Title:

TDP-43-metabolism interplay in neurodegenerative disorders : PhD thesis

Creator:

Gbadamosi, Ismail

Contributor:

Kaczmarek, Leszek (1957– ) : Supervisor ; Jawaid, Ali : Auxiliary supervisor

Publisher:

Nencki Institute of Experimental Biology PAS

Place of publishing:

Warsaw

Date issued/created:

2025

Description:

IX, [4], 173 pages : illustrations ; 30 cm ; Note: partially incorrect page numbering [4] ; Bibliography ; Summary in Polish

Degree name:

PhD in Biological Sciences

Degree discipline :

Biological Sciences

Degree grantor:

Nencki Institute of Experimental Biology PAS ; degree obtained: 2026

Type of object:

Thesis

Subject and Keywords:

Amyotrophic lateral sclerosis ; AMPK ; Energy metabolism ; Frontotemporal lobar degeneration ; Motor neurons ; Metabolic sensing ; Systemic metabolism ; TDP-43

Abstract:

Cytoplasmic aggregation and nuclear depletion of TAR DNA-binding protein 43 (TDP-43) represent key pathological features in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Since TDP-43 is a critical regulator of RNA processing and metabolism, its dysfunction contributes to cellular stress through both loss- and gain-of-function mechanisms. Interestingly, metabolic conditions commonly linked to poor systemic health, including type 2 diabetes mellitus (T2DM), dyslipidemia, and elevated body mass index (BMI), are associated with prolonged survival in ALS. Conversely, high levels of physical activity have been linked to increased ALS risk, suggesting a complex interplay between metabolism and TDP-43- mediated neurodegeneration. This study systematically investigates the impact of TDP-43 dysfunction—via knockdown or M337V mutation—on cellular energy metabolism and metabolic sensing, with a focus on motor neuron vulnerability. Using NSC34 motor neuron-like cells, TDP-43 knockdown induced a hypermetabolic state characterized by increased glycolysis, oxidative phosphorylation, and ATP production, accompanied by persistent activation of AMP-activated protein kinase (AMPK). In contrast, mutant TDP-43 disrupted AMPK regulation primarily under metabolic stress, leading to prolonged AMPK activation during recovery phases. Comparative analyses in BV2 microglia and N2A neuroblastoma cells highlighted distinct cell-specific metabolic responses to TDP-43 perturbation. To explore how systemic metabolic status influences TDP-43–associated metabolic changes, we treated TDP-43–deficient NSC34 motor neuron–like cells with serum from mice subjected to voluntary exercise (VE) or a high-fat diet (HFD), revealing a sex-dependent modulation of those metabolic alterations. Female-derived serum more strongly regulated glycolytic and mitochondrial responses in both motor neurons and microglia. Finally, integration of patient-derived transcriptomic datasets from ALS and FTLD postmortem tissues with NSC34 RNA-seq data identified both common and disease-specific metabolic dysregulation. ALS transcriptomes were enriched for lipid metabolism and insulin signaling pathways, while FTLD transcriptomes showed predominant alterations in RNA processing and translation. Collectively, these findings demonstrate that TDP-43 dysfunction disrupts cellular metabolism in a cell-type- and context-dependent manner, with motor neurons displaying heightened vulnerability. The data further suggest that systemic metabolic states modulate TDP-43-driven metabolic stress, providing insights into potential metabolic targets for therapeutic intervention in ALS and FTLD.

Resource type:

Text

Detailed Resource Type:

PhD Dissertations

Source:

IBD PAN, call no. 20888

Language:

eng

Language of abstract:

pol

Rights:

Rights Reserved - Free Access

Terms of use:

Copyright-protected material. May be used within the limits of statutory user freedoms

Copyright holder:

Publication made available with the written permission of the author

Digitizing institution:

Nencki Institute of Experimental Biology of the Polish Academy of Sciences

Original in:

Library of the Nencki Institute of Experimental Biology PAS

Access:

Open

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