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Extracellular Protein Aggregates Colocalization and Neuronal Dystrophy in Comorbid Alzheimer's and Creutzfeldt-Jakob Disease: A Micromorphological Pilot Study on 20 Brains

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064190%3A_____%2F21%3AN0000098" target="_blank" >RIV/00064190:_____/21:N0000098 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11120/21:43921205 RIV/00216208:11110/21:10425200 RIV/00064165:_____/21:10425200 RIV/00064173:_____/21:N0000145

  • Result on the web

    <a href="http://dx.doi.org/10.3390/ijms22042099" target="_blank" >http://dx.doi.org/10.3390/ijms22042099</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms22042099" target="_blank" >10.3390/ijms22042099</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Extracellular Protein Aggregates Colocalization and Neuronal Dystrophy in Comorbid Alzheimer's and Creutzfeldt-Jakob Disease: A Micromorphological Pilot Study on 20 Brains

  • Original language description

    Alzheimer's disease (AD) and sporadic Creutzfeldt-Jakob disease (sCJD) are both characterized by extracellular pathologically conformed aggregates of amyloid proteins-amyloid beta-protein (A beta) and prion protein (PrPSc), respectively. To investigate the potential morphological colocalization of A beta and PrPSc aggregates, we examined the hippocampal regions (archicortex and neocortex) of 20 subjects with confirmed comorbid AD and sCJD using neurohistopathological analyses, immunohistochemical methods, and confocal fluorescent microscopy. Our data showed that extracellular A beta and PrPSc aggregates tended to be, in most cases, located separately, and "compound" plaques were relatively rare. We observed PrPSc plaque-like structures in the periphery of the non-compact parts of A beta plaques, as well as in tau protein-positive dystrophic structures. The AD ABC score according to the NIA-Alzheimer's association guidelines, and prion protein subtype with codon 129 methionine-valine (M/V) polymorphisms in sCJD, while representing key characteristics of these diseases, did not correlate with the morphology of the A beta/PrPSc co-aggregates. However, our data showed that PrPSc aggregation could dominate during co-aggregation with non-compact A beta in the periphery of A beta plaques.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    4

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    12

  • Pages from-to

    Article Number 2099

  • UT code for WoS article

    000623837000001

  • EID of the result in the Scopus database

    2-s2.0-85100944415