Dose-dependent and sequence-sensitive effects of amyloid-β peptide on neurosteroidogenesis in human neuroblastoma cells

2008 ◽  
Vol 52 (6) ◽  
pp. 948-955 ◽  
Author(s):  
Véronique Schaeffer ◽  
Laurence Meyer ◽  
Christine Patte-Mensah ◽  
Anne Eckert ◽  
Ayikoe G. Mensah-Nyagan
Keyword(s):  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
Dose Dependent

scholarly journals The antioxidant xanthorrhizol prevents amyloid-β-induced oxidative modification and inactivation of neprilysin

2018 ◽  
Vol 38 (1) ◽  
Author(s):  
Chol Seung Lim ◽  
Jung-Soo Han
Keyword(s):  
Therapeutic Potential ◽  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Enzymatic Activities ◽  
Oxidative Modification ◽  
Amyloid Β Peptide ◽  
Oxygen Species ◽  
Human Neuroblastoma Cells ◽  
Neuroprotective Effects ◽  
Human Neuroblastoma

Activity of neprilysin (NEP), the major protease which cleaves amyloid-β peptide (Aβ), is reportedly reduced in the brains of patients with Alzheimer’s disease (AD). Accumulation of Aβ generates reactive oxygen species (ROS) such as 4-hydroxynonenal (HNE), and then reduces activities of Aβ-degrading enzymes including NEP. Xanthorrhizol (Xan), a natural sesquiterpenoid, has been reported to possess antioxidant and anti-inflammatory properties. The present study examined the effects of Xan on HNE- or oligomeric Aβ42-induced oxidative modification of NEP protein. Xan was added to the HNE- or oligomeric Aβ42-treated SK-N-SH human neuroblastoma cells and then levels, oxidative modification and enzymatic activities of NEP protein were measured. Increased HNE levels on NEP proteins and reduced enzymatic activities of NEP were observed in the HNE- or oligomeric Aβ42-treated cells. Xan reduced HNE levels on NEP proteins and preserved enzymatic activities of NEP in HNE- or oligomeric Aβ42-treated cells. Xan reduced Aβ42 accumulation and protected neurones against oligomeric Aβ42-induced neurotoxicity through preservation of NEP activities. These findings indicate that Xan possesses therapeutic potential for the treatment of neurodegenerative diseases, including AD, and suggest a potential mechanism for the neuroprotective effects of antioxidants for the prevention of AD.

scholarly journals Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

2021 ◽  
Vol 15 ◽  
Author(s):  
Ryan Limbocker ◽  
Roxine Staats ◽  
Sean Chia ◽  
Francesco S. Ruggeri ◽  
Benedetta Mannini ◽  
...  
Keyword(s):  
Small Molecules ◽  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
Parkinson’S Diseases ◽  
Wide Range ◽  
Opposing Effects

The aberrant aggregation of proteins is a key molecular event in the development and progression of a wide range of neurodegenerative disorders. We have shown previously that squalamine and trodusquemine, two natural products in the aminosterol class, can modulate the aggregation of the amyloid-β peptide (Aβ) and of α-synuclein (αS), which are associated with Alzheimer’s and Parkinson’s diseases. In this work, we expand our previous analyses to two squalamine derivatives, des-squalamine and α-squalamine, obtaining further insights into the mechanism by which aminosterols modulate Aβ and αS aggregation. We then characterize the ability of these small molecules to alter the physicochemical properties of stabilized oligomeric species in vitro and to suppress the toxicity of these aggregates to varying degrees toward human neuroblastoma cells. We found that, despite the fact that these aminosterols exert opposing effects on Aβ and αS aggregation under the conditions that we tested, the modifications that they induced to the toxicity of oligomers were similar. Our results indicate that the suppression of toxicity is mediated by the displacement of toxic oligomeric species from cellular membranes by the aminosterols. This study, thus, provides evidence that aminosterols could be rationally optimized in drug discovery programs to target oligomer toxicity in Alzheimer’s and Parkinson’s diseases.

scholarly journals New Alzheimer Amyloid β Responsive Genes Identified in Human Neuroblastoma Cells by Hierarchical Clustering

PLoS ONE ◽  
2009 ◽  
Vol 4 (8) ◽  
pp. e6779 ◽  
Author(s):  
Markus Uhrig ◽  
Carina Ittrich ◽  
Verena Wiedmann ◽  
Yuri Knyazev ◽  
Annette Weninger ◽  
...  
Keyword(s):  
Hierarchical Clustering ◽  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma

scholarly journals Carnosic acid suppresses the production of amyloid-β 1–42 by inducing the metalloprotease gene TACE/ADAM17 in SH-SY5Y human neuroblastoma cells

2013 ◽  
Vol 75 (2) ◽  
pp. 94-102 ◽  
Author(s):  
Pengfei Meng ◽  
Hidemi Yoshida ◽  
Tomoh Matsumiya ◽  
Tadaatsu Imaizumi ◽  
Kunikazu Tanji ◽  
...  
Keyword(s):  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Carnosic Acid ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma

Rebamipide reduces amyloid-β 1–42 (Aβ42) production and ameliorates Aβ43-lowered cell viability in cultured SH-SY5Y human neuroblastoma cells

2017 ◽  
Vol 124 ◽  
pp. 40-50 ◽  
Author(s):  
Kenta Fukui ◽  
Kazuma Yachi ◽  
Hidemi Yoshida ◽  
Kunikazu Tanji ◽  
Tomoh Matsumiya ◽  
...  
Keyword(s):  
Cell Viability ◽  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma

Carnosic acid attenuates apoptosis induced by amyloid-β 1–42 or 1–43 in SH-SY5Y human neuroblastoma cells

2015 ◽  
Vol 94 ◽  
pp. 1-9 ◽  
Author(s):  
Pengfei Meng ◽  
Hidemi Yoshida ◽  
Kunikazu Tanji ◽  
Tomoh Matsumiya ◽  
Fei Xing ◽  
...  
Keyword(s):  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Carnosic Acid ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma
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