Evidence map›Paper›PMID 41173863›Full record

ArticleScientific reports2025

Seeding Alzheimer's disease-associated tau pathology in MAPT knock-in primary neurons causes early axonopathy and synaptic dysfunction.

Rebecca L Mueller, Benjamin Combs, Nicholas M Kanaan

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Rebecca L MuellerDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA.
Benjamin CombsDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA.
Nicholas M KanaanDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA. nkanaan@msu.edu.

Funding

Tau Conformation in Tauopathies and Neuronal FunctionR01NS082730 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS, KANAAN, NICHOLAS M · 2014 to 2023
$7.0M
Tau-Mediated Regulation and Dysregulation of Protein Phosphatase 1R01AG067762 · NIA · MICHIGAN STATE UNIVERSITY · PI KANAAN, NICHOLAS M · 2020 to 2024
$2.6M
Integrative Pharmacological Sciences Training Program (IPSTP)T32GM142521 · NIGMS · MICHIGAN STATE UNIVERSITY · PI ANNE M. DORRANCE, Gina Marie Leinninger · 2021 to 2026
$2.4M
Tau Conformation in Tauopathies and Neuronal FunctionRF1NS082730 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS, KANAAN, NICHOLAS M · 2025 to 2025
$1.6M
Investigating the functional consequences of seeding in mammalian primary neurons with Alzheimer’s Disease brain-derived tau filamentsF31AG074521 · NIA · MICHIGAN STATE UNIVERSITY · PI MUELLER, REBECCA LYNN · 2022 to 2023
$59k
NIA NIH HHS F31 AG074521NIA NIH HHS R01 AG067762NIGMS NIH HHS T32 GM142521NINDS NIH HHS R01 NS082730NINDS NIH HHS RF1 NS082730
6 · The paper itself

Abstract

The progressive accumulation of pathological tau is a hallmark of Alzheimer's disease (AD). The bulk of existing in vitro and in vivo evidence suggests that pathological tau forms can seed further aggregation of the protein. However, many of the subsequent functional consequences following the formation of pathogenic tau aggregates are not yet fully understood. Here, we utilized the tau seeding phenomenon to induce the formation of pathogenic tau and identify intracellular consequences in a neuron culture model of AD-associated tauopathy. Primary neurons from human tau knock-in (MAPT-KI) mice were seeded with human AD brain-derived insoluble tau (AD-tau). Microscopy and biochemical assays were used to characterize the pathological tau species formed, as well as the extent of neuronal, axonal and synaptic degeneration in seeded MAPT-KI neurons. In addition, high-density microelectrode arrays were used to assess synaptic functionality in seeded MAPT-KI neuron cultures. Human-derived AD-tau seeded intracellular endogenous tau inclusions that contained AD-associated modifications (i.e. phosphorylation at the PHF1, AT8, and pS422 antibody epitopes) and adopted multiple pathogenic conformations (i.e. oligomers and exposure of an N-terminal phosphatase activating domain; PAD). Tau inclusions, containing pS422 + and PAD-exposed tau, colocalized with active glycogen synthase kinase 3β (the kinase involved in PAD-mediated axonal transport impairment) and accumulations of axonal transport cargo proteins (i.e. synaptophysin and amyloid precursor protein) in dystrophic axons. While there was no overt axonal degeneration or cell loss, intact excitatory synapses were reduced in the AD-tau neurons. Neuron cultures treated with AD-tau exhibited an N-methyl-D-aspartate receptor-dependent increase in network burst frequency when activated with glutamate as measured through high-density microelectrode arrays. Together, the data demonstrate that the AD-tau seeded MAPT-KI neuron model exhibits features associated with neuronal dysfunction resembling those that occur early in human disease (i.e. axonal pathology and dystrophy, hyperexcitability and hypersynchrony), without causing overt neurodegeneration.

Indexed as

Alzheimer DiseaseAxonsNeuronsSynapsestau ProteinsAnimalsCells, CulturedDisease Models, AnimalGene Knock-In TechniquesHumansMiceMice, TransgenicPhosphorylationTauopathiesMAPT protein, humantau Proteins

Identifiers

PMID41173863
PMCPMC12578843

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.