Leaf and stem of Vitis amurensis and its active components protect against amyloid β protein (25–35)-induced neurotoxicity

2010 ◽  
Vol 33 (10) ◽  
pp. 1655-1664 ◽  
Author(s):  
Ha Yeon Jeong ◽  
Joo Youn Kim ◽  
Hong Kyu Lee ◽  
Do Thi Ha ◽  
Kyung-Sik Song ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Vitis Amurensis ◽  
Amyloid Β Protein ◽  
Active Components ◽  
Β Protein

Protective effect of Vitis amurensis against amyloid β protein (25–35)-induced neurotoxicity

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
JY Kim ◽  
HS Ju ◽  
KH Bae ◽  
YH Seong
Keyword(s):  
Protective Effect ◽  
Amyloid Β ◽  
Vitis Amurensis ◽  
Amyloid Β Protein ◽  
Β Protein

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.

scholarly journals The Amyloid β Protein Induces Oxidative Damage of Mitochondrial DNA

1997 ◽  
Vol 56 (12) ◽  
pp. 1356-1362 ◽  
Author(s):  
PETER BOZNER ◽  
VALENTINA GRISHKO ◽  
SUSAN P. LEDOUX ◽  
GLENN L. WILSON ◽  
Y-C CHYAN ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Oxidative Damage ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein
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