Isolation of Low-n Amyloid β-Protein Oligomers from Cultured Cells, CSF, and Brain

2010 ◽  
pp. 33-44 ◽  
Author(s):  
Ganesh M. Shankar ◽  
Alfred T. Welzel ◽  
Jessica M. McDonald ◽  
Dennis J. Selkoe ◽  
Dominic M. Walsh
Keyword(s):  
Cultured Cells ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein

scholarly journals Enhanced amyloid-β generation by γ-secretase complex in DRM microdomains with reduced cholesterol levels

2019 ◽  
Vol 29 (3) ◽  
pp. 382-393 ◽  
Author(s):  
Saori Hata ◽  
Anqi Hu ◽  
Yi Piao ◽  
Tadashi Nakaya ◽  
Hidenori Taru ◽  
...  
Keyword(s):  
Cultured Cells ◽  
Late Onset ◽  
Senile Plaques ◽  
Amyloid Β ◽  
Cholesterol Content ◽  
Amyloid Β Protein ◽  
Tissue Samples ◽  
Β Protein ◽  
Aβ Generation ◽  
Carboxy Terminal

Abstract A neuropathologic hallmark of Alzheimer’s disease (AD) is the presence of senile plaques that contain neurotoxic amyloid-β protein (Aβ) species, which are generated by the cleavage of amyloid β-protein precursor by secretases such as the γ-secretase complex, preferentially located in detergent-resistant membrane (DRM) regions and comprising endoproteolysed amino- and carboxy-terminal fragments of presenilin, nicastrin, anterior pharynx defective 1 and presenilin enhancer 2. Whereas some of familial AD patients harbor causative PSEN mutations that lead to more generation of neurotoxic Aβ42, the contribution of Aβ generation to sporadic/late-onset AD remains unclear. We found that the carboxy-terminal fragment of presenilin 1 was redistributed from DRM regions to detergent-soluble membrane (non-DRM) regions in brain tissue samples from individuals with sporadic AD. DRM fractions from AD brain sample had the ability to generate significantly more Aβ and had a lower cholesterol content than DRM fractions from non-demented control subjects. We further demonstrated that lowering the cholesterol content of DRM regions from cultured cells contributed to the redistribution of γ-secretase components and Aβ production. Taken together, the present analyses suggest that the lowered cholesterol content in DRM regions may be a cause of sporadic/late-onset AD by enhancing overall Aβ generation.

Amyloid β-protein precursor (APP) of cultured cells: Secretory and non-secretory forms of APP

1990 ◽  
Vol 97 (1) ◽  
pp. 43-52 ◽  
Author(s):  
Fuyuki Kametani ◽  
Seiichi Haga ◽  
Kikuko Tanaka ◽  
Tsuyoshi Ishii
Keyword(s):  
Cultured Cells ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein

Tenuigenin treatment decreases secretion of the Alzheimer’s disease amyloid β-protein in cultured cells

2004 ◽  
Vol 367 (1) ◽  
pp. 123-128 ◽  
Author(s):  
Hongxiao Jia ◽  
Yong Jiang ◽  
Yan Ruan ◽  
Yanbo Zhang ◽  
Xin Ma ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cultured Cells ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein

Amyloid β protein substituent peptides do not interact with the substance P receptor expressed in cultured cells

1991 ◽  
Vol 11 (2) ◽  
pp. 177-180 ◽  
Author(s):  
Masato Mitsuhashi ◽  
Tatsuo Akitaya ◽  
Christoph W. Turk ◽  
Donald G. Payan
Keyword(s):  
Substance P ◽  
Cultured Cells ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Substance P Receptor

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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