DCP-LA neutralizes mutant amyloid β peptide-induced impairment of long-term potentiation and spatial learning

2010 ◽  
Vol 206 (1) ◽  
pp. 151-154 ◽  
Author(s):  
Tetsu Nagata ◽  
Takemi Tominaga ◽  
Hiroshi Mori ◽  
Takahiro Yaguchi ◽  
Tomoyuki Nishizaki
Keyword(s):  
Spatial Learning ◽  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Peptide ◽  
Term Potentiation

scholarly journals Amyloid-β Peptide Is Needed for cGMP-Induced Long-Term Potentiation and Memory

2017 ◽  
Vol 37 (29) ◽  
pp. 6926-6937 ◽  
Author(s):  
Agostino Palmeri ◽  
Roberta Ricciarelli ◽  
Walter Gulisano ◽  
Daniela Rivera ◽  
Claudia Rebosio ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Long Term Potentiation ◽  
Amyloid Β Peptide ◽  
Term Potentiation

Hippocampal long-term potentiation and spatial learning in the rat: effects of GABAB receptor blockade

Neuroscience ◽  
1996 ◽  
Vol 74 (2) ◽  
pp. 331-339 ◽  
Author(s):  
F.H Brucato ◽  
E.D Levin ◽  
D.D Mott ◽  
D.V Lewis ◽  
W.A Wilson ◽  
...  
Keyword(s):  
Spatial Learning ◽  
Gabab Receptor ◽  
Long Term Potentiation ◽  
Receptor Blockade ◽  
Term Potentiation

Dissociation between genes activated in long-term potentiation and in spatial learning in the rat

1998 ◽  
Vol 251 (1) ◽  
pp. 41-44 ◽  
Author(s):  
G Richter-Levin ◽  
K.L Thomas ◽  
S.P Hunt ◽  
T.V.P Bliss
Keyword(s):  
Spatial Learning ◽  
Long Term Potentiation ◽  
Term Potentiation

Neuroprotective properties of mitochondria-targeted antioxidants of the SkQ-type

2016 ◽  
Vol 27 (8) ◽  
pp. 849-855 ◽  
Author(s):  
Nickolay K. Isaev ◽  
Elena V. Stelmashook ◽  
Elisaveta E. Genrikhs ◽  
Galina A. Korshunova ◽  
Natalya V. Sumbatyan ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Brain Area ◽  
Hippocampal Slices ◽  
Amyloid Β ◽  
Long Term Potentiation ◽  
Term Potentiation ◽  
Neuroprotective Action

AbstractIn 2008, using a model of compression brain ischemia, we presented the first evidence that mitochondria-targeted antioxidants of the SkQ family, i.e. SkQR1 [10-(6′-plastoquinonyl)decylrhodamine], have a neuroprotective action. It was shown that intraperitoneal injections of SkQR1 (0.5–1 μmol/kg) 1 day before ischemia significantly decreased the damaged brain area. Later, we studied in more detail the anti-ischemic action of this antioxidant in a model of experimental focal ischemia provoked by unilateral intravascular occlusion of the middle cerebral artery. The neuroprotective action of SkQ family compounds (SkQR1, SkQ1, SkQTR1, SkQT1) was manifested through the decrease in trauma-induced neurological deficit in animals and prevention of amyloid-β-induced impairment of long-term potentiation in rat hippocampal slices. At present, most neurophysiologists suppose that long-term potentiation underlies cellular mechanisms of memory and learning. They consider inhibition of this process by amyloid-β1-42as anin vitromodel of memory disturbance in Alzheimer’s disease. Further development of the above studies revealed that mitochondria-targeted antioxidants could retard accumulation of hyperphosphorylated τ-protein, as well as amyloid-β1-42, and its precursor APP in the brain, which are involved in developing neurodegenerative processes in Alzheimer’s disease.

scholarly journals TDP-43 interacts with amyloid-β, inhibits fibrillization, and worsens pathology in a model of Alzheimer’s disease

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Yao-Hsiang Shih ◽  
Ling-Hsien Tu ◽  
Ting-Yu Chang ◽  
Kiruthika Ganesan ◽  
Wei-Wei Chang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Long Term Potentiation ◽  
Model Of Alzheimer’S Disease ◽  
Term Potentiation ◽  
Spatial Memory Deficit ◽  
Aβ Aggregation ◽  
Intrahippocampal Injection

AbstractTDP-43 inclusions are found in many Alzheimer’s disease (AD) patients presenting faster disease progression and greater brain atrophy. Previously, we showed full-length TDP-43 forms spherical oligomers and perturbs amyloid-β (Aβ) fibrillization. To elucidate the role of TDP-43 in AD, here, we examined the effect of TDP-43 in Aβ aggregation and the attributed toxicity in mouse models. We found TDP-43 inhibited Aβ fibrillization at initial and oligomeric stages. Aβ fibrillization was delayed specifically in the presence of N-terminal domain containing TDP-43 variants, while C-terminal TDP-43 was not essential for Aβ interaction. TDP-43 significantly enhanced Aβ’s ability to impair long-term potentiation and, upon intrahippocampal injection, caused spatial memory deficit. Following injection to AD transgenic mice, TDP-43 induced inflammation, interacted with Aβ, and exacerbated AD-like pathology. TDP-43 oligomers mostly colocalized with intracellular Aβ in the brain of AD patients. We conclude that TDP-43 inhibits Aβ fibrillization through its interaction with Aβ and exacerbates AD pathology.

Reduced hippocampal CA1 Ca2+-induced long-term potentiation is associated with age-dependent impairment of spatial learning

1995 ◽  
Vol 686 (1) ◽  
pp. 107-110 ◽  
Author(s):  
Giovanni Diana ◽  
Maria Rosaria Domenici ◽  
Arsenia Scotti de Carolis ◽  
Alberto Loizzo ◽  
Stefano Sagratella
Keyword(s):  
Spatial Learning ◽  
Long Term Potentiation ◽  
Term Potentiation ◽  
Hippocampal Ca1 ◽  
Age Dependent
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