RAGE Does Not Affect Amyloid Pathology in Transgenic ArcAβ Mice

@article{Vodopivec2009RAGEDN,
  title={RAGE Does Not Affect Amyloid Pathology in Transgenic ArcA$\beta$ Mice},
  author={Ivana Vodopivec and Arnaud Galichet and Marlen Knobloch and Angelika Bierhaus and Claus W. Heizmann and Roger M. Nitsch},
  journal={Neurodegenerative Diseases},
  year={2009},
  volume={6},
  pages={270 - 280}
}
Background: Alzheimer’s disease (AD) is characterized by brain accumulation of the amyloid-β peptide (Aβ) that triggers a cascade of biochemical and cellular alterations resulting in the clinical phenotype of the disease. While numerous experiments addressed Aβ toxicity, the mechanisms are still not fully understood. The receptor for advanced glycation end products (RAGE) binds Aβ and was suggested to be involved in the pathological processes of AD. Objective: Our purpose was to assess the… Expand
The Complexity of Sporadic Alzheimer's Disease Pathogenesis: The Role of RAGE as Therapeutic Target to Promote Neuroprotection by Inhibiting Neurovascular Dysfunction
TLDR
Evidence is presented that pharmacological inhibition of RAGE will promote neuroprotection by blocking neurovascular dysfunction in AD and a novel pathway induced by RAGE in AD, which leads to the expression of thioredoxin interacting protein (TXNIP). Expand
TOM1 Regulates Neuronal Accumulation of Amyloid-β Oligomers by FcγRIIb2 Variant in Alzheimer's Disease
TLDR
It is described that the FcγRIIb2 variant is responsible for both neuronal uptake and intraneuronal distribution of pathogenic Aβ linked to memory deficits in AD mice, showing a pathologic significance of the internalized Aβ. Expand
Microglial Scavenger Receptors and Their Roles in the Pathogenesis of Alzheimer's Disease
TLDR
It is proposed that various scavenger receptors play complementary, nonredundant functions in the development of AD pathology and potential therapeutic applications for these receptors in AD are proposed. Expand
Microglia in Alzheimer's Disease.
TLDR
Current knowledge about the stage-dependent role of microglia activation in AD is summarized, including recent insights from genetic and gene expression profiling studies as well as novel imaging techniques focusing on microglial activation in human AD pathology and AD mouse models. Expand
Association of the RAGE G82S polymorphism with Alzheimer’s disease
TLDR
Investigation of associations between AGER, AD diagnosis, cognitive scores and cerebrospinal fluid AD biomarkers in a European cohort of 316 neurochemically verified AD cases and 579 controls found a weak, but significant effect of AGER on risk of AD. Expand
RAGE is a key cellular target for Abeta-induced perturbation in Alzheimer's disease.
TLDR
The role of RAGE in the pathogenesis of AD is summarized, specifically in Abeta-induced cellular perturbation. Expand
Microglial Aβ Receptors in Alzheimer’s Disease
  • Y. Yu, R. Ye
  • Biology, Medicine
  • Cellular and Molecular Neurobiology
  • 2014
TLDR
This review focuses on microglial membrane receptors that bind Aβ and contribute to microglia activation and/or Aβ phagocytosis and clearance and the potential therapeutic value of these receptors in AD. Expand
Binding Sites for Amyloid-β Oligomers and Synaptic Toxicity.
TLDR
In Alzheimer's disease, insoluble and fibrillary amyloid-β (Aβ) peptide accumulates in plaques and receptors for Aβ oligomers are hypothesized to be the first step in a neuronal cascade leading to dementia. Expand
The S100B/RAGE Axis in Alzheimer's Disease
TLDR
The role of S100B/RAGE activation in Alzheimer's disease is discussed and the regulation of RAGE signaling by S 100B is complex and probably involves other ligands including the amyloid beta peptide, the Advanced Glycation Endproducts, or transtheyretin. Expand
The S 100 B / RAGE Axis in Alzheimer ’ s Disease
Increasing evidence suggests that the small EF-hand calcium-binding protein S100B plays an important role in Alzheimer’s disease. Among other evidences are the increased levels of both S100B and itsExpand
...
1
2
...

References

SHOWING 1-10 OF 35 REFERENCES
RAGE potentiates Aβ‐induced perturbation of neuronal function in transgenic mice
TLDR
It is indicated that RAGE is a cofactor for Aβ‐induced neuronal perturbation in a model of Alzheimer's‐type pathology, and its potential as a therapeutic target to ameliorate cellular dysfunction is suggested. Expand
Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice
TLDR
The co-incidence of intrACEllular A deposits with behavioral deficits support an early role of intracellular A in the pathophysiological cascade leading to -amyloid formation and functional impairment. Expand
RAGE regulates BACE1 and Aβ generation via NFAT1 activation in Alzheimer's disease animal model
  • H. Cho, S. Son, +5 authors I. Mook-Jung
  • Medicine, Biology
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2009
TLDR
The receptor for advanced glycation end products (RAGE) is a multiligand cell surface receptor, and amyloid P peptide (Aβ) is one of the ligands for RAGE, which regulates BACE1 and Aβ generation via NFAT1 activation in Alzheimer's disease animal model. Expand
Abeta-induced inflammatory processes in microglia cells of APP23 transgenic mice.
TLDR
Although up-regulation of major histocompatibility complex class II (IA) points toward an intact antigen-presenting function of microglia, lack of T and B lymphocytes does not indicate a cell-mediated immune response in the brains of APP23 mice, rendering the mouse model suitable to study the role of inflammatory processes during AD pathogenesis. Expand
Plaque-Associated Overexpression of Insulin-Degrading Enzyme in the Cerebral Cortex of Aged Transgenic Tg2576 Mice With Alzheimer Pathology
TLDR
It is proposed that in Tg2576 mice and in contrast to its behavior in Alzheimer brains, active IDE increases with age around plaques as a component of astrocyte activation as a result of A&bgr;-triggered inflammation. Expand
IL-4-Induced Selective Clearance of Oligomeric β-Amyloid Peptide1–42 by Rat Primary Type 2 Microglia1
TLDR
IL-4-stimulated uptake and degradation of o-Aβ1–42 were selectively enhanced in type 2, but not type 1 MG that express CD40, which suggests that the two MG types may play different neuroimmunomodulating roles in the Aβ-overproducing brain. Expand
A specific amyloid-β protein assembly in the brain impairs memory
TLDR
It is found that memory deficits in middle-aged Tg2576 mice are caused by the extracellular accumulation of a 56-kDa soluble amyloid-β assembly, which is proposed to be Aβ*56 (Aβ star 56), which may contribute to cognitive deficits associated with Alzheimer's disease. Expand
Increased expression of Aβ degrading enzyme IDE in the cortex of transgenic mice with Alzheimer's disease-like neuropathology
TLDR
Examination of expression levels of amyloid beta (Abeta)-degrading enzymes, insulin degrading enzyme (IDE) and neprilysin (NEP), were examined in transgenic mice with Alzheimer's disease-like neuropathology found significant up-regulation of IDE and possibly of NEP expression in response to the Abeta accumulation. Expand
Altered expression of Aβ metabolism-associated molecules from d-galactose/AlCl3 induced mouse brain
TLDR
It is shown that mice treated with Al plus D-gal represent a good model of AD with altered expression of Abeta metabolism-associated molecules that are responsible for Abeta deposition during AD, suggesting that this mouse model can be a useful model for studying the mechanisms and biomarkers of AD and for drug screening. Expand
Involvement of Microglial Receptor for Advanced Glycation Endproducts (RAGE) in Alzheimer's Disease: Identification of a Cellular Activation Mechanism
TLDR
A positive feedback loop in which Abeta-RAGE-mediated microglial activation enhances expression of M-CSF and RAGE, possibly initiating an ascending spiral of cellular activation is suggested. Expand
...
1
2
3
4
...