CIDeRplusGeneral Information:
| Id: | 2,533 |
| Diseases: |
Alzheimer disease
- [OMIM]
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| Mammalia | |
| review | |
| Reference: | Di Paolo G and Kim TW(2011) Linking lipids to Alzheimers disease: cholesterol and beyond. Nat. Rev. Neurosci. 12: 284-296 [PMID: 21448224] |
Interaction Information:
| Comment | Dysregulation of lipid pathways has been implicated in a growing number of neurodegenerative disorders, such as Alzheimer disease (AD). |
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Formal Description Interaction-ID: 23580 |
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| Comment | Patients with AD display loss of synapses and neurons, as well as extracellular senile plaques and intracellular neurofibrillary tangles (NFTs). |
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Formal Description Interaction-ID: 23590 |
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| Comment | Patients with AD display loss of synapses and neurons, as well as extracellular senile plaques and intracellular neurofibrillary tangles (NFTs). |
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Formal Description Interaction-ID: 23591 |
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| Comment | Brains with AD display a higher occurrence of adipose inclusions or lipoid granules, suggesting aberrant lipid metabolism. |
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Formal Description Interaction-ID: 23592 |
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| Comment | APOE encodes a protein that serves as acrucial regulator of cholesterol metabolism in the brain and of triglyceride metabolism throughout the body. |
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Formal Description Interaction-ID: 23593 |
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| Drugbank entries | Show/Hide entries for APOE |
| Comment | The epsilon 4 allele of the apolipoprotein E (APOE) gene was identified as the strongest genetic risk factor for AD. |
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Formal Description Interaction-ID: 23594 |
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| Comment | APOE encodes a protein that serves as acrucial regulator of cholesterol metabolism in the brain and of triglyceride metabolism throughout the body. |
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Formal Description Interaction-ID: 23600 |
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| Drugbank entries | Show/Hide entries for APOE |
| Comment | APOE mediates the uptake of lipoprotein particles in the brain via the low-density lipoprotein (LDL) receptor related protein (LRP) and the very low-density family lipoprotein receptor. |
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Formal Description Interaction-ID: 23601 |
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| Drugbank entries | Show/Hide entries for APOE |
| Comment | APOE in amyloid pathology is supported by evidence that it binds amyloid-beta and modulates the aggregation and clearance of amyloid-beta. |
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Formal Description Interaction-ID: 23602 |
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| Drugbank entries | Show/Hide entries for APOE |
| Comment | Pharmacological inhibition of ACAT1 (for example, using CP-113,818) leads to the reduction of both amyloid-beta and cholesteryl ester. |
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Formal Description Interaction-ID: 23603 |
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| Drugbank entries | Show/Hide entries for SOAT1 |
| Comment | Pharmacological inhibition of ACAT1 (for example, using CP-113,818) leads to the reduction of both amyloid-beta and cholesteryl ester. |
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Formal Description Interaction-ID: 23711 |
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| Drugbank entries | Show/Hide entries for SOAT1 |
| Comment | Genetic ablation of ACAT1 reduces both amyloid-beta pathology and cognitive impairments in a mouse model of AD. |
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Formal Description Interaction-ID: 23712 |
gene/protein increases_activity of phenotype Abeta pathology |
| Drugbank entries | Show/Hide entries for SOAT1 |
| Comment | Genetic ablation of ACAT1 reduces both amyloid-beta pathology and cognitive impairments in a mouse model of AD. |
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Formal Description Interaction-ID: 23713 |
gene/protein increases_activity of phenotype cognitive impairment |
| Drugbank entries | Show/Hide entries for SOAT1 |
| Comment | ACAT1 ablation also increases levels of oxysterol, 24(S)-hydroxycholesterol, suggesting a potential role of this cholesterol metabolite in decreasing amyloidogenesis. |
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Formal Description Interaction-ID: 23714 |
gene/protein decreases_quantity of drug/chemical compound |
| Drugbank entries | Show/Hide entries for SOAT1 |
| Comment | Cholesterol efflux also controls amyloid-beta generation. |
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Formal Description Interaction-ID: 23804 |
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| Comment | ATP-binding cassette transporter A1 (ABCA1) serves as an important regulator of the levels and lipidation status of APOE by stimulating efflux of excess intracellular cholesterol to extracellular lipid acceptors, including unlipidated APOE and deletion of ABCA1 gene in mouse models of AD dramatically decreases the levels of APOE both in the brain and in the periphery, which correlates with greater amyloid-beta deposits. |
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Formal Description Interaction-ID: 23805 |
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| Drugbank entries | Show/Hide entries for ABCA1 or APOE |
| Comment | ATP-binding cassette transporter A1 (ABCA1) serves as an important regulator of the levels and lipidation status of APOE by stimulating efflux of excess intracellular cholesterol to extracellular lipid acceptors, including unlipidated APOE. |
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Formal Description Interaction-ID: 23806 |
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| Drugbank entries | Show/Hide entries for ABCA1 or APOE |
| Comment | ATP-binding cassette transporter A1 (ABCA1) serves as an important regulator of the levels and lipidation status of APOE by stimulating efflux of excess intracellular cholesterol to extracellular lipid acceptors, including unlipidated APOE. |
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Formal Description Interaction-ID: 23807 |
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| Drugbank entries | Show/Hide entries for ABCA1 or APOE |
| Comment | Increased levels of ABCA1 were found to lower amyloid-beta levels in cultured cells. |
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Formal Description Interaction-ID: 23808 |
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| Drugbank entries | Show/Hide entries for ABCA1 |
| Comment | Reducing membrane cholesterol levels through cholesterol-extracting compounds, such as beta-methyl cyclodextrin (betaMCD), decreases activity of both BACE1 and gamma-secretase, leading to an additive reduction in amyloid-beta generation. |
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Formal Description Interaction-ID: 23822 |
drug/chemical compound Methyl-beta-cyclodextrin decreases_quantity of drug/chemical compound |
| Drugbank entries | Show/Hide entries for |
| Comment | Reducing membrane cholesterol levels through cholesterol-extracting compounds, such as beta-methyl cyclodextrin (betaMCD), decreases activity of both BACE1 and gamma-secretase, leading to an additive reduction in amyloid-beta generation. |
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Formal Description Interaction-ID: 23825 |
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| Drugbank entries | Show/Hide entries for Cholesterol or BACE1 |
| Comment | Reducing membrane cholesterol levels through cholesterol-extracting compounds, such as beta-methyl cyclodextrin (betaMCD), decreases activity of both BACE1 and gamma-secretase, leading to an additive reduction in amyloid-beta generation. |
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Formal Description Interaction-ID: 23826 |
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| Drugbank entries | Show/Hide entries for Cholesterol |
| Comment | Reducing membrane cholesterol levels through cholesterol-extracting compounds, such as beta-methyl cyclodextrin (betaMCD), decreases activity of both BACE1 and gamma-secretase, leading to an additive reduction in amyloid-beta generation. |
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Formal Description Interaction-ID: 23827 |
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| Drugbank entries | Show/Hide entries for Cholesterol |
| Comment | Inclusion of cholesterol or sphingolipids in phosphatidylcholine-containing vesicles leads to increased gamma-secretase activity. |
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Formal Description Interaction-ID: 24058 |
drug/chemical compound Sphingolipid increases_activity of complex/PPI Gamma-secretase complex |
| Comment | Cholesterol- and sphingolipid enriched membrane microdomains called 'lipid rafts' play a role in the amyloidogenic processing of APP. |
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Formal Description Interaction-ID: 24059 |
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| Comment | A substantial pool of BACE1 is localized to lipid rafts mainly through palmitoylation of its transmembrane and cytoplasmic domains. |
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Formal Description Interaction-ID: 24060 |
gene/protein interacts (colocalizes) with cellular component |
| Drugbank entries | Show/Hide entries for BACE1 |
| Comment | Cholesterol depletion decreases the association of BACE1 with lipid rafts, which correlates with decreased amyloidogenic processing of APP. |
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Formal Description Interaction-ID: 24061 |
drug/chemical compound affects_processing of gene/protein |
| Drugbank entries | Show/Hide entries for Cholesterol or APP |
| Comment | Cholesterol depletion decreases the association of BACE1 with lipid rafts, which correlates with decreased amyloidogenic processing of APP. |
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Formal Description Interaction-ID: 24063 |
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| Drugbank entries | Show/Hide entries for Cholesterol |
| Comment | Cholesterol depletion decreases the association of BACE1 with lipid rafts, which correlates with decreased amyloidogenic processing of APP. |
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Formal Description Interaction-ID: 24064 |
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| Drugbank entries | Show/Hide entries for APP |
| Comment | Acute cell exposure to cholesterol promotes the co-clustering of APP and BACE1 in lipid raft domains, as well as their rapid endocytosis. |
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Formal Description Interaction-ID: 24085 |
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| Drugbank entries | Show/Hide entries for Cholesterol |
| Comment | Acute cell exposure to cholesterol promotes the co-clustering of APP and BACE1 in lipid raft domains, as well as their rapid endocytosis. |
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Formal Description Interaction-ID: 24086 |
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| Drugbank entries | Show/Hide entries for BACE1 or APP |
| Comment | Core components of the gamma-secretase complex, including presenilins, are also associated with lipid rafts. |
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Formal Description Interaction-ID: 24087 |
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| Comment | Core components of the gamma-secretase complex, including presenilins, are also associated with lipid rafts. |
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Formal Description Interaction-ID: 24088 |
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| Comment | Core components of the gamma-secretase complex, including presenilins, are also associated with lipid rafts. |
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Formal Description Interaction-ID: 24089 |
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| Comment | Inhibition of gamma-secretase activity leads to the accumulation of APP COOH-terminal products in lipid rafts. |
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Formal Description Interaction-ID: 24090 |
complex/PPI Gamma-secretase complex decreases_quantity of gene/protein |
| Comment | Sphingolipids, including ceramide, sphingomyelin and glycosphingolipids (GSLs) are major components of lipid rafts, playing a number of crucial parts in cell functions associated with normal as well as diseased states. |
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Formal Description Interaction-ID: 24094 |
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| Comment | Sphingolipids, including ceramide, sphingomyelin and glycosphingolipids (GSLs) are major components of lipid rafts, playing a number of crucial parts in cell functions associated with normal as well as diseased states. |
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Formal Description Interaction-ID: 24095 |
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| Comment | Sphingolipids, including ceramide, sphingomyelin and glycosphingolipids (GSLs) are major components of lipid rafts, playing a number of crucial parts in cell functions associated with normal as well as diseased states. |
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Formal Description Interaction-ID: 24096 |
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| Comment | Ceramide levels are elevated at the earliest clinically recognizable stage of AD, perhaps mediating oxidative stress-induced neuronal death. |
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Formal Description Interaction-ID: 24097 |
disease increases_quantity of drug/chemical compound |
| Comment | Ceramide also regulates BACE1-mediated processing of APP independently of its role in oxidative cell death. |
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Formal Description Interaction-ID: 24098 |
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| Drugbank entries | Show/Hide entries for APP |
| Comment | Inhibition of sphingomyelinase, the enzyme that mediates the conversion of sphingomyelin to ceramide, and the resulting sphingomyelin accumulation, reduces amyloid-beta secretion owing to inhibition of gamma-secretase activity. |
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Formal Description Interaction-ID: 24099 |
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| Comment | Inhibition of sphingomyelinase, the enzyme that mediates the conversion of sphingomyelin to ceramide, and the resulting sphingomyelin accumulation, reduces amyloid-beta secretion owing to inhibition of gamma-secretase activity. |
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Formal Description Interaction-ID: 24100 |
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| Comment | Suppression of the entire sphingolipid biosynthetic pathway by inhibition of serine palmitoyl transferase leads to increased production of amyloid-beta 42 (Abeta42; the 42-amino-acid form of amyloid-beta), whereas Abeta40 levels remain unchanged. |
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Formal Description Interaction-ID: 24102 |
complex/PPI Serine-palmitoyltransferase complex decreases_quantity of gene/protein |
| Comment | Suppression of the entire sphingolipid biosynthetic pathway by inhibition of serine palmitoyl transferase leads to increased production of amyloid-beta 42 (Abeta42; the 42-amino-acid form of amyloid-beta), whereas Abeta40 levels remain unchanged. |
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Formal Description Interaction-ID: 24103 |
complex/PPI Serine-palmitoyltransferase complex NOT affects_quantity of gene/protein |
| Comment | Sphingolipids modulate activity of BACE1. |
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Formal Description Interaction-ID: 24130 |
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| Drugbank entries | Show/Hide entries for BACE1 |
| Comment | GGPP and, to a lesser extent, FPP are significantly elevated in the frontal cortex of patients with AD, consistent with increased levels of their respective synthases. |
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Formal Description Interaction-ID: 24131 |
disease increases_quantity of drug/chemical compound |
| Comment | GGPP and, to a lesser extent, FPP are significantly elevated in the frontal cortex of patients with AD, consistent with increased levels of their respective synthases. |
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Formal Description Interaction-ID: 24146 |
disease increases_quantity of drug/chemical compound |
| Comment | Wortmannin, a classical inhibitor of the phosphatidylinositol 3-kinase (PI3K) pathway was shown to reduce the levels of amyloid- both in vitro and in vivo, thus further highlighting a potential role of phosphoinositides in AD pathogenesis. |
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Formal Description Interaction-ID: 24147 |
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| Comment | Gamma-secretase complex activity in liposomes is exquisitely sensitive to the presence of PtdIns(4,5)P2. |
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Formal Description Interaction-ID: 24149 |
drug/chemical compound affects_activity of complex/PPI Gamma-secretase complex |
| Comment | Cellular PtdIns(4,5)P2 levels inversely correlate with secreted Abeta42 levels in cultured fibroblasts. |
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Formal Description Interaction-ID: 24150 |
drug/chemical compound affects_quantity of gene/protein |
| Comment | PLD1 negatively regulates the processing of APP by PS1, probably through modulation of PS1 activity. |
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Formal Description Interaction-ID: 24156 |
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| Drugbank entries | Show/Hide entries for PLD1 or APP |
| Comment | PLD1 also promotes the cell surface delivery of PS1 and physically interacts with this protein. |
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Formal Description Interaction-ID: 24157 |
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| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | Gangliosides are abundant membrane glycosphingolipids that are primary modulators of amyloid-beta aggregation. They are concentrated in the luminal leaflet of various cellular organelles and the outer leaflet of the plasma membrane, where they are found in raftlike lipid microdomains that also contain cholesterol. |
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Formal Description Interaction-ID: 24158 |
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| Comment | Gangliosides, such as GM1, bind amyloid-beta and alter the conformation from random coils to more ordered structures with increased beta-sheet content, which correlates with toxicity. The presence of GM1-bound amyloid-beta (GAbeta) is associated with early pathological changes in A. |
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Formal Description Interaction-ID: 24159 |
drug/chemical compound interacts (colocalizes) with gene/protein |
| Comment | Cell surface GM1 acts as a 'seed' for amyloid-beta aggregation in neurons as well as in nerve terminal preparations. |
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Formal Description Interaction-ID: 24160 |
drug/chemical compound increases_quantity of phenotype |
| Comment | The seeding property of GM1 increases with the ageing process and is facilitated by cholesterol-rich environments, indicating that the process might occur in membrane rafts. |
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Formal Description Interaction-ID: 24161 |
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| Comment | Ablation of beta-1,4 N-acetylgalactosaminyltransferase 1 (also known as GM2/GD2 synthase) in a transgenic mouse model of AD leads to an accumulation of GM3 and a loss of GM1. |
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Formal Description Interaction-ID: 24162 |
gene/protein increases_quantity of drug/chemical compound |
| Comment | Ablation of beta-1,4 N-acetylgalactosaminyltransferase 1 (also known as GM2/GD2 synthase) in a transgenic mouse model of AD leads to an accumulation of GM3 and a loss of GM1. |
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Formal Description Interaction-ID: 24163 |
gene/protein decreases_quantity of drug/chemical compound |
| Comment | Genetic ablation of GD3 synthase (GD3S) improves cognitive function and decreases the amyloid-beta plaque burden in a bigenic mouse expressing FAD mutant versions of the APP and PSEN1 genes. |
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Formal Description Interaction-ID: 24164 |
gene/protein affects_activity of phenotype cognitive impairment |
| Comment | Genetic ablation of GD3 synthase (GD3S) improves cognitive function and decreases the amyloid-beta plaque burden in a bigenic mouse expressing FAD mutant versions of the APP and PSEN1 genes. |
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Formal Description Interaction-ID: 24165 |
gene/protein affects_quantity of phenotype |
| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 24182 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 24183 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 24184 |
gene/protein increases_activity of process |
| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 24185 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 24186 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 24187 |
disease increases_activity of process |
| Comment | Amyloid-beta can reduce metal ions like Zn2+ and Cu2+, thus producing hydrogen peroxide. |
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Formal Description Interaction-ID: 24188 |
gene/protein affects_quantity of drug/chemical compound |
| Comment | Response to cation stress is part of responses to stress. |
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Formal Description Interaction-ID: 36320 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 66691 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 66692 |
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| Comment | Amyloid-beta has been shown to cause oxidative stress through its interaction with transition metal ions, such as Cu2+ and Zn2+, which are enriched in senile plaques (aggregated amyloid-beta peptides). |
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Formal Description Interaction-ID: 66693 |
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| Comment | Inhibition of sphingomyelinase, the enzyme that mediates the conversion of sphingomyelin to ceramide, and the resulting sphingomyelin accumulation, reduces amyloid-beta secretion owing to inhibition of gamma-secretase activity. |
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Formal Description Interaction-ID: 77660 |
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| Comment | Inhibition of sphingomyelinase, the enzyme that mediates the conversion of sphingomyelin to ceramide, and the resulting sphingomyelin accumulation, reduces amyloid-beta secretion owing to inhibition of gamma-secretase activity. |
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Formal Description Interaction-ID: 77661 |
drug/chemical compound decreases_activity of process Abeta secretion |
| Comment | Inhibition of sphingomyelinase, the enzyme that mediates the conversion of sphingomyelin to ceramide, and the resulting sphingomyelin accumulation, reduces amyloid-beta secretion owing to inhibition of gamma-secretase activity. |
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Formal Description Interaction-ID: 79969 |
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| Comment | Inhibition of sphingomyelinase, the enzyme that mediates the conversion of sphingomyelin to ceramide, and the resulting sphingomyelin accumulation, reduces amyloid-beta secretion owing to inhibition of gamma-secretase activity. |
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Formal Description Interaction-ID: 79970 |
process increases_quantity of drug/chemical compound |
| Comment | The seeding property of GM1 increases with the ageing process and is facilitated by cholesterol-rich environments, indicating that the process might occur in membrane rafts. |
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Formal Description Interaction-ID: 80188 |
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| Drugbank entries | Show/Hide entries for Cholesterol |
| Comment | ACAT1 ablation also increases levels of oxysterol, 24(S)-hydroxycholesterol, suggesting a potential role of this cholesterol metabolite in decreasing amyloidogenesis. |
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Formal Description Interaction-ID: 88980 |
gene/protein decreases_quantity of drug/chemical compound Oxysterol |
| Drugbank entries | Show/Hide entries for SOAT1 |
| Comment | Cellular PtdIns(4,5)P2 levels inversely correlate with secreted Abeta42 levels in cultured fibroblasts. |
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Formal Description Interaction-ID: 125274 |
phenotype decreased Phosphatidylinositol-4,5-bisphosphate level increases_activity of phenotype increased Amyloid beta peptide (42) level |
| Comment | PLD1 also promotes the cell surface delivery of PS1 and physically interacts with this protein. |
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Formal Description Interaction-ID: 134637 |
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| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | PLD1 also promotes the cell surface delivery of PS1 and physically interacts with this protein. |
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Formal Description Interaction-ID: 134650 |
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| Comment | PLD1 hydrolyzes phosphatidylcholine to generate phosphatidic acid (PA) and free choline. |
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Formal Description Interaction-ID: 134783 |
gene/protein decreases_quantity of drug/chemical compound |
| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | PLD1 hydrolyzes phosphatidylcholine to generate phosphatidic acid (PA) and free choline. |
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Formal Description Interaction-ID: 134784 |
gene/protein increases_quantity of drug/chemical compound |
| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | PLD1 hydrolyzes phosphatidylcholine to generate phosphatidic acid (PA) and free choline. |
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Formal Description Interaction-ID: 134785 |
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| Drugbank entries | Show/Hide entries for PLD1 or Choline |
| Comment | Phosphatidic acid is a bioactive lipid mediating signalling processes as well as membrane budding and fusion along the secretory, endolysosomal and autophagy pathway. |
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Formal Description Interaction-ID: 134787 |
drug/chemical compound increases_activity of process |
| Comment | Phosphatidic acid is a bioactive lipid mediating signalling processes as well as membrane budding and fusion along the secretory, endolysosomal and autophagy pathway. |
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Formal Description Interaction-ID: 134789 |
drug/chemical compound increases_activity of process |
| Comment | PLD1 overexpression was shown to promote the cell surface delivery of APP and neurite outgrowth in primary hippocampal neurons expressing FAD mutant versions of PS1, two processes that are defective in mutant neurons. |
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Formal Description Interaction-ID: 134791 |
gene/protein increases_activity of phenotype increased cell surface delivery of APP |
| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | Cholesterol and sphingolipids are positive modulators of gamma-secretase activity while SMase and PLD1 have been identified as negative modulators of gamma-secretase activity. |
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Formal Description Interaction-ID: 134795 |
gene/protein decreases_activity of complex/PPI Gamma-secretase complex |
| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | PLD1 overexpression was shown to promote the cell surface delivery of APP and neurite outgrowth in primary hippocampal neurons expressing FAD mutant versions of PS1, two processes that are defective in mutant neurons. |
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Formal Description Interaction-ID: 134816 |
gene/protein increases_activity of process |
| Drugbank entries | Show/Hide entries for PLD1 |
| Comment | Cholesterol and sphingolipids are positive modulators of gamma-secretase activity while SMase and PLD1 have been identified as negative modulators of gamma-secretase activity. |
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Formal Description Interaction-ID: 134817 |
gene/protein Sphingomyelinase decreases_activity of complex/PPI Gamma-secretase complex |
| Comment | Cholesterol and sphingolipids are positive modulators of gamma-secretase activity while SMase and PLD1 have been identified as negative modulators of gamma-secretase activity. |
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Formal Description Interaction-ID: 134818 |
drug/chemical compound increases_activity of complex/PPI Gamma-secretase complex |
| Drugbank entries | Show/Hide entries for Cholesterol |
| Comment | Cholesterol and sphingolipids are positive modulators of gamma-secretase activity while SMase and PLD1 have been identified as negative modulators of gamma-secretase activity. |
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Formal Description Interaction-ID: 134819 |
drug/chemical compound Sphingolipids increases_activity of complex/PPI Gamma-secretase complex |