Limbic system synaptic dysfunctions associated with prion disease onset

Misfolding of normal prion protein (PrP<sup>C</sup>) to pathological isoforms (prions) causes prion diseases (PrDs) with clinical manifestations including cognitive decline and mood-related behavioral changes. Cognition and mood are linked to the neurophysiology of the limbic system. Little is known about how the disease affects the synaptic activity in brain parts associated with this system. We hypothesize that the dysfunction of synaptic transmission in the limbic regions correlates with the onset of reduced cognition and behavioral deficits. Here, we studied how prion infection in mice disrupts the synaptic function in three limbic regions, the hippocampus, hypothalamus, and amygdala, at a pre-clinical stage (mid-incubation period) and early clinical onset. PrD caused calcium flux dysregulation associated with lesser spontaneous synchronous neuronal firing and slowing neural oscillation at the pre-clinical stage in the hippocampal CA1, ventral medial hypothalamus, and basolateral amygdala (BLA). At clinical onset, synaptic transmission and synaptic plasticity became significantly disrupted. This correlated with a substantial depletion of the soluble prion protein, loss of total synapses, abnormal neurotransmitter levels and synaptic release, decline in synaptic vesicle recycling, and cytoskeletal damage. Further, the amygdala exhibited distinct disease-related changes in synaptic morphology and physiology compared with the other regions, but generally to a lesser degree, demonstrating how different rates of damage in the limbic system influence the evolution of clinical disease. Overall, PrD causes synaptic damage in three essential limbic regions starting at a preclinical stage and resulting in synaptic plasticity dysfunction correlated with early disease signs. Therapeutic drugs that alleviate these early neuronal dysfunctions may significantly delay clinical onset.

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Publication Details

Journal
Acta Neuropathologica Communications
Published
2024-12-20
DOI
https://doi.org/10.1186/s40478-024-01905-w
Citations
4
Primary Topic
Prion Diseases and Protein Misfolding
Type
article
Field-Weighted Citation Impact
0.94

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article

Limbic system synaptic dysfunctions associated with prion disease onset

Eric Bohrnsen, Bradley R. Groveman, Cathryn L. Haigh, Cindi L. Schwartz et al.
4 citations
Acta Neuropathologica Communications
Prion Diseases and Protein Misfolding
0.94
article

Limbic system synaptic dysfunctions associated with prion disease onset

Eric Bohrnsen, Bradley R. Groveman, Cathryn L. Haigh, Cindi L. Schwartz, Benjamin Schwarz, Hadil El Soufi, Jacqueline M. Leung, Brent Race, Simote Totauhelotu Foliaki, Christine A. Schneider, Katie Williams, Cole D. Kimzey, Emmett A. Dews
article en
4 citations

Abstract

Misfolding of normal prion protein (PrP<sup>C</sup>) to pathological isoforms (prions) causes prion diseases (PrDs) with clinical manifestations including cognitive decline and mood-related behavioral changes. Cognition and mood are linked to the neurophysiology of the limbic system. Little is known about how the disease affects the synaptic activity in brain parts associated with this system. We hypothesize that the dysfunction of synaptic transmission in the limbic regions correlates with the onset of reduced cognition and behavioral deficits. Here, we studied how prion infection in mice disrupts the synaptic function in three limbic regions, the hippocampus, hypothalamus, and amygdala, at a pre-clinical stage (mid-incubation period) and early clinical onset. PrD caused calcium flux dysregulation associated with lesser spontaneous synchronous neuronal firing and slowing neural oscillation at the pre-clinical stage in the hippocampal CA1, ventral medial hypothalamus, and basolateral amygdala (BLA). At clinical onset, synaptic transmission and synaptic plasticity became significantly disrupted. This correlated with a substantial depletion of the soluble prion protein, loss of total synapses, abnormal neurotransmitter levels and synaptic release, decline in synaptic vesicle recycling, and cytoskeletal damage. Further, the amygdala exhibited distinct disease-related changes in synaptic morphology and physiology compared with the other regions, but generally to a lesser degree, demonstrating how different rates of damage in the limbic system influence the evolution of clinical disease. Overall, PrD causes synaptic damage in three essential limbic regions starting at a preclinical stage and resulting in synaptic plasticity dysfunction correlated with early disease signs. Therapeutic drugs that alleviate these early neuronal dysfunctions may significantly delay clinical onset.

Acta Neuropathologica CommunicationsVol. 12(1)
National Institutes of Health (US), National Institute of Allergy and Infectious Diseases (US)
Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, National Institute of Allergy and Infectious Diseases, NHLBI Division of Intramural Research
Good health and well-being
Openalex Percentile: Top 24%
Prion Diseases and Protein Misfolding
0.94
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