtzman et al., 2000; Schmechel et al., 1993).”
From Overexpressing low‐density lipoprotein receptor reduces tau‐associated neurodegeneration in relation to apoE‐linked mechanisms (2021) · cites this paper as Holtzman et al., 2000
The Results section reports greater Aβ deposition in apoE4- than apoE3-expressing mice, supporting the E4>E3 comparison. The paper does not test apoE2 or establish the claimed dose-dependent relationship; its Discussion proposes a concentration threshold rather than demonstrating a dose-response. Page numbers were not available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Restoration of APOE expression in astrocytes alone is sufficient to induce formation of fibrillar plaques and microglia reactivity.
“Restoration of APOE expression in astrocytes alone is sufficient to induce formation of fibrillar plaques and microglia reactivity, extending findings from previous studies (Holtzman et al, 2000a; Liu et al, 2017b; Mahan et al, 2022).”
From APOE from astrocytes restores Alzheimer’s Aβ-pathology and DAM-like responses in APOE deficient microglia (2024) · cites this paper as Holtzman et al, 2000a
The Results section (“Expression of Human apoE Results in Fibrillar Aβ Deposition and Neuritic Plaques”; page unavailable) reports thioflavine-S-positive plaques in APPV717F mice expressing human apoE under an astrocyte-specific promoter. It does not report that restoring astrocytic apoE induced microglial reactivity; the Discussion mentions activated glial cells only as a general feature of neuritic plaques. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Expression of human apoE isoform transgenes in PDAPP mice resulted in a marked delay in the deposition of Aβ and formation of neuritic plaques, compared to PDAPP mice expressing murine apoE or no apoE.
“The expression of human apoE isoform transgenes in PDAPP mice resulted in a marked delay in the deposition of Aβ and formation of neuritic plaques, compared to PDAPP mice expressing murine apoE or no apoE (Fagan et al., 2002; Holtzman et al., 2000; Holtzman et al., 1999).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Holtzman et al., 2000
The Discussion states that human apoE3 and apoE4 delay Aβ deposition relative to murine apoE and no apoE. The Results also report fewer neuritic plaques with human apoE than with murine apoE at 15 months. But the comparison with no apoE does not hold for neuritic plaques: mice lacking apoE developed very few or none through 15 months, whereas mice expressing human apoE developed plaques. (LLM, conf=0.90)
Experimental — accuracy not yet measured
Initial studies using PDAPP and Tg2576 APP transgenic mouse models demonstrated that the lack of murine apoE resulted in a significant decrease in Aβ deposition, along with an almost complete lack of true amyloid plaques and neuritic dystrophy.
“Initial studies using the PDAPP and Tg2576 APP transgenic mouse models that develop Aβ deposition demonstrated that the lack of murine apoE resulted in a significant decrease in Aβ deposition, along with an almost complete lack of true amyloid plaques and neuritic dystrophy (Bales et al., 1997; Holtzman et al., 2000; Holtzman et al., 1999).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Holtzman et al., 2000
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measured
Introduction of human APOE to existing FAD-Tg mice significantly delays plaque deposition, although once detected, plaque levels are generally greater with APOE4 than APOE3.
“Introduction of human APOE to existing FAD-Tg mice significantly delays plaque deposition, although once detected, plaque levels are generally greater with APOE4 than APOE3 (3, 6 -8).”
From APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease (2012) · cites this paper as [7]
APOE isoform-dependent amyloid deposition has been consistently observed in humans and Aβ depositing mouse models.
“APOE isoform-dependent amyloid deposition has been consistently observed in humans and Aβ depositing mouse models (Holtzman et al., 2000; Bales et al., 2009; Reiman et al., 2009; Morris et al., 2010).”
From Haploinsufficiency of Human APOE Reduces Amyloid Deposition in a Mouse Model of Amyloid-β Amyloidosis (2011) · cites this paper as Holtzman et al., 2000
APOE has been shown to influence Aβ plaque morphology.
“APOE has been shown to influence Aβ plaque morphology.”
From Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice (2026) · cites this paper as [45]
Human apoE transgenic mice display an isoform-specific pattern of Aβ deposition in the hippocampus, with apoE4 mice having increased levels of Aβ deposits and more thioflavine-S positive plaques than apoE3 mice.
“Interestingly, the human apoE transgenic mice display an isoform-specific pattern of Aβ deposition in the hippocampus, with apoE4 mice having increased levels of Aβ deposits and more thioflavine-S positive plaques than apoE3 mice (Fagan et al., 2002; Holtzman et al., 2000).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Holtzman et al., 2000
ApoE assists in amyloid-β clearance in an isoform-dependent manner wherein apoE2 > apoE3 > apoE4.
“ApoE assists in Aβ clearance in an isoform-dependent manner wherein apoE2 > apoE3 > apoE4 [29, 30, 59].”
From Apolipoprotein E4, inhibitory network dysfunction, and Alzheimer’s disease (2019) · cites this paper as [30]
ApoE4 exacerbates the deposition of amyloid plaques in the brain compared to other ApoE isoforms.
“Compared with other ApoE isoforms, ApoE4 exacerbates the deposition of amyloid plaques in the brain98–100.”
From Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight (2018) · cites this paper as [98]
ApoE affects amyloid-β deposition in a dosage and isoform-specific fashion (ApoE4>ApoE3>ApoE2).
“To date, substantial evidence has demonstrated ApoE affects amyloid-β deposition in a dosage and isoform-specific fashion (ApoE4>ApoE3>ApoE2)96–100”
From Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight (2018) · cites this paper as [98]
Expression of mouse ApoE resulted in greater plaque formation than expression of human ApoE, and mouse ApoE preferentially promoted the formation of parenchymal plaques, while human ApoE promoted the formation of CAA.
“Expression of mouse ApoE resulted in greater plaque formation than expression of human ApoE, and mouse ApoE preferentially promoted the formation of parenchymal plaques, while human ApoE promoted the formation of CAA [59, 60, 94].”
From Alzheimer's disease: experimental models and reality (2017) · cites this paper as [59]
Expression of different isoforms of human ApoE in transgenic mice results in different levels of plaque and CAA burden with apoE4 expression enhancing amyloid deposition compared to apoE3 or apoE2.
“This is further complicated by the fact that expression of different isoforms of human ApoE in transgenic mice results in different levels of plaque and CAA burden with apoE4 expression enhancing amyloid deposition compared to apoE3 or apoE2 [3, 21, 40, 59, 86, 178].”
From Alzheimer's disease: experimental models and reality (2017) · cites this paper as [59]

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Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis
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Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
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“Consistent with this observation, we found that old PDAPP/TRE mice developed Aβ/amyloid deposition in an apoE isoform-dependent pattern, that is, E4> E3> E2, a finding that extends previous reports of apoE isoform-dependent Aβ deposition in various mouse models (10, 11, 13, 14).”
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Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
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Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
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APOE predicts amyloid‐beta but not tau Alzheimer pathology in cognitively normal aging
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Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
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Alzheimer's disease: experimental models and reality
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apoE isoform–specific disruption of amyloid β peptide clearance from mouse brain
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The Aging Brain
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Alzheimer's disease as homeostatic responses to age-related myelin breakdown
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Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice
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ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions
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Profile and Regulation of Apolipoprotein E (ApoE) Expression in the CNS in Mice with Targeting of Green Fluorescent Protein Gene to the ApoE Locus
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ApoE and Clusterin Cooperatively Suppress Aβ Levels and Deposition
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Knockout of the cholesterol 24-hydroxylase gene in mice reveals a brain-specific mechanism of cholesterol turnover
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Neuron-Specific Apolipoprotein E4 Proteolysis Is Associated with Increased Tau Phosphorylation in Brains of Transgenic Mice
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IL-10 Alters Immunoproteostasis in APP Mice, Increasing Plaque Burden and Worsening Cognitive Behavior
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Lipid- and receptor-binding regions of apolipoprotein E4 fragments act in concert to cause mitochondrial dysfunction and neurotoxicity
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Apolipoprotein E, Especially Apolipoprotein E4, Increases the Oligomerization of Amyloid β Peptide
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Human and Murine ApoE Markedly Alters Aβ Metabolism before and after Plaque Formation in a Mouse Model of Alzheimer's Disease
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Human Apolipoprotein E4 Alters the Amyloid-β 40:42 Ratio and Promotes the Formation of Cerebral Amyloid Angiopathy in an Amyloid Precursor Protein Transgenic Model
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HumanAPOEIsoform-Dependent Effects on Brain β-Amyloid Levels in PDAPP Transgenic Mice
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Apolipoprotein (apo) E4 enhances amyloid β peptide production in cultured neuronal cells: ApoE structure as a potential therapeutic target
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Overexpression of Low-Density Lipoprotein Receptor in the Brain Markedly Inhibits Amyloid Deposition and Increases Extracellular Aβ Clearance
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APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease
Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 259 · see citing works
Apolipoprotein E (APOE) genotype has dissociable effects on memory and attentional–executive network function in Alzheimer’s disease
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Novel allele-dependent role for APOE in controlling the rate of synapse pruning by astrocytes
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Apolipoprotein E: Diversity of Cellular Origins, Structural and Biophysical Properties, and Effects in Alzheimer's Disease
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Concerted changes in transcripts in the prefrontal cortex precede neuropathology in Alzheimer's disease
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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
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Apolipoprotein E and Alzheimer’s disease: Findings, hypotheses, and potential mechanisms
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Age-Dependent Effects of apoE Reduction Using Antisense Oligonucleotides in a Model of β-amyloidosis
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Apolipoprotein E and Alzheimer's disease: the influence of apolipoprotein E on amyloid-β and other amyloidogenic proteins
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Gene delivery of human apolipoprotein E alters brain Aβ burden in a mouse model of Alzheimer's disease
Dodart, J.-C., Marr, R. A., Koistinaho, M., Gregersen, B. M., Malkani, S., Verma, I. M., & Paul, S. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409072102 · Cited by 207 · see citing works
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Haploinsufficiency of Human APOE Reduces Amyloid Deposition in a Mouse Model of Amyloid-β Amyloidosis
Kim, J., Jiang, H., Park, S., Eltorai, A. E. M., Stewart, F. R., Yoon, H., Basak, J. M., Finn, M. B., & Holtzman, D. M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3773-11.2011 · Cited by 199 · see citing works
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Apolipoprotein E4, inhibitory network dysfunction, and Alzheimer’s disease
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Impaired Spine Stability Underlies Plaque-Related Spine Loss in an Alzheimer's Disease Mouse Model
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Apolipoprotein E isoform-specific regulation of dendritic spine morphology in apolipoprotein E transgenic mice and Alzheimer's disease patients
Ji, Y., Gong, Y., Gan, W., Beach, T., Holtzman, D. M., & Wisniewski, T. (2003) · Neuroscience · doi:10.1016/j.neuroscience.2003.08.007 · Cited by 189 · see citing works
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Gene Transfer of Human Apoe Isoforms Results in Differential Modulation of Amyloid Deposition and Neurotoxicity in Mouse Brain
Hudry, E., Dashkoff, J., Roe, A. D., Takeda, S., Koffie, R. M., Hashimoto, T., Scheel, M., Spires-Jones, T., Arbel-Ornath, M., Betensky, R., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007000 · Cited by 187 · see citing works
Modulation of Alzheimer-like synaptic and cholinergic deficits in transgenic mice by human apolipoprotein E depends on isoform, aging, and overexpression of amyloid β peptides but not on plaque formation
Buttini, M., Yu, G.-Q., Shockley, K., Huang, Y., Jones, B., Masliah, E., Mallory, M., Yeo, T., Longo, F. M., & Mucke, L. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-24-10539.2002 · Cited by 183 · see citing works
“…Berr et al., 1994; Heinonen et al., 1995; Hyman et al., 1995; Gearing et al., 1996; Ishii et al., 1997; Johnson et al., 1998; McNamara et al., 1998; Holtzman et al., 2000a,b) but also in their capacity to protect the brain against diverse injuries, including those elicited by excitotoxins,…”
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Neuronal hyperactivity due to loss of inhibitory tone in APOE4 mice lacking Alzheimer’s disease-like pathology
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Lipid Alterations in the Earliest Clinically Recognizable Stage of Alzheimers Disease: Implication of the Role of Lipids in the Pathogenesis of Alzheimers Disease
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Purification and characterization of astrocyte-secreted apolipoprotein E and J-containing lipoproteins from wild-type and human apoE transgenic mice
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Transgenic mouse models of alzheimer disease: Developing a better model as a tool for therapeutic interventions.
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Apolipoprotein E ε4 is associated with disease-specific effects on brain atrophy in Alzheimer's disease and frontotemporal dementia
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Apolipoprotein E4 Potentiates Amyloid β Peptide-induced Lysosomal Leakage and Apoptosis in Neuronal Cells
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Diffusion tensor imaging detects age-dependent white matter changes in a transgenic mouse model with amyloid deposition
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Molecular Genetics of Late‐Onset Alzheimer's Disease
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Blocking the apolipoprotein E/amyloid-β interaction as a potential therapeutic approach for Alzheimer's disease
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Apolipoprotein E and cholesterol in aging and disease in the brain
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Authors: Holtzman, D. M., Bales, K. R., Tenkova, T., Fagan, A. M., Parsadanian, M., Sartorius, L. J., Mackey, B., Olney, J., McKeel, D., Wozniak, D., & Paul, S. M.
Affiliations: Washington University in St. Louis (US)
ORCID: Holtzman, David M.
Fagan, Anne M.
Wozniak, David
Paul, Steven M.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2000-02-29
Volume: 97
Issue: 6
Pages: 2892-2897
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.050004797
PMC: PMC16026
OpenAlex: W2119556701
Cited by: 937
References: 31
Citations by year: 2026: 17 · 2025: 27 · 2024: 41 · 2023: 22 · 2022: 29 · 2021: 21 · 2020: 39 · 2019: 31 · 2018: 14 · 2017: 31 · 2016: 35 · 2015: 27 · 2014: 34 · 2013: 29 · 2012: 39
FWCI: 32.12
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Alzheimer's Association (AG13956)
American Federation for Aging Research
Ruth K. Broad Biomedical Research Foundation
National Institutes of Health (AG13956)
National Institute on Aging (R01AG013956, R37AG013956, AG13956)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: apolipoprotein E, Alzheimer's disease, amyloid-beta deposition, fibrillar amyloid-beta, neuritic plaques, neuritic dystrophy, APOE isoforms, APOE ε4, APOE3, amyloid plaques, mouse model
MeSH terms: Alzheimer Disease, Animals, Apolipoproteins E, Disease Models, Animal, Hippocampus, Humans, Mice, Inbred C57BL, Mice, Inbred DBA, Mice, Transgenic, Nerve Degeneration, Thiazoles, Time Factors, Neurites, Genetic Predisposition to Disease, Protein Isoforms, Mice, Benzothiazoles, Plaque, Amyloid

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Apolipoprotein E isoform-dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease

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