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Страница 1 од 373 резултати
Navβ2 knockdown improves cognition in APP/PS1 mice by partially inhibiting seizures and APP amyloid processing.
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Voltage-gated sodium channels beta 2 (Navβ2, encoded by SCN2B) is a substrate of β-site amyloid precursor protein cleaving enzyme 1 (BACE1) and regulates cell surface expression of channels in neurons. Previous studies reported enhanced Navβ2 processing by BACE1 in Alzheimer's disease (AD) model and
Amyloid precursor protein mRNA encoding the Kunitz protease inhibitor domain is increased by kainic acid-induced seizures in rat hippocampus.
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A 168-nucleotide exon, found in alternatively spliced amyloid precursor protein (APP) mRNAs, encodes a Kunitz protease inhibitor (KPI) domain. Kainic acid (ip) caused a selective increase of KPI mRNA in rat hippocampus. By in situ hybridization, KPI mRNA was induced in the neuronal layers of the
[The use of SWI-MRI to differentiate between seizures and transient ischemic attacks in a patient with cerebral amyloid angiopathy].
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BACKGROUND
Cerebral amyloid angiopathy (CAA) is characterized by the deposit of β-amyloid on the walls of small and medium-sized arteries of the cerebral cortex and leptomeninges causing cerebral bleeding. Clinical presentations may include transient neurological events for which differential
Amyloid β-Related Central Nervous System Angiitis Presenting With an Isolated Seizure.
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Amyloid beta-related angiitis (ABRA) of the central nervous system (CNS) is a very rare inflammatory disorder that causes destruction of CNS arteries and subsequent neuronal injury. Most patients with ABRA are old and present with cognitive dysfunction and stroke; however, some patients may present
DBA/2J genetic background exacerbates spontaneous lethal seizures but lessens amyloid deposition in a mouse model of Alzheimer's disease.
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Alzheimer's disease (AD) is a leading cause of dementia in the elderly and is characterized by amyloid plaques, neurofibrillary tangles (NFTs) and neuronal dysfunction. Early onset AD (EOAD) is commonly caused by mutations in amyloid precursor protein (APP) or genes involved in the processing of APP
The distribution of beta-amyloid precursor protein in rat cortex after systemic kainate-induced seizures.
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In the current study we employed immunohistochemical techniques to identify neuronal and glial cells in specific brain areas that modulate beta-amyloid precursor protein (betaAPP) synthesis following kainate-induced seizures. In addition, antibodies directed against the FOS protein, which is
Cortical petechial hemorrhage, leukoencephalopathy, and subacute dementia associated with seizures due to cerebral amyloid angiopathy.
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Although cerebral amyloid angiopathy is a well-known cause of cerebral lobar hemorrhage, subacute dementia, seizures, and acute encephalopathy without lobar hemorrhage are infrequently recognized as manifestations of this disease. In this report, we describe a case of cerebral amyloid angiopathy in
Seizure-Induced Regulations of Amyloid-β, STEP61, and STEP61 Substrates Involved in Hippocampal Synaptic Plasticity.
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Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive cognitive decline. Pathologic accumulation of soluble amyloid-β (Aβ) oligomers impairs synaptic plasticity and causes epileptic seizures, both of which contribute to cognitive dysfunction in AD. However, whether
Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1 Inhibition Impairs Synaptic Plasticity via Seizure Protein 6.
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BACKGROUND
Beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) is a promising drug target for the treatment of Alzheimer's disease. Prolonged BACE1 inhibition interferes with structural and functional synaptic plasticity in mice, most likely by altering the metabolism of BACE1 substrates.
Cerebrospinal fluid biomarkers of β-amyloid metabolism and neuronal damage in epileptic seizures.
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OBJECTIVE
The main objectives of this study were to investigate if epileptic seizures have effects on brain metabolism of β-amyloid (Aβ), as reflected by cerebrospinal fluid (CSF) levels of different isoforms of Aβ peptides and soluble amyloid precursor protein (APP), and neuronal degeneration, as
Single amyloid-beta injection exacerbates 4-aminopyridine-induced seizures and changes synaptic coupling in the hippocampus.
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Accumulation of amyloid-beta (Aβ) in temporal lobe structures, including the hippocampus, is related to a variety of Alzheimer's disease symptoms and seems to be involved in the induction of neural network hyperexcitability and even seizures. Still, a direct evaluation of the pro-epileptogenic
Seizure susceptibility and mortality in mice that over-express amyloid precursor protein.
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Alzheimer's disease and Fragile X syndrome both display synaptic phenotypes, and based on recent studies, likely share dendritic over expression of amyloid precursor protein (APP) and beta-amyloid (Abeta). In order to create a mouse model to specifically study the effects of APP and Abeta at
Amyloid-β precursor protein mutant zebrafish exhibit seizure susceptibility that depends on prion protein.
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It has been proposed that Amyloid β Precursor Protein (APP) might act as a rheostat controlling neuronal excitability, but mechanisms have remained untested. APP and its catabolite Aβ are known to impact upon synapse function and dysfunction via their interaction with the prion protein
Inflammasome-derived cytokine IL18 suppresses amyloid-induced seizures in Alzheimer-prone mice.
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Alzheimer's disease (AD) is characterized by the progressive destruction and dysfunction of central neurons. AD patients commonly have unprovoked seizures compared with age-matched controls. Amyloid peptide-related inflammation is thought to be an important aspect of AD pathogenesis. We previously
Seizure susceptibility in the APP/PS1 mouse model of Alzheimer's disease and relationship with amyloid β plaques.
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Alzheimer's disease is a common age associated neurodegenerative disorder associated with an elevated risk of seizures that may be fundamentally connected to cognitive dysfunction. We used 4-9month-old mice of the APP/PS1 mouse model of Alzheimer's disease to study the presence of epileptiform-like
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