HCSGD entry for APP
1. General information
| Official gene symbol | APP |
|---|---|
| Entrez ID | 351 |
| Gene full name | amyloid beta (A4) precursor protein |
| Other gene symbols | AAA ABETA ABPP AD1 APPI CTFgamma CVAP PN-II PN2 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000085 | Mitotic G2 phase | ISS | biological_process |
| GO:0001967 | Suckling behavior | IEA | biological_process |
| GO:0002576 | Platelet degranulation | TAS | biological_process |
| GO:0003677 | DNA binding | ISS | molecular_function |
| GO:0004867 | Serine-type endopeptidase inhibitor activity | IDA IEA | molecular_function |
| GO:0005102 | Receptor binding | IPI | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005576 | Extracellular region | TAS | cellular_component |
| GO:0005737 | Cytoplasm | IDA ISS | cellular_component |
| GO:0005794 | Golgi apparatus | IDA ISS | cellular_component |
| GO:0005829 | Cytosol | TAS | cellular_component |
| GO:0005886 | Plasma membrane | IDA | cellular_component |
| GO:0005887 | Integral component of plasma membrane | TAS | cellular_component |
| GO:0005905 | Coated pit | IEA | cellular_component |
| GO:0006378 | MRNA polyadenylation | ISS | biological_process |
| GO:0006417 | Regulation of translation | ISS | biological_process |
| GO:0006468 | Protein phosphorylation | ISS | biological_process |
| GO:0006878 | Cellular copper ion homeostasis | ISS | biological_process |
| GO:0006897 | Endocytosis | ISS | biological_process |
| GO:0006979 | Response to oxidative stress | IEA | biological_process |
| GO:0007155 | Cell adhesion | IEA | biological_process |
| GO:0007176 | Regulation of epidermal growth factor-activated receptor activity | ISS | biological_process |
| GO:0007219 | Notch signaling pathway | IEA | biological_process |
| GO:0007409 | Axonogenesis | ISS | biological_process |
| GO:0007596 | Blood coagulation | TAS | biological_process |
| GO:0007617 | Mating behavior | ISS | biological_process |
| GO:0007626 | Locomotory behavior | ISS | biological_process |
| GO:0008088 | Axon cargo transport | ISS | biological_process |
| GO:0008201 | Heparin binding | IEA | molecular_function |
| GO:0008203 | Cholesterol metabolic process | IEA | biological_process |
| GO:0008344 | Adult locomotory behavior | ISS | biological_process |
| GO:0008542 | Visual learning | ISS | biological_process |
| GO:0009986 | Cell surface | IDA | cellular_component |
| GO:0010951 | Negative regulation of endopeptidase activity | IDA | biological_process |
| GO:0010971 | Positive regulation of G2/M transition of mitotic cell cycle | IEA | biological_process |
| GO:0016021 | Integral component of membrane | IEA ISS | cellular_component |
| GO:0016199 | Axon midline choice point recognition | ISS | biological_process |
| GO:0016322 | Neuron remodeling | ISS | biological_process |
| GO:0016358 | Dendrite development | ISS | biological_process |
| GO:0016504 | Peptidase activator activity | IEA | molecular_function |
| GO:0030168 | Platelet activation | TAS | biological_process |
| GO:0030198 | Extracellular matrix organization | ISS TAS | biological_process |
| GO:0030424 | Axon | ISS | cellular_component |
| GO:0030900 | Forebrain development | IEA | biological_process |
| GO:0031093 | Platelet alpha granule lumen | TAS | cellular_component |
| GO:0031175 | Neuron projection development | ISS | biological_process |
| GO:0031594 | Neuromuscular junction | IEA | cellular_component |
| GO:0033130 | Acetylcholine receptor binding | IPI | molecular_function |
| GO:0035235 | Ionotropic glutamate receptor signaling pathway | ISS | biological_process |
| GO:0035253 | Ciliary rootlet | IEA | cellular_component |
| GO:0035872 | Nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway | TAS | biological_process |
| GO:0040014 | Regulation of multicellular organism growth | ISS | biological_process |
| GO:0042802 | Identical protein binding | IPI | molecular_function |
| GO:0043197 | Dendritic spine | IDA | cellular_component |
| GO:0043198 | Dendritic shaft | IDA | cellular_component |
| GO:0043231 | Intracellular membrane-bounded organelle | IDA | cellular_component |
| GO:0043235 | Receptor complex | IDA | cellular_component |
| GO:0043393 | Regulation of protein binding | IEA | biological_process |
| GO:0045087 | Innate immune response | TAS | biological_process |
| GO:0045177 | Apical part of cell | IEA | cellular_component |
| GO:0045202 | Synapse | IDA | cellular_component |
| GO:0045665 | Negative regulation of neuron differentiation | IEA | biological_process |
| GO:0045931 | Positive regulation of mitotic cell cycle | ISS | biological_process |
| GO:0045944 | Positive regulation of transcription from RNA polymerase II promoter | IEA | biological_process |
| GO:0046914 | Transition metal ion binding | IEA | molecular_function |
| GO:0048471 | Perinuclear region of cytoplasm | IEA | cellular_component |
| GO:0048669 | Collateral sprouting in absence of injury | ISS | biological_process |
| GO:0050803 | Regulation of synapse structure and activity | ISS | biological_process |
| GO:0050885 | Neuromuscular process controlling balance | IEA | biological_process |
| GO:0051124 | Synaptic growth at neuromuscular junction | IEA | biological_process |
| GO:0051233 | Spindle midzone | IEA | cellular_component |
| GO:0051402 | Neuron apoptotic process | IMP | biological_process |
| GO:0051425 | PTB domain binding | IPI | molecular_function |
| GO:0051563 | Smooth endoplasmic reticulum calcium ion homeostasis | IEA | biological_process |
| GO:0052548 | Regulation of endopeptidase activity | IDA | biological_process |
| GO:0070851 | Growth factor receptor binding | IEA | molecular_function |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.0995358345 | 0.9837052468 | 0.6585929361 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Up | 0.0520092218 |
| GSE13712_SHEAR | Down | -0.1411177274 |
| GSE13712_STATIC | Up | 0.1320911817 |
| GSE19018 | Up | 0.0267272031 |
| GSE19899_A1 | Up | 0.2337903821 |
| GSE19899_A2 | Up | 0.2832275160 |
| PubMed_21979375_A1 | Up | 0.1695185986 |
| PubMed_21979375_A2 | Up | 0.1437693197 |
| GSE35957 | Up | 0.4623222686 |
| GSE36640 | Up | 0.4684581196 |
| GSE54402 | Down | -0.0262998655 |
| GSE9593 | Up | 0.3110651366 |
| GSE43922 | Up | 0.2813040136 |
| GSE24585 | Up | 0.0823663568 |
| GSE37065 | Up | 0.0157689528 |
| GSE28863_A1 | Up | 0.0948272826 |
| GSE28863_A2 | Up | 0.1516969200 |
| GSE28863_A3 | Down | -0.0836126326 |
| GSE28863_A4 | Up | 0.0147118146 |
| GSE48662 | Up | 0.4016415514 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
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- Drugs
Name | Drug | Accession number |
|---|---|---|
| L-methionine (R)-S-oxide | DB02235 | EXPT02921 |
| CAD106 | DB05150 | - |
| Mito-4509 | DB05846 | - |
| Florbetaben (18F) | DB09148 | - |
| Florbetapir (18F) | DB09149 | - |
| Flutemetamol (18F) | DB09151 | - |
- MicroRNAs
- mirTarBase
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-106b-5p | MIMAT0000680 | MIRT000373 | Luciferase reporter assay//Western blot | Functional MTI | 19110058 |
| hsa-miR-101-3p | MIMAT0000099 | MIRT000430 | qRT-PCR//Luciferase reporter assay//Western blot | Functional MTI | 20395292 |
| hsa-miR-101-3p | MIMAT0000099 | MIRT000430 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 21172309 |
| hsa-miR-520c-3p | MIMAT0002846 | MIRT001934 | Luciferase reporter assay//Western blot | Functional MTI | 18684319 |
| hsa-miR-106a-5p | MIMAT0000103 | MIRT001935 | Luciferase reporter assay | Non-Functional MTI | 19110058 |
| hsa-miR-106a-5p | MIMAT0000103 | MIRT001935 | Luciferase reporter assay//Western blot | Functional MTI | 18684319 |
| hsa-miR-20a-5p | MIMAT0000075 | MIRT003382 | Luciferase reporter assay//Western blot | Functional MTI | 19110058 |
| hsa-miR-20a-5p | MIMAT0000075 | MIRT003382 | GFP reporter assay//qRT-PCR//Western blot | Functional MTI | 20458444 |
| hsa-miR-17-5p | MIMAT0000070 | MIRT003898 | Luciferase reporter assay//Western blot | Functional MTI | 19110058 |
| hsa-miR-17-5p | MIMAT0000070 | MIRT003898 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-15a-5p | MIMAT0000068 | MIRT003899 | Luciferase reporter assay | Non-Functional MTI | 19110058 |
| hsa-miR-130a-3p | MIMAT0000425 | MIRT003900 | Luciferase reporter assay | Non-Functional MTI | 19110058 |
| hsa-let-7d-5p | MIMAT0000065 | MIRT003901 | Luciferase reporter assay | Non-Functional MTI | 19110058 |
| hsa-let-7a-5p | MIMAT0000062 | MIRT003902 | Luciferase reporter assay | Non-Functional MTI | 19110058 |
| hsa-miR-16-5p | MIMAT0000069 | MIRT031838 | Proteomics | Functional MTI (Weak) | 18668040 |
| hsa-miR-532-3p | MIMAT0004780 | MIRT037918 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-500a-5p | MIMAT0004773 | MIRT038001 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-484 | MIMAT0002174 | MIRT042260 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-423-3p | MIMAT0001340 | MIRT042631 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-328-3p | MIMAT0000752 | MIRT043760 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-222-3p | MIMAT0000279 | MIRT046755 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-196a-5p | MIMAT0000226 | MIRT048186 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-1260b | MIMAT0015041 | MIRT052777 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-3620-3p | MIMAT0018001 | MIRT052863 | CLASH | Functional MTI (Weak) | 23622248 |
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- mirRecord
- mirRecord
MicroRNA name | mirBase ID | Target site number | MiRNA mature ID | Test method inter | MiRNA regulation site | Reporter target site | Pubmed ID |
|---|---|---|---|---|---|---|---|
| hsa-miR-520c-3p | MIMAT0002846 | 1 | hsa-miR-520c-3p | {Western blot} | {overexpression} | 18684319 | |
| hsa-miR-106a-5p | MIMAT0000103 | 1 | hsa-miR-106a | {Western blot} | {overexpression} | 18684319 |
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6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 18 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 27115165 | Detecting Abeta deposition and RPE cell senescence in the retinas of SAMP8 mice |
| 27115165 | Abeta deposition and p16-positive senescent RPE cells were traced using immunofluorescence labeling |
| 27115165 | Increased Abeta deposits in OS layer and p16-positive senescent RPE cells were observed using immunofluorescence microscopy |
| 26793112 | It has been shown that there is a JNK pathway activation after exposure to different stressing factors, including cytokines, growth factors, oxidative stress, unfolded protein response signals or Abeta peptides |
| 26793112 | JNK's, particularly JNK3, not only enhance Abeta production, moreover it plays a key role in the maturation and development of neurofibrillary tangles |
| 25564872 | In view of the central role of telomere and telomerase in the aging process, herein we found that the aggregated form Abeta (Abeta1-40 and Abeta1-42), not Abeta monomer, could inhibit telomerase activity both in vitro and in living cells |
| 25564872 | Further studies indicated Abeta oligomers inhibited telomerase activity through binding to DNA |
| 25564872 | We also identified that intracellular Abeta localized at telomere, and induced cell senescence and telomere shortening |
| 25564872 | These results indicate that Abeta oligomers can be potential natural inhibitors of telomerase and that inhibition of telomerase activity may be one of the factors for Abeta-induced cytotoxicity |
| 25385658 | In our previous study, we found that amyloid-beta (Abeta) peptide, a component of drusen, induced the cells of the retinal pigment epithelium (RPE; RPE cells) to enter senescence; however, its effects in vivo remain unknown |
| 25385658 | Thus, the present study was carried out to explore the in vivo effects of Abeta peptide on RPE cell senescence and senescence-associated inflammation in C57BL/6 mice |
| 24750067 | We also observed an abnormal expression of death receptor-6 and beta-amyloid precursor protein (APP) |
| 24750067 | Expression of APP, DR6, pTau (in GG and DNT) and caspase-3 (in GG) positively correlated with duration of epilepsy |
| 23557734 | RESULTS: Abeta promotes RPE cells to enter senescence and secrete higher concentrations of IL-8 and MMP-9 |
| 23296681 | Cerebral amyloid angiopathy (CAA) caused by amyloid beta (Abeta) deposition around brain microvessels is a human neurovascular degenerative disease that is characterized by an early onset of recurrent stroke episodes, vascular brain degenerative changes, and moderate to severe clinical presentations |
| 23296681 | Recently, by using the zebrafish model, we investigated whether Abeta peptides cause endothelial cells to enter senescence at an early stage of vascular development |
| 23296681 | By measuring beta-galactosidase activity and p21 expression in whole-mount zebrafish embryos exposed to Abeta, we demonstrated that these oxidative peptides promote vascular senescence at an early stage of development, a harbinger of vascular clinical symptoms in adult |
| 23061730 | Much evidence indicate that vascular impairment is a fundamental contributor to AD pathology and platelets are generally considered a key element because they represent the link between amyloid-beta (Abeta) deposition, peripheral inflammation and endothelial senescence |
| 23061730 | Both activated and senescent platelets are a source of Abeta, in addition activated platelets secrete many proinflammatory mediators that could contribute to increased peripheral inflammation and endothelial senescence |
| 23061730 | Heparin has been proposed as a treatment for senile dementia and exhibits anti-inflammatory action as well as inhibitory effects on Abeta assembly |
| 23061729 | However, accumulating evidence now support the idea that assistance by peripheral mononuclear phagocytes (MP) in AD could be essential to control local brain inflammation and remove Abeta depots |
| 22482456 | In AD, alterations in enzymes involved in oxidative phosphorylation, oxidative damage, and mitochondrial binding of Abeta and amyloid precursor protein have been reported |
| 21258649 | In AD, alterations in enzymes involved in oxidative phosphorylation, oxidative damage, and mitochondrial binding of Abeta and amyloid precursor protein have been reported |
| 20127045 | The major pathologic feature of AD is senile plaques mainly containing amyloid-beta (Abeta) components |
| 20127045 | However, little direct evidence has shown aging in association with Abeta |
| 20127045 | Here we show that the protein-protein interaction of amyloid precursor protein (APP) and beta -site amyloid cleavage enzyme 1 (BACE1) is enhanced by the fluorescence resonance energy transfer (FRET) assay during the aging process, and the APP-BACE1 complex accumulates in the endosome in the IMR-90 fibroblast (NHF) cellular aging models |
| 20127045 | Moreover, enhanced Abeta is observed in aged cells, rat brain homogenates and human serum |
| 20127045 | Interestingly, addition of the dominant-negative mutant of Rab5, a small G-protein Rab5 involved in the endocytic process, inhibits the aging-related APP-BACE1 interaction and Abeta production, suggesting that endocytosis contributes to AD progression |
| 17601350 | An intronic SNP in the APP gene (rs2830102) was significantly associated with cognitive ageing in both LBC1921 and a combined LBC1921/ABC1936 analysis (p < 0 |
| 17601350 | CONCLUSION: This study suggests a possible role for APP in normal cognitive ageing, in addition to its role in Alzheimer's disease |
| 16303768 | Processing of amyloid precursor protein (APP) is a well acknowledged central pathogenic mechanism in Alzheimer disease |
| 16303768 | However, influences of age-associated cellular alterations on the biochemistry of APP processing have not been studied in molecular detail so far |
| 16303768 | Here, we report that processing of endogenous APP is down-regulated during the aging of normal human fibroblasts (IMR-90) |
| 16303768 | The generation of intracellular APP cleavage products C99, C83, and AICD gradually declines with increasing life span and is accompanied by a reduced secretion of soluble APP (sAPP) and sAPPalpha |
| 16303768 | Further, the maturation of APP was reduced in senescent cells, which has been shown to be directly mediated by age-associated increased cellular cholesterol levels |
| 12834113 | Secretion and accumulation of Abeta by brain vascular smooth muscle cells from AbetaPP-Swedish transgenic mice |
| 12834113 | Alzheimer amyloid-beta is deposited in the neuropil and in brain blood vessels in transgenic Tg2576 mice that overexpress human amyloid-beta precursor protein (AbetaPP) containing the Swedish mutation (AbetaPP-Swe) |
| 12834113 | Because the AbetaPP transgene in Tg2576 mice is placed behind the PrP promoter, all amyloid-beta, including vascular amyloid, is considered to be of neuronal origin |
| 12834113 | We studied the expression of the transgenic AbetaPP in smooth muscle cells cultured from brain blood vessels from Tg2576 mice |
| 12834113 | We found that brain vascular smooth muscle cells overexpressed human AbetaPP-Swe approximately 4 times the physiological levels of mouse AbetaPP |
| 12834113 | The percentage of cells containing intracellular Abeta and the amount of intracellular Abeta were significantly higher in cultures obtained from 14-month-old than from 4-month-old mice, as tested on first or second passages |
| 12834113 | During cell senescence in culture, intracellular accumulation of Abeta and C-terminal fragments of AbetaPP increased in cells derived from both 4- and 14-month-old mice |
| 12834113 | Vascular muscle cells from Tg2576 mice appear to be a valuable model of the intracellular accumulation of Abeta |
| 12731644 | On the basis of our research, several processes seem to be important in relation to the still speculative pathogenesis, including (a) increased transcription and accumulation of amyloid-beta precursor protein and accumulation of its proteolytic fragment amyloid-beta; (b) abnormal accumulation of components related to lipid metabolism, for example, cholesterol, accumulation of which is possibly owing to its abnormal trafficking; (c) oxidative stress; (d) accumulations of other Alzheimer's disease-related proteins; and (e) a milieu of muscle cellular aging in which these changes occur |
| 12351995 | Our basic hypothesis is that over-expression of amyloid-beta precursor protein within aging muscle fibers is an early upstream event causing the subsequent pathogenic cascade |
| 12351995 | On the basis of our research, several processes seem to be important in relation to the still speculative pathogenesis: (a) increased transcription and accumulation of amyloid-beta precursor protein, and accumulation of its proteolytic fragment Abeta; (b) accumulations of phosphorylated tau and other Alzheimer-related proteins; (c) accumulation of cholesterol and low-density lipoprotein receptors, the cholesterol accumulation possibly due to its abnormal trafficking; (d) oxidative stress; and (e) a milieu of muscle cellular aging in which these changes occur |
| 1722012 | The beta amyloid precursor protein (beta APP) has been shown to have adhesive interactions |
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