Extracellular Prion Protein Aggregates in Nine Gerstmann-Straussler-Scheinker Syndrome Subjects with Mutation P102L: A Micromorphological Study and Comparison with Literature Data
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064190%3A_____%2F21%3AN0000007" target="_blank" >RIV/00064190:_____/21:N0000007 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11120/21:43922682 RIV/00216208:11110/21:10435476 RIV/00064165:_____/21:10435476 RIV/00064173:_____/21:N0000144
Result on the web
<a href="http://mdpi.com/1422-0067/22/24/13303" target="_blank" >http://mdpi.com/1422-0067/22/24/13303</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms222413303" target="_blank" >10.3390/ijms222413303</a>
Alternative languages
Result language
angličtina
Original language name
Extracellular Prion Protein Aggregates in Nine Gerstmann-Straussler-Scheinker Syndrome Subjects with Mutation P102L: A Micromorphological Study and Comparison with Literature Data
Original language description
Gerstmann-Straussler-Scheinker syndrome (GSS) is a hereditary neurodegenerative disease characterized by extracellular aggregations of pathological prion protein (PrP) forming characteristic plaques. Our study aimed to evaluate the micromorphology and protein composition of these plaques in relation to age, disease duration, and co-expression of other pathogenic proteins related to other neurodegenerations. Hippocampal regions of nine clinically, neuropathologically, and genetically confirmed GSS subjects were investigated using immunohistochemistry and multichannel confocal fluorescent microscopy. Most pathognomic prion protein plaques were small (2-10 mu m), condensed, globous, and did not contain any of the other investigated proteinaceous components, particularly dystrophic neurites. Equally rare (in two cases out of nine) were plaques over 50 mu m having predominantly fibrillar structure and exhibit the presence of dystrophic neuritic structures; in one case, the plaques also included bulbous dystrophic neurites. Co-expression with hyperphosphorylated protein tau protein or amyloid beta-peptide (A beta) in GSS PrP plaques is generally a rare observation, even in cases with comorbid neuropathology. The dominant picture of the GSS brain is small, condensed plaques, often multicentric, while presence of dystrophic neuritic changes accumulating hyperphosphorylated protein tau or A beta in the PrP plaques are rare and, thus, their presence probably constitutes a trivial observation without any relationship to GSS development and progression.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International journal of molecular sciences
ISSN
1422-0067
e-ISSN
1422-0067
Volume of the periodical
22
Issue of the periodical within the volume
24
Country of publishing house
CH - SWITZERLAND
Number of pages
12
Pages from-to
Article Number 13303
UT code for WoS article
000739026800001
EID of the result in the Scopus database
2-s2.0-85120771118