The effect of chronic stimulation of serotonin receptor type 7 on recognition, passive avoidance memory, hippocampal long-term potentiation, and neuronal apoptosis in the amyloid β protein treated rat

2018 ◽  
Vol 235 (5) ◽  
pp. 1513-1525 ◽  
Author(s):  
Siamak Shahidi ◽  
Sara Soleimani Asl ◽  
Alireza Komaki ◽  
Nasrin Hashemi-Firouzi
Keyword(s):  
Neuronal Apoptosis ◽  
Serotonin Receptor ◽  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Protein ◽  
Chronic Stimulation ◽  
Β Protein ◽  
Term Potentiation ◽  
Avoidance Memory

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Nature ◽  
2002 ◽  
Vol 416 (6880) ◽  
pp. 535-539 ◽  
Author(s):  
Dominic M. Walsh ◽  
Igor Klyubin ◽  
Julia V. Fadeeva ◽  
William K. Cullen ◽  
Roger Anwyl ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Term Potentiation

[Gly14]-humanin rescues long-term potentiation from amyloid β protein-induced impairment in the rat hippocampal CA1 region in vivo

Synapse ◽  
2010 ◽  
Vol 64 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Fen Guo ◽  
Wei Jing ◽  
Cun-Gen Ma ◽  
Mei-Na Wu ◽  
Jun-Fang Zhang ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Protein ◽  
Ca1 Region ◽  
Hippocampal Ca1 Region ◽  
Β Protein ◽  
Term Potentiation ◽  
Hippocampal Ca1

Amyloid-β oligomers: their production, toxicity and therapeutic inhibition

2002 ◽  
Vol 30 (4) ◽  
pp. 552-557 ◽  
Author(s):  
D. M. Walsh ◽  
I. Klyubin ◽  
J. V. Fadeeva ◽  
M. J. Rowan ◽  
D. J. Selkoe
Keyword(s):  
Amyloid Β ◽  
Long Term Potentiation ◽  
Specific Form ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Term Potentiation ◽  
Modelling Data

Despite extensive genetic and animal modelling data that support a central role for the amyloid β-protein (Aβ) in the genesis of Alzheimer's disease, the specific form(s) of Aβ which causes injury to neurons in vivo has not been identified. In the present study, we examine the importance of soluble, pre-fibrillar assemblies of Aβ as mediators of neurotoxicity. Specifically, we review the role of cell-derived SDS-stable oligomers, their blocking of hippocampal long-term potentiation in vivo and the finding that this blocking can be prevented by prior treatment of oligomer-producing cells withγ-secretase inhibitors.

scholarly journals Transglutaminase Induces Protofibril-like Amyloid β-Protein Assemblies That Are Protease-resistant and Inhibit Long-term Potentiation

2008 ◽  
Vol 283 (24) ◽  
pp. 16790-16800 ◽  
Author(s):  
Dean M. Hartley ◽  
Chaohui Zhao ◽  
Austin C. Speier ◽  
Gavitt A. Woodard ◽  
Shaomin Li ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Protein ◽  
Protein Assemblies ◽  
Β Protein ◽  
Term Potentiation

scholarly journals Soluble Aβ Inhibits Specific Signal Transduction Cascades Common to the Insulin Receptor Pathway

2007 ◽  
Vol 282 (46) ◽  
pp. 33305-33312 ◽  
Author(s):  
Matthew Townsend ◽  
Tapan Mehta ◽  
Dennis J. Selkoe
Keyword(s):  
Protein Kinase ◽  
Alzheimer Disease ◽  
Insulin Receptor ◽  
Hippocampal Neurons ◽  
Amyloid Β ◽  
Principal Component ◽  
Long Term Potentiation ◽  
Amyloid Β Protein ◽  
Term Potentiation

Numerous studies have now shown that the amyloid β-protein (Aβ), the principal component of cerebral plaques in Alzheimer disease, rapidly and potently inhibits certain forms of synaptic plasticity. The amyloid (or Aβ) hypothesis proposes that the continuous disruption of normal synaptic physiology by Aβ contributes to the development of Alzheimer disease. However, there is little consensus about how Aβ mediates this inhibition at the molecular level. Using mouse primary hippocampal neurons, we observed that a brief treatment with cell-derived, soluble, human Aβ disrupted the activation of three kinases (Erk/MAPK, CaMKII, and the phosphatidylinositol 3-kinase-activated protein Akt/protein kinase B) that are required for long term potentiation, whereas two other kinases (protein kinase A and protein kinase C) were stimulated normally. An antagonist of the insulin receptor family of tyrosine kinases was found to mimic the pattern of Aβ-mediated kinase inhibition. We then found that soluble Aβ binds to the insulin receptor and interferes with its insulin-induced autophosphorylation. Taken together, these data demonstrate that physiologically relevant levels of naturally secreted Aβ interfere with insulin receptor function in hippocampal neurons and prevent the rapid activation of specific kinases required for long term potentiation.

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