Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory

@article{Turner2003RolesOA,
  title={Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory},
  author={Paul R. Turner and Kathleen D. O’Connor and Warren P Tate and Wickliffe C. Abraham},
  journal={Progress in Neurobiology},
  year={2003},
  volume={70},
  pages={1-32}
}
Amyloid-beta precursor protein (APP) is a membrane-spanning protein with a large extracellular domain and a much smaller intracellular domain. It is the source of the amyloid-beta (Abeta) peptide found in neuritic plaques of Alzheimer's disease (AD) patients. Because Abeta shows neurotoxic properties, and because familial forms of AD promote Abeta accumulation, a massive international research effort has been aimed at understanding the mechanisms of Abeta generation, catabolism and toxicity… Expand
Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
TLDR
The biological functions of APP are discussed in the context of tissue morphogenesis and restructuring, where APP appears to play significant roles both as a contact receptor and as a diffusible factor. Expand
Physiological role of amyloid precursor protein during neural development
TLDR
The physiological functions of the zebrafish Appb, a highly conserved homologue of human APP, during neural development are examined and it is found that Appb is required for the patterning and outgrowth of motor neurons in the spinal cord as well as for the synapse formation at the neuromuscular junctions, thus essential for the formation of normal locomotor behavior. Expand
Restoring Soluble Amyloid Precursor Protein α Functions as a Potential Treatment for Alzheimer's Disease
TLDR
It is likely that identification and characterization of sAPPα receptors in the brain, downstream effectors, and signaling pathways will pave the way for an attractive therapeutic target for AD prevention or intervention. Expand
Amyloid precursor protein (APP) regulates synaptic structure and function
TLDR
It is proposed that APP, specifically sAPP, is necessary for the maintenance of dendritic integrity in the hippocampus in an age-associated manner and these age-related changes may contribute to AD pathology independent of Aβ-mediated synaptic toxicity. Expand
The amyloid precursor protein and postnatal neurogenesis/neuroregeneration.
  • Yanan Chen, B. Tang
  • Biology, Medicine
  • Biochemical and biophysical research communications
  • 2006
TLDR
Two possible functions of the APP family in the brain-regulation of neural progenitor cell proliferation and axonal outgrowth after injury are brought to light; these two apparently related neurogenic/neuroregenerative functions of APP involve two separate domains of the molecule. Expand
Novel Insights into the Physiological Function of the APP (Gene) Family and Its Proteolytic Fragments in Synaptic Plasticity
TLDR
Recent findings are summarized with emphasis on the physiological role of the APP gene family and its proteolytic products on synaptic function and plasticity, especially during processes of hippocampal LTP. Expand
Amyloid precursor protein: cellular studies and animal models
TLDR
It is found that antibody-bound APP upregulates expression of ornithine decarboxylase (ODC), which is the initial and rate-controlling enzyme in polyamine biosynthesis, and demonstrated that ODC translocates in AD, from the nuclear compartment towards the cytoplasmic. Expand
The human β-amyloid precursor protein: biomolecular and epigenetic aspects
  • K. Nguyen
  • Biology, Medicine
  • Biomolecular concepts
  • 2015
TLDR
An overview of the current understanding of Beta-amyloid precursor protein, including its structure, expression patterns, proteolytic processing and putative functions is provided, and recent data concerning its epigenetic regulation, especially in alternative APP pre-mRNA splicing and in the control of genomic rearrangements of the APP gene are reported. Expand
The physiological processing of Alzheimer-associated amyloid beta precursor protein in human and animal-derived neuronal models
Alzheimer’s disease (AD) is characterized by cognitive impairment due to the loss of structure and/or function of neurons, and amyloid plaques composed of aggregated-amyloid beta (Aβ) peptides,Expand
Investigation of secreted amyloid precursor protein-α binding partners
Alzheimer’s disease is characterised by progressive loss of memory and cognitive functions. The symptoms extend to severe dementia and, in extreme cases, death. The neurological damage arises fromExpand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 293 REFERENCES
APP-BP1, a Novel Protein That Binds to the Carboxyl-terminal Region of the Amyloid Precursor Protein (*)
TLDR
The cloning of a cDNA encoding a ubiquitously expressed 59-kDa APP-binding protein, called APP-BP1, is 61% similar to a protein encoded by the Arabidopsis AXR1 gene, required for normal response to the hormone auxin, and is a relative of the ubiquitin activating enzyme E1. Expand
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives.
  • M. Mattson
  • Medicine, Biology
  • Physiological reviews
  • 1997
TLDR
Alternative enzymatic processing of beta-APP liberates A beta, which has a propensity to form amyloid fibrils; A beta can damage and kill neurons and increase their vulnerability to excitotoxicity. Expand
Beta-amyloid-related peptides inhibit potassium-evoked acetylcholine release from rat hippocampal slices
TLDR
Results demonstrate that APP-derived A beta-related peptides can regulate the release of endogenous acetylcholine potently by acting on cholinergic terminals, and suggests a potential mechanistic link between the deposition of A beta and the preferential vulnerability of certain Cholinergic projections in AD. Expand
Signaling by β-Amyloid Precursor Protein
The β-amyloid precursor protein (βAPP) is widely expressed in neurons and glial cells throughout the mammalian nervous system. APP is a large transmembrane glycoprotein having a single transmembraneExpand
Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein
TLDR
It is reported that APPss have a potent neuroprotective action in cultured rat hippocampal and septal neurons and in human cortical neurons, and the neuroprotection was abolished by antibodies to a specific region common to both APPs695 and APPs751. Expand
The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain.
TLDR
It is concluded that the pathogenically critical process of Abeta oligomers, principally dimers, in primary human neurons and in neuronal and nonneural cell lines begins intraneuronally. Expand
The amyloid precursor protein is developmentally regulated and correlated with synaptogenesis.
TLDR
It is shown, in the primary visual pathway of the hamster, that APPs are developmentally regulated proteins rapidly transported to the growing tips of nerve fibers, suggesting that target recognition and synaptic contact may result in a signal for APP cleavage in the CNS in vivo. Expand
Increase of synaptic density and memory retention by a peptide representing the trophic domain of the amyloid beta/A4 protein precursor.
  • J. Roch, E. Masliah, +4 authors T. Saitoh
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1994
TLDR
It is reported here that a 17-mer peptide, containing this active domain of sAPP, can induce cellular and behavioral changes when infused into rat brains and this results suggest that APP is involved in memory retention through its effect on synaptic structure. Expand
Nicotine and its interaction with β-amyloid protein: a short review
Abstract Two features of Alzheimer’s disease (AD) are β-amyloid protein (βAP) deposition and a severe cholinergic deficit. β-Amyloid protein is a 39– to 43–amino acid transmembrane fragment of aExpand
Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates.
Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid deposits associated with damaged neuropil and blood vessels contain abundant fibrils formed by the amyloidExpand
...
1
2
3
4
5
...