Understanding the natural variability of prion diseases
Abstract
Prion diseases are a heterogeneous group of disorders with an invariably fatal disease course. Although various etiologies have been proposed it is apparent that at least a subset of these diseases are of infectious nature. An essential part of the infectious agent, termed the prion, is mainly composed of an abnormal isoform (PrP(Sc)) of a host-encoded normal cellular protein (PrP(C)). The molecular details of the pathophysiology of this group of diseases are unclear but the conversion of PrP(C) to PrP(Sc) plays a fundamental role. In all human prion diseases, PrP(Sc) is deposited in the central nervous system. These disorders include sporadic, genetic and acquired Creutzfeldt-Jakob disease. The molecular classification of human prion diseases is important in order to understand underlying disease mechanisms and for the development of novel therapy protocols. Current classification systems are based on the assessment of clinical presentation, genetic investigations, neuropathological findings and biochemical analysis of PrP(Sc).
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The heterogeneity of PrPSc deposition patterns is higher in human prion diseases and comprises synaptic, perivacuolar, plaque-like, kuru-plaque, florid-plaque, punctuate, perineuronal, and intraneuronal patterns, which might occur side-by-side or even overlapping in the same patient.
“Although the deposition patterns of misfolded PrPSc are diverse in murine models of prion disease, the heterogeneity of PrPSc deposition patterns is higher in human prion diseases and comprises synaptic, perivacuolar, plaque-like, kuru-plaque, florid-plaque, punctuate, perineuronal, and intraneuronal patterns, which might occur side-by-side or even overlapping in the same patient [119,120].”
From Loss of Homeostatic Microglia Signature in Prion Diseases (2022) · cites this paper as [120]
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Loss of Homeostatic Microglia Signature in Prion Diseases
Wang, Y., Hartmann, K., Thies, E., Mohammadi, B., Altmeppen, H., Sepulveda-Falla, D., Glatzel, M., & Krasemann, S. (2022) · Cells · doi:10.3390/cells11192948 · Cited by 12 · see citing works
Self-citation
- Authors
- Geissen, M., Krasemann, S., Matschke, J., & Glatzel, M.
- Affiliations
- University Medical Center Hamburg-Eppendorf (DE)
- Corresponding author
- Glatzel, Markus
- Venue
- Vaccine
- Publisher
- Elsevier BV
- Published
- 2007-07
- Volume
- 25
- Issue
- 30
- Pages
- 5631-5636
- ISSN
- 0264-410X (ISSN-L)
- OpenAlex
- W2018428043
- Cited by
- 24
- References
- 57
- Citations by year
- 2022: 2 · 2020: 2 · 2018: 1 · 2017: 4 · 2016: 1 · 2015: 1 · 2014: 3 · 2013: 3 · 2012: 1
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Vaccine (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Keywords
- prion disease, natural variation, prion protein, PrPSc, Creutzfeldt-Jakob disease, sporadic CJD, molecular classification, neuropathology, pathophysiology
- MeSH terms
- Central Nervous System, Humans, Prions, Prion Diseases
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