Immunohistochemical Analysis of Amyloid β-Protein Isoforms in CAA

2000 ◽  
pp. 179-188 ◽  
Author(s):  
Haruyasu Yamaguchi ◽  
Marion L. C. Maat-Schieman
Keyword(s):  
Amyloid Β ◽  
Immunohistochemical Analysis ◽  
Protein Isoforms ◽  
Amyloid Β Protein ◽  
Β Protein

scholarly journals Blood amyloid-β protein isoforms are affected by HIV-1 in a subtype-dependent pattern

2019 ◽  
Vol 26 (1) ◽  
pp. 3-13 ◽  
Author(s):  
Sérgio M. de Almeida ◽  
◽  
Clea E. Ribeiro ◽  
Indianara Rotta ◽  
Scott Letendre ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Protein Isoforms ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Hiv 1

Amyloid-β-protein isoforms in brain of subjects with PS1-linked, βAPP-linked and sporadic Alzheimer disease

1998 ◽  
Vol 56 (1-2) ◽  
pp. 178-185 ◽  
Author(s):  
Akira Tamaoka ◽  
Paul E Fraser ◽  
Kazuhiro Ishii ◽  
Naruhiko Sahara ◽  
Kazuharu Ozawa ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Β ◽  
Protein Isoforms ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Sporadic Alzheimer Disease

scholarly journals Surface enhanced Raman spectroscopy distinguishes amyloid Β-protein isoforms and conformational states

2018 ◽  
Vol 27 (8) ◽  
pp. 1427-1438 ◽  
Author(s):  
Xinke Yu ◽  
Eric Y. Hayden ◽  
Ming Xia ◽  
Owen Liang ◽  
Lisa Cheah ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Amyloid Β ◽  
Surface Enhanced Raman Spectroscopy ◽  
Protein Isoforms ◽  
Amyloid Β Protein ◽  
Conformational States ◽  
Β Protein ◽  
Surface Enhanced ◽  
Surface Enhanced Raman

scholarly journals Extracellular Protein Aggregates Colocalization and Neuronal Dystrophy in Comorbid Alzheimer’s and Creutzfeldt–Jakob Disease: A Micromorphological Pilot Study on 20 Brains

2021 ◽  
Vol 22 (4) ◽  
pp. 2099
Author(s):  
Nikol Jankovska ◽  
Tomas Olejar ◽  
Radoslav Matej
Keyword(s):  
Prion Protein ◽  
Fluorescent Microscopy ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Key Characteristics ◽  
Jakob Disease ◽  
Immunohistochemical Methods ◽  
Confocal Fluorescent Microscopy ◽  
Codon 129

Alzheimer’s disease (AD) and sporadic Creutzfeldt–Jakob disease (sCJD) are both characterized by extracellular pathologically conformed aggregates of amyloid proteins—amyloid β-protein (Aβ) and prion protein (PrPSc), respectively. To investigate the potential morphological colocalization of Aβ 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 Aβ 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 Aβ 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 Aβ/PrPSc co-aggregates. However, our data showed that PrPSc aggregation could dominate during co-aggregation with non-compact Aβ in the periphery of Aβ plaques.

scholarly journals Correction to: Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Woo Shik Shin ◽  
Jing Di ◽  
Qin Cao ◽  
Binsen Li ◽  
Paul M. Seidler ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Tau Aggregation

An amendment to this paper has been published and can be accessed via the original article.

Amyloid β-protein deposition in skin of patients with dementia

The Lancet ◽  
1992 ◽  
Vol 339 (8787) ◽  
pp. 245 ◽  
Author(s):  
Hilkka Soininen ◽  
Stina Syrjänen ◽  
Outi Heinonen ◽  
Heikki Neittaanmäki ◽  
Riitta Miettinen ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Protein Deposition ◽  
Β Protein

scholarly journals Amyloid-β Oligomers Induce Only Mild Changes to Inhibitory Bouton Dynamics

2021 ◽  
Vol 5 (1) ◽  
pp. 153-160 ◽  
Author(s):  
Marvin Ruiter ◽  
Christine Lützkendorf ◽  
Jian Liang ◽  
Corette J. Wierenga
Keyword(s):  
Hippocampal Slices ◽  
Inhibitory Neuron ◽  
Amyloid Β ◽  
Inhibitory Neurons ◽  
Inhibitory Synapses ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein ◽  
Plaque Load ◽  
Early Alzheimer’S Disease

The amyloid-β protein precursor is highly expressed in a subset of inhibitory neuron in the hippocampus, and inhibitory neurons have been suggested to play an important role in early Alzheimer’s disease plaque load. Here we investigated bouton dynamics in axons of hippocampal interneurons in two independent amyloidosis models. Short-term (24 h) amyloid-β (Aβ)-oligomer application to organotypic hippocampal slices slightly increased inhibitory bouton dynamics, but bouton density and dynamics were unchanged in hippocampus slices of young-adult AppNL - F - G-mice, in which Aβ levels are chronically elevated. These results indicate that loss or defective adaptation of inhibitory synapses are not a major contribution to Aβ-induced hyperexcitability.

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