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The proteome of APP/PS1 mouse amyloid beta oligomers

ABSTRACT: Amyloid β (Aβ) oligomers are thought to play an important role in the onset and progression of Alzheimer’s disease (AD). Several oligomer-binding proteins have been implicated in mechanisms leading to AD pathology. Such proteins could provide insights into the pathways involved in the disease process of AD and might reveal novel targets for disease-modifying therapy approaches. Here, we separated different native Aβ assemblies in brain homogenates of transgenic AD mice samples by density gradient centrifugation, then isolated Aβ-containing complexes by co-immunoprecipitation. Mass spectrometry of immunoprecipitated proteins with label-free quantification (LFQ) showed numerous significant changes between transgenic AD mice and wildtype mice, confirming familiar binding proteins and also indicating putative new interactors.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

DISEASE(S): Alzheimer's Disease

SUBMITTER: Gereon Poschmann

LAB HEAD: Gereon Poschmann

PROVIDER: PXD053785 | Pride | 2026-04-07

REPOSITORIES: Pride

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			Action	DRS
	191016AD_related_proteins.fasta	Fasta
	LM00932.raw	Raw
	LM00933.raw	Raw
	LM00934.raw	Raw
	LM00935.raw	Raw

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Publications

The Proteome of Human Amyloid Beta Oligomers.

Kass Bettina B Poschmann Gereon G Demir Fatih F Huesgen Pitter P Stühler Kai K Kutzsche Janine J Willbold Dieter D

Biochemistry 20260114 3

Amyloid beta (Aβ) oligomers are thought to play an important role during development and progression of Alzheimer's disease (AD). Previously, we determined the Aβ oligomer concentrations in various AD mouse models and in human brain tissues of former AD patients. Here, we investigate which proteins are part of these Aβ oligomers, apart from Aβ itself. Because several oligomer-associated proteins have been implicated in mechanisms leading to AD pathology, identification of the Aβ oligomer proteom ...[more]

PMID: 41532798

Similar Datasets

The proteome of human amyloid beta oligomers

Project description:Amyloid β (Aβ) oligomers are thought to play an important role in the onset and progression of Alzheimer’s disease (AD). Several oligomer-binding proteins have been implicated in mechanisms leading to AD pathology. Such proteins could provide insights into the pathways involved in the disease process of AD and might reveal novel targets for disease-modifying therapy approaches. Here, we separated different native Aβ assemblies in brain homogenates of human AD post mortem tissue by density gradient centrifugation, then isolated Aβ-containing complexes by co-immunoprecipitation. Mass spectrometry of immunoprecipitated proteins with label-free quantification (LFQ) showed numerous significant changes between AD and control samples, confirming familiar binding proteins and also indicating putative new interactors.

2026-04-07 | PXD053759 | Pride

Expression data from C57/6J mice (Normal), APP/PS1 mice and APP/PS1 mice treatment with HPYD

Project description:Aβ is a peptide of 39-42 amino acid residues that derived from putative intramembranous processing of amyloid precursor protein (APP) at the proposed active site of the γ-secretase/PS1 aspartyl. Aβ has been shown to aggregate and accumulate abnormally in the brain of AD (Alzheimer's disease), and extracellular amyloid plaques of Aβ peptides aggregation can trigger a cascade of pathologic events leading to nerve fiber entanglement and neuronal apoptosis protease. We used microarrays to investigate the effects of HPYD on the gene expression of APP/PS1 transgenic mice, the brain tissues of control group, model group and HPYD group mice.

2018-02-23 | GSE104249 | GEO

Effect of Bacteroides fragilis administration on microglia in WT and the APP-PS1 model of Alzheimer's disease [Bfrag]

Project description:The gut microbiota and innate immune system play critical roles in Alzheimer’s disease (AD). Bacteroides is elevated in AD patients and correlates with cerebrospinal fluid levels of Aβ and tau. We found that increased amyloid-β (Aβ) plaques in Bacteroides fragilis treated APP/PS1-21 mice were associated with altered cortical expression Aβ processing genes. B. fragilis suppressed peripheral CD4+ T cell production of GM-CSF and IL-4 and transcriptional changes in microglia related to GM-CSF and IL-4 signaling, phagocytosis, and protein degradation. Furthermore, B. fragilis impaired the microglial uptake of intracranially injected Aβ42, whereas Erysipelotrichaceae strains increased uptake. Depleting murine Bacteroidetes with metronidazole decreased amyloid load in aged 5xFAD mice, increased CD4+ T cell GM-CSF production, and activated microglial pathways related to cytokine signaling, phagocytosis and lysosomal degradation. These data suggest that the gut microbiome may contribute to AD pathogenesis by suppressing peripheral cytokines and microglia phagocytic function, leading to impaired immune-mediated Aβ clearance.

2024-10-12 | GSE215438 | GEO

Early amyloid-induced changes in microglia gene expression in APP/PS1 mice [scRNA-seq]

Project description:Alzheimer’s disease (AD) is a progressive neurodegenerative disease and the most common cause of dementia, characterized by deposition of extracellular amyloid-beta (Aβ) aggregates and intraneuronal hyperphosphorylated Tau. Many AD risk genes, identified in genome-wide association studies (GWAS), are expressed in microglia, the innate immune cells of the central nervous system. Specific subtypes of microglia emerged in relation to AD pathology, such as disease-associated microglia (DAMs), which increased in number with age in amyloid mouse models and in human AD cases. However, the initial transcriptional changes in these microglia in response to amyloid are still unknown. Here, to determine early changes in microglia gene expression, hippocampal microglia from APPswe/PS1dE9 (APP/PS1) mice and wildtype littermates were isolated and analyzed by RNA sequencing (RNA-seq). By bulk RNA-seq, transcriptomic changes were detected in hippocampal microglia from 6-months-old APP/PS1 mice. By performing single cell RNA-seq of CD11c-positive and negative microglia from 6-months-old APP/PS1 mice and analysis of the transcriptional trajectory from homeostatic to CD11c-positive microglia, we identified a set of genes that potentally reflect the initial response of microglia to Aβ.

2024-04-01 | GSE226938 | GEO

Early amyloid-induced changes in microglia gene expression in APP/PS1 mice [bulk RNA-seq]

2024-04-01 | GSE226937 | GEO

Differential and synergistic transcriptional effects of early amyloid-β and tau pathologies in the hippocampus of APP, Tau, and APP/Tau female mice

Project description:Alzheimer’s disease (AD) is characterized by memory loss associated with accumulation of amyloid-β (Aβ) and tau in the brain, but how memory-processing neural circuits are differentially affected by each pathology remains unclear. Here, we investigated the transcriptional vulnerability to single and concomitant Aβ and tau pathologies in 6-month-old transgenic mice expressing mutant human amyloid precursor protein (APP), Tau, or both (APP/Tau mice) in excitatory neurons. We identified differential and synergistic pathology-induced transcriptional responses in the hippocampus of AD transgenic mice. These findings support the idea that Aβ and tau pathologies exert synergistic effects to disrupt gene expression programs underlying vulnerability of memory neural circuits in AD.

2025-02-07 | GSE280199 | GEO

Mouse hippocampus LC/MS with TMT labeling

Project description:Transgenic mouse models have been widely used to investigate the pathology of Alzheimer’s disease (AD). To elucidate underlying mechanisms of AD pathogenesis by amyloid beta (Aβ) and tau, we have generated a novel animal model of AD; ADLP - APT mice (Alzheimer’s Disease-Like Pathology) – carrying mutations of human amyloid precursor protein (APP), human presenilin-1 (PS1) and human tau. We profiled 9,824 proteins in the hippocampus of ADLP model mice using quantitative proteomics. To identify functional signatures in pathology of ADLP - APT mice, in-depth bioinformatics analysis was performed. For a longitudinal change of differentially expressed proteins (DEPs), we identified ADLP - APT mice hippocampal proteome in an age-dependent manner. Network maps of interactome between Aβ and tau in newly generated ADLP - APT mice reveal relationship between accelerated NFT pathology of AD and proteomic changes.

2018-01-25 | PXD006214 | Pride

Transcriptional vulnerability to amyloid-β and tau pathologies differentially disrupts emotional and memory neural circuits

Project description:Alzheimer’s disease (AD) is characterized by memory loss and neuropsychiatric symptoms associated with cerebral accumulation of amyloid-β (Aβ) and tau, but how memory and emotional neural circuits are disrupted by AD pathology remains unclear. Here, we investigated the transcriptional vulnerability of memory and emotional circuits to concomitant Aβ and tau pathologies in transgenic mice expressing mutant human amyloid precursor protein (APP) and Tau (APP/Tau mice) in excitatory neurons. At 9 months, we detected common and region-specific transcriptional responses in the hippocampus and basolateral amygdala (BLA) of APP/Tau mice, including astrocytic, microglia and 63 AD-associated genes. These findings suggest that Aβ and tau pathologies disrupt region-specific gene expression programs underlying vulnerability of memory and emotional circuits to AD neuropathology.

2025-02-07 | GSE279050 | GEO

In vivo response of microglia to Aβ and prostaglandin-E2 EP2 receptor signaling

Project description:Microglia, the innate immune cells of the central nervous system, perform critical inflammatory and non-inflammatory functions to maintain homeostasis and normal neural function. However in Alzheimer’s disease (AD), these beneficial functions become progressively impaired, contributing to synapse and neuron loss and cognitive impairment. The inflammatory cyclooxygenase-PGE2 pathway, including the PGE2 receptor EP2, is implicated in AD development, both in human epidemiology and in transgenic models of AD. To test the transcriptional responses of EP2-deficient microglia to Aβ in vivo, we used mice in which the EP2 receptor is conditionally deleted in microglia using the CD11b-Cre transgene and floxed alleles of the EP2 gene. By injecting these mice with Aβ ICV and isolating microglia from the brains, we have been able to establish the transcriptional response of microglia to Aβ in vivo and test how EP2 deletion in microglia affects this response. 8 month-old C57BL/6 mice, of the genotype CD11b-Cre; EP2+/+ or CD11b-Cre; EP2lox/lox, were injected I.C.V. with either Aβ or vehicle. 48 hours after injection, the mice were sacrificed and transcardially perfused with cold heparinized 0.9% NaCl. Brains were then removed from the mice and pooled, two brains of the same genotype per sample, to ensure adequate cell and RNA yield. The brains were then enzymatically dissociated for microglia isolation using the Neural Tissue Dissociation Kit (P), MACS Separation Columns (LS), and magnetic CD11b Microbeads from Miltenyi Biotec according to the manufacturer's protocol. Immediately after isolating the microglia, RNA was extracted from the cells for microarray analysis.

2015-02-20 | E-GEOD-57181 | biostudies-arrayexpress

Transcriptome sequencing of hippocampal tissue of APP/PS1 mice treated with rotating magnetic field for 12 months

Project description:Amyloid beta (Aβ) monomers aggregate to form fibrils and amyloid plaques, which is one of the important mechanisms in the pathogenesis of Alzheimer's disease (AD). Since the Aβ1-42 aggregation has prominent role in plaque formation, which eventually lead to the patient's brain lesions and cognitive impairment, an increasing number of studies have been devoted to reduce Aβ aggregation process to slow down AD progression. Since the diphenylalanine (FF) sequence is critical for amyloid aggregation, and it has been shown that magnetic fields can affect the alignment of peptide assembly due to the diamagnetic anisotropy of aromatic rings, here we used a moderate-intensity rotating magnetic field (RMF) to explore its effect on Aβ aggregation and AD pathogenesis. Our data showed that RMF can directly inhibit Aβ amyloid fibril formation and reduce Aβ-induced cytotoxicity on neural cells in vitro. Using the AD mouse model APP/PS1, we found that the RMF can restore their motor ability to the healthy control level. Their cognitive impairments, including exploration ability, spatial and non-spatial memory abilities, were also significantly alleviated. Tissue examinations reveal that RMF has reduced amyloid plaque accumulation, attenuated microglial activation ,and reduced oxidative stress in the APP/PS1 mouse brain. Therefore, our data demonstrate the great potential of RMF to be developed as a non-invasive, high-penetration physical approach to be applied in the treatment of AD.

2024-06-06 | GSE269222 | GEO

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