"How and when environmental agents and dietary factors affect the course of Alzheimer's disease: the ""LEARn"" model (latent early-life associated regulation) may explain the triggering of AD."
<b>Background:</b> The beta-amyloid peptide (Aβ) involved in Alzheimer's disease (AD) has been described to associate/aggregate on the cell surface disrupting the membrane through pore formation and breakage.
<b>Conclusion:</b> ICA shows the neuroprotective effects via modulating the CD4<sup>+</sup> T lymphocyte-related immuno-inflammatory responses in APP/PS1 mice and may be a promising drug against AD progression.
<b>Materials and methods:</b> Sixty APP/PS1 transgenic mice were randomly divided into an AD model group, a T10-treated group and a T4-treated group (<i>n</i> = 20); 20 wild-type littermates served as the control group.
<b>Methods</b>: The AD animal model (APP/PS1 transgenic mice) and KIBRA knockout (KIBRA KO) mice were used to investigate pathophysiological changes of KIBRA <i>in vivo</i>.
<b>Methods:</b> Thirty seven-month-old APP/PS1 mice were randomly divided into AD Model group (AD group), medicine group (M group) and EA group, C57BL/6 mice were used for Normal control group (N group), <i>n</i> = 10 in each group.
<b>Results</b>: The oral treatment of AD brain extract or normal brain extract neither aggravated nor mitigated the Aβ load, glial activation or the abnormal behaviors in recipient Amyloid precursor protein/presenilin 1 (APP/PS1) mice.
(-)-Epigallocatechin gallate (EGCG) effectively reduces the cytotoxicity of the Alzheimer's diseaseβ-amyloid peptide (Aβ) by remodeling seeding-competent Aβ oligomers into off-pathway seeding-incompetent Aβ assemblies.
(i) The expression of Drebrin is decreased in the hippocampus of aged AD mice compared with that of age-matched WT and young adult AD mice; (ii) cognitive ability of APP/PS1 mice decreases with age; (iii) Drebrin protein expression in the hippocampus correlates with behavioral performance in different aged AD mice; (iv) cognitive ability improved significantly in APP/PS1-Dbn1 mice; (v) the expression level of Drebrin in APP/PS1-Dbn1 mouse hippocampus was significantly increased; (vi) the pathological lesion of AD was alleviated in APP/PS1-Dbn1 mice; (vii) the filamentous actin (F-actin) and microtubule-associated protein 2(MAP-2) in APP/PS1-Dbn1 mice were notably more than control mice.
5-Lipoxygenase (5LO) is upregulated in Alzheimer's disease (AD) and in vivo modulates the amyloidotic phenotype of amyloid precursor protein transgenic mice.
6-month-old male APP/PS1 double transgenic mice ran four months and then the effects of exercise on the cognitive function and the white matter of AD were investigated.
6-month-old of the male mice were divided into 3 groups (n = 8), the wild type C57BL/6 mice in the control group, the APP/PS1 transgenic mice of AD reared in either the standard environment or the EE.
Alzheimer's disease is characterized by accumulation in the brain of a family of insoluble amyloid peptides (Abeta peptides), which are produced as a result of the normal processing of beta-amyloid precursor protein (beta-APP).Russo et al. claim that a truncated Abeta peptide that lacks the first ten amino acids accumulates in the brains of patients carrying a mutant form of pre-senilin 1 (PS1), a protein that is involved in cleavage of beta-APP.
Alzheimer's disease (AD) is a neurodegenerative disorder of the central nervous system, and beta-amyloid precursor protein (betaAPP) plays a pivotal role in AD pathology.
Alzheimer's disease (AD) occurs when neurons in the memory and cognition regions of the brain are accompanied by an accumulation of the long amyloid beta-proteins of the 39 to 43 amino acids derived from the amyloid precursor protein (APP) by cleavage with beta- and gamma-secretase.
Alzheimer's disease (AD)-associated gamma-secretase is a presenilin (PS)- dependent proteolytic activity involved in the intramembraneous cleavage of the beta-amyloid precursor protein, Notch, LDL receptor-related protein, E-cadherin, and ErbB-4.
Alzheimer's disease (AD) is caused by the cerebral deposition of beta-amyloid (Abeta), a 38-43-amino acid peptide derived by proteolytic cleavage of the amyloid precursor protein (APP).
Alzheimer's disease (AD) is characterized by the deposition of beta-amyloid (A beta) plaques derived from the amyloidogenic processing; of a transmembrane protein called beta-amyloid precursor protein (APP).
Alzheimer's disease (AD) is characterized by pathological lesions, such as senile plaques (SPs) and cerebral amyloid angiopathy (CAA), both predominantly consisting of a proteolytic cleavage product of the amyloid-beta precursor protein (APP), the amyloid-beta peptide (Abeta).
Alzheimer's disease (AD) is characterized by pathological lesions, such as senile plaques (SPs) and cerebral amyloid angiopathy (CAA), both predominantly consisting of a proteolytic cleavage product of the amyloid-beta precursor protein (APP), the amyloid-beta peptide (Abeta).
Alzheimer's disease (AD) is characterized by massive neuron loss in distinct brain regions, extracellular accumulations of the amyloid precursor protein-fragment amyloid-beta (A beta) and intracellular tau fibrils containing hyperphosphorylated tau.