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 Protective Effect of Green Perilla-Derived Chalcone Derivative DDC on Amyloid β Protein-Induced Neurotoxicity in Primary Cortical Neurons

2019 ◽  
Vol 42 (11) ◽  
pp. 1942-1946 ◽  
Author(s):  
Mami Iwasaki ◽  
Naotaka Izuo ◽  
Yasuhiko Izumi ◽  
Yuki Takada-Takatori ◽  
Akinori Akaike ◽  
...  
Keyword(s):  
Protective Effect ◽  
Cortical Neurons ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Primary Cortical Neurons ◽  
Chalcone Derivative ◽  
Β Protein

scholarly journals Protective Effect of T-588 on Toxic Damage by Serum Deprivation and Amyloid-β Protein in Cultured Neurons

2003 ◽  
Vol 92 (2) ◽  
pp. 153-156 ◽  
Author(s):  
Akiko Yamamuro ◽  
Yukio Ago ◽  
Sadaaki Maeda ◽  
Yoshiyuki Sakai ◽  
Akemichi Baba ◽  
...  
Keyword(s):  
Protective Effect ◽  
Amyloid Β ◽  
Serum Deprivation ◽  
Cultured Neurons ◽  
Amyloid Β Protein ◽  
Toxic Damage ◽  
Β Protein

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

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.

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