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Human APP Protein expressed in HEK-293 Cells - ABIN2714676
Planque, Nishiyama, Sonoda, Lin, Taguchi, Hara, Kolodziej, Mitsuda, Gonzalez, Sait, Fukuchi, Massey, Friedland, ONuallain, Sigurdsson, Paul: Specific amyloid β clearance by a catalytic antibody construct. in The Journal of biological chemistry 2015
This review highlights the existing link between oxidative stress and Alzheimer's disease, and the consequences towards the ABETA peptide and surrounding molecules in terms of oxidative damage. [review]
overall results and observations regarding human serum albumin (show ALB Proteins), amyloid-beta, and metal ions advance our knowledge of how protein-protein interactions associated with amyloid-beta and metal ions could be linked to Alzheimer's disease pathogenesis
electrostatic interactions in the center of the Abeta peptide sequence play a crucial role in the three-dimensional fold of the fibrils, and by inference, fibril-induced neuronal toxicity and AD pathogenesis
This study applies methodologies on the initial stages of aggregation of a hexamer of Alzheimer's amyloid beta fragment 25-35 (ABETA 25-35) and finds that transitions within the hexameric aggregate are dominated by entropic barriers and speculates that especially the conformation entropy plays a major role in the formation of the fibril as a rate limiting factor.
c-Abl is activated in AbetaOs exposed neurons and in Alzheimer's disease patient's brain, and the inhibition of activated c-Abl ameliorates cognitive deficits
RelA (show NFkBP65 Proteins), RelB (show RELB Proteins) and c-Rel (show NFkBP65 Proteins) can be activated by Abeta1-40, all of which mediate pro-inflammatory cytokine transcription and retinal pigment epithelium damage.
specific balance between the concentrations of monomeric and fibrillar alpha-synuclein determines the outcome of the Abeta42 aggregation reaction
Nuclear HSP70 (show HSP70 Proteins) leads to enhancement of vaccinia H1-related phosphatase (VHR (show DUSP3 Proteins)) activity via protein-protein interaction rather than its molecular chaperone (show HSP90AA1 Proteins) activity, thereby suppressing excessive ERK (show EPHB2 Proteins) activation. Downregulation of either VRK3 or HSP70 (show HSP70 Proteins) rendered cells vulnerable to glutamate (show GRIN1 Proteins)-induced apoptosis.
The authors show that lipoproteins including brain (apoE (show APOE Proteins)) and circulating (high-density lipoprotein, HDL (show HSD11B1 Proteins)) synergize to facilitate beta-amyloid transport across bioengineered human cerebral vessels.
The Network analyses identified APP expression in temporal cortex in patient with late-onset Alzheimer's disease.
Results show that Drosophila APPL-RNAi largely mimics transgenic amyloid beta in various phenotypes which include eye degeneration, reduced longevity and motor neuron deficit functions. This is the first report showing comparable phenotypes between APPL and amyloid beta in Alzheimer's disease model of Drosophila.
Appl siRNA inhibition in cortex glia resulted in longer sleep and reduced expression of genes involved in glutamate (show GRIN2A Proteins) recycling.
memory is altered by two connected mechanisms-APPL loss-of-function and amyloid peptide toxicity-revealing in Drosophila a functional interaction between APPL and amyloid peptide.
Our data demonstrate that, in addition to secreted APPL, the noncleaved form is involved in memory, raising the possibility that secreted and full-length APPL act together in memory processes.
findings suggest that a normal function of presenilin (PS)is to repress kinesin-1 and dynein motor activity during axonal transport of amyloid precursor protein (APP) vesicles; perturbations of APP/PS transport could contribute to early neuropathology observed in Alzheimer's Disease
APPL is the first example of a modulator of the Wnt (show WNT4 Proteins)-PCP (show PRCP Proteins) pathway specifically required for axon outgrowth.
Data show that Appl is directly regulated by the Ras/MAPK (show MAPK1 Proteins) pathway through a mechanism mediated by PntP2 (show ETS2 Proteins).
[review] APP-like proteins are involved in neuronal differentiation, neuritic outgrowth, and synapse formation.
Disruption of amyloid protein (show IAPP Proteins) precursor (APP) proteins and specifically their soluble alpha-cleaved ectodomains can protect against progressive neurodegeneration in vivo.
Down-regulation of the ATP-binding cassette transporter 2 (Abca2 (show ABCA2 Proteins)) reduces amyloid-beta production by altering Nicastrin (show NCSTN Proteins) maturation and intracellular localization.
This study describes Abeta deposition in 102 clinically characterized cattle brains from animals aged 0 to 20 years, demonstrates certain similarities between Abeta deposition patterns exhibited in cattle brains and those in the human brain in early stages of aging
release and aggregation of amyloid beta-peptide from brain lipid bilayers is regulated by cholesterol and GM1
Amyloid-beta inhibits No-cGMP signaling in a CD36 (show CD36 Proteins)- and CD47 (show CD47 Proteins)-dependent manner
These experiments demonstrate the roles of Chol and ApoE (show APOE Proteins) in the modulation of membrane insertion of APP.
Two novel transcript variants of porcine APP have been identified, producing isoforms of 695 and 751 amino acids, respectively.
APP could be acting through a semaphorin receptor as well
ADAP KO mice developed glomerular pathology. ADAP KO podocytes lack cell protrusions with actin cytoskeleton forming circumferential stress fibers.
Therefore, APP modulates Nav1.6 (show SCN8A Proteins) sodium channels through a Go-coupled JNK (show MAPK8 Proteins) pathway, which is dependent on phosphorylation of APP at Thr668.
These findings suggest that in the absence of CLU (show CLU Proteins), Abeta clearance shifts to perivascular drainage pathways, resulting in fewer parenchymal plaques but more CAA because of loss of CLU (show CLU Proteins) chaperone activity, complicating the potential therapeutic targeting of CLU (show CLU Proteins) for AD.
Chronic Dyrk1 (show DYRK1A Proteins) inhibition reversed cognitive deficits in Alzheimer's disease transgenic mice via reduction of APP and phosphorylated tau pathology.
The results of the present study substantiate that cGMP has a role in the endocytic pathway of APP and suggest a scenario where the cyclic nucleotide enhances the production of Abeta by favoring the trafficking of APP from the cell cortex to the endolysosomal compartment.
Study showed that the APP Osaka mutation has dual effects: it causes a loss-of-function of APP and gain-of-toxic-function of Abeta, though the latter seems to come out only after the former causes GABAergic depletion. Also present OSK-KI mice as a mouse model to replicate the hereditary form of recessive familial Alzheimer's disease.
Results show that the duration of UP state, which is a key feature of cortical synaptic integration occurring predominantly during slow-wave sleep, is significantly increased in the prefrontal cortex in the absence of APP. This was accompanied by a specific reduction in the glutamine synthetase (show GLUL Proteins) and tissue GABA content and sequential upregulation in the levels of GABA-B receptor expression.
results support the hypothesis that the miR (show MLXIP Proteins)-132/212 network, including Sirt1 (show SIRT1 Proteins) and likely other target genes, contributes to abnormal Abeta metabolism and senile plaque deposition in AD.
Activation of CaMKIV (show CAMK4 Proteins) by soluble amyloid-beta1-42 impedes trafficking of axonal vesicles and impairs activity-dependent synaptogenesis
Abpp /KPI(R13I) mutant mice were similarly deficient as Abpp knock out mice in regulating cerebral thrombosis in experimental models of carotid artery thrombosis and intracerebral hemorrhage.
Amyloid beta precursor protein and prion protein (show PRNP Proteins) have a conserved interaction affecting cell adhesion and central nervous system development.
A reduction in app levels causes defective axonal outgrowth of facial branchiomotor and spinal motor neurons, which involves disorganized axonal cytoskeletal elements.
these results indicate the Appa-RFP (show MKRN1 Proteins) and Aplp2 (show APLP2 Proteins) fusion proteins are likely secreted from the central nervous system and accumulate in the embryonic veins independent of blood flow.
Data show that knock down of APP in zebrafish results in fish with reduced body length and a short, curly tail, and that wild-type human APP rescues the morphant phenotype, but the Swedish mutant APP, which causes familial AD (fAD (show PSEN1 Proteins)), does not.
Report of biosynthesis of APP in physiological context and illuminate occurrence of two pools of APP, one of which is linked to neuroendocrine cell activation.
A "CAGA (show S100A8 Proteins)" sequence proximal to the "ATG" start codon & immediately upstream of an interleukin-1-responsive element was found in a location unique to APP genes of amyloid plaque-forming species & absent in all other genes surveyed.
endogenous cleavages at prohormone convertase-like sites in APP
amyloid and oxidative stress-related disease proteins like Alzheimer A beta (show SUCLA2 Proteins) peptide are increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.
study suggests that hypercholesterolemia-induced Abeta accumulation may be mediated by 27-hydroxycholesterol, involving IGF-1 (show IGF1 Proteins) signaling
This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.
alzheimer disease amyloid protein
, amyloid beta A4 protein
, beta-amyloid peptide
, cerebral vascular amyloid peptide
, peptidase nexin-II
, protease nexin-II
, amyloid protein
, alzheimer disease amyloid A4 protein homolog
, amyloid beta (A4) precursor protein (peptidase nexin-II, Alzheimer disease)
, Amyloid beta A4 protein precursor (APP) (ABPP) (Alzheimers disease amyloid protein) (Cerebral vascular amyloid peptide) (CVAP) (Protease nexin-II) (PN-II) (APPI) (PreA4)
, amyloid beta (A4) precursor protein (peptidase nexin-2, Alzheimer disease)
, amyloid beta (A4) precursor protein (protease nexin-II, Alzheimer disease)
, beta-amyloid precursor protein
, amyloid precursor protein
, amyloid precursor protein-like
, amyloid A4
, amyloidogenic glycoprotein
, protease nexin II
, amyloid beta precursor protein a
, beta-amyloid precursor protein A