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Cited by 3Prion Diseases and Protein MisfoldingNeuroinflammation and Neurodegeneration MechanismsAlzheimer's disease research and treatments

Novel morphological glial alterations in the spectrum of prion disease types: A focus on common findings.

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Garcés, Moisés, Guijarro, Isabel M., Ritchie, Diane L., Badiola, Juan J., Monzón, Marta·2021·Pathogens
DOI 10.3390/pathogens10050596PMC PMC8153175
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Abstract

Human prion diseases are a group of rare fatal neurodegenerative diseases with sporadic, genetic, and acquired forms. They are neuropathologically characterized by pathological prion protein accumulation, neuronal death, and vacuolation. Classical immunological response has long been known not to play a major in prion diseases; however, gliosis is known to be a common feature although variable in extent and poorly described. In this investigation, astrogliosis and activated microglia in two brain regions were assessed and compared with non-neurologically affected patients in a representative sample across the spectrum of Creutzfeldt–Jakob disease (CJD) forms and subtypes in order to analyze the influence of prion strain on pathological processes. In this report, we choose to focus on features common to all CJD types rather than the diversity among them. Novel pathological changes in both glial cell types were found to be shared by all CJD types. Microglial activation correlated to astrogliosis. Spongiosis, but not pathological prion protein deposition, correlated to both astrogliosis and microgliosis. At the ultrastructural level, astrocytic glial filaments correlated with pathological changes associated with prion disease. These observations confirm that neuroglia play a prominent role in the neurodegenerative process of prion diseases, regardless of the causative prion type.

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  • Astrocytes are the first cells to exhibit aggregates of the scrapie form of the prion protein, resulting in profound alterations in astrocytic morphology.

    “Astrocytes are the first cells to exhibit aggregates of the scrapie form of the prion protein, resulting in profound alterations in astrocytic morphology.”

    From Interlaminar and varicose-projection astrocytes: toward a new understanding of the primate brain (2024) · cites this paper as Garcés et al., 2021

    The Discussion (page unavailable) says astrocytes are the first cells to show PrPsc deposits, and the Results describe substantial changes in astrocytic morphology. But the Discussion says a link between prion protein presence and those changes *might* exist; it does not establish that the deposits cause them. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Human prion diseases are a group of progressive and fatal conditions caused by pathological aggregates of misfolded prion protein which lead to protein deposits, neuronal death, vacuolation, and gliosis.

    “Among neurodegenerative disorders, human prion diseases are a group of progressive and fatal conditions caused by pathological aggregates of misfolded prion protein which lead to protein deposits, neuronal death, vacuolation, and gliosis (Garcés et al., 2021).”

    From Interlaminar and varicose-projection astrocytes: toward a new understanding of the primate brain (2024) · cites this paper as Garcés et al., 2021

    The Introduction describes CJD as progressive and inevitably fatal, identifies misfolded prion-protein accumulation as the generally held cause, and lists protein deposition, vacuolation, neuronal loss, and gliosis as prominent features. The Discussion cautions that misfolded protein deposits alone do not account for neurodegeneration, so the claim overstates the evidence by presenting all the listed changes as direct consequences of the aggregates. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • In prion diseases, ILAs show disorganized palisades and varicosities along their processes and terminal buttons, with features similar to those observed in Alzheimer's disease brains.

    “In particular, ILAs show disorganized palisades and varicosities along their processes and terminal buttons, with features similar to those observed in AD brains (Garcés et al., 2021).”

    From Interlaminar and varicose-projection astrocytes: toward a new understanding of the primate brain (2024) · cites this paper as Garcés et al., 2021

    The Results (§2.3.1) describe disorganized or fragmented interlaminar astroglial processes and increased terminal masses in CJD; the Discussion (§3) says these changes agree with those described in Alzheimer’s disease. However, the paper describes varicose fibers in cerebellar astroglia, not varicosities along interlaminar astroglial processes or terminal buttons. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Garcés, M., Guijarro, I. M., Ritchie, D. L., Badiola, J. J., & Monzón, M.
Affiliations
  • Universidad de Zaragoza (ES)
  • University of Edinburgh (GB)
Corresponding author
Monzón, Marta
ORCID
Venue
Pathogens
Publisher
MDPI AG
Published
2021-05-13
Volume
10
Issue
5
Pages
596
ISSN
2076-0817 (ISSN-L)
DOI
10.3390/pathogens10050596
PMC
PMC8153175
OpenAlex
W3162570144
Cited by
3
References
3
Citations by year
2024: 1 · 2023: 1 · 2022: 1
FWCI
0.24
Type
journal article
Language
en
Open access
Licence
Locations
  • Pathogens (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Edinburgh Research Explorer (University of Edinburgh) (publishedVersion, cc-by)
  • Zaguan (University of Zaragoza Repository) (publishedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
university of zaragoza (UZ2017-BIO-4)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Keywords
prion disease, Creutzfeldt-Jakob disease, astrocyte activation, microglial activation, spongiosis, prion strains, neurodegeneration, neuropathology

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