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p(HGNC:IDE)

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Entity

Name
IDE
Namespace
hgnc
Namespace Version
20180828
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/1b20f0637c395f8aa89c2e2e342d7b704062c242/external/hgnc-symbols.belns

Appears in Networks 6

Nuclear receptors as therapeutic targets for Alzheimer's disease. v1.0.0

Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing v1.0.0

Clearance systems in the brain-implications for Alzheimer disease. v1.0.1

Clearance of Amyloid Beta and Tau in Alzheimer’s Disease:from Mechanisms to Therapy v1.0.1

Inflammasome activation and innate immunity in Alzheimer’s disease v1.0.2

Oxidative stress in health and disease: The therapeutic potential of Nrf2 activation v1.0.0

In-Edges 17

a(CHEBI:"GW 501516") increases p(HGNC:IDE) View Subject | View Object

In a study reported by Kalinin et al., treatment of 5xFAD mice with the PPAR-d agonist, GW742, resulted in decreased plaque burden and an increase in the expression of two Ab proteases, neprilysin and IDE [72]. PubMed:21718217

Appears in Networks:
Annotations
Confidence
High

a(CHEBI:"(-)-epigallocatechin") increases p(HGNC:IDE) View Subject | View Object

In regard to pharmacological manipulation, substances such as epigallocatechin and somatostatin promote the expression, secretion and (allosterically) catalytic activ- ity of IDE and neprilysin in parallel with an increase in the degradation of Aβ peptides 259,280 . PubMed:30116051

Appears in Networks:

a(CHEBI:"amyloid-beta polypeptide 42") decreases p(HGNC:IDE) View Subject | View Object

In a vicious circle, Aβ42 itself decreases IDE expression, although it may prompt its release from glia 254,259 . PubMed:30116051

Appears in Networks:

a(CHEBI:"(-)-epigallocatechin") increases sec(p(HGNC:IDE)) View Subject | View Object

In regard to pharmacological manipulation, substances such as epigallocatechin and somatostatin promote the expression, secretion and (allosterically) catalytic activ- ity of IDE and neprilysin in parallel with an increase in the degradation of Aβ peptides 259,280 . PubMed:30116051

Appears in Networks:

a(CHEBI:"(-)-epigallocatechin") increases act(p(HGNC:IDE)) View Subject | View Object

In regard to pharmacological manipulation, substances such as epigallocatechin and somatostatin promote the expression, secretion and (allosterically) catalytic activ- ity of IDE and neprilysin in parallel with an increase in the degradation of Aβ peptides 259,280 . PubMed:30116051

Appears in Networks:

a(CHEBI:somatostatin) increases p(HGNC:IDE) View Subject | View Object

In regard to pharmacological manipulation, substances such as epigallocatechin and somatostatin promote the expression, secretion and (allosterically) catalytic activ- ity of IDE and neprilysin in parallel with an increase in the degradation of Aβ peptides 259,280 . PubMed:30116051

Appears in Networks:

a(CHEBI:somatostatin) increases sec(p(HGNC:IDE)) View Subject | View Object

In regard to pharmacological manipulation, substances such as epigallocatechin and somatostatin promote the expression, secretion and (allosterically) catalytic activ- ity of IDE and neprilysin in parallel with an increase in the degradation of Aβ peptides 259,280 . PubMed:30116051

Appears in Networks:

a(CHEBI:somatostatin) increases act(p(HGNC:IDE)) View Subject | View Object

In regard to pharmacological manipulation, substances such as epigallocatechin and somatostatin promote the expression, secretion and (allosterically) catalytic activ- ity of IDE and neprilysin in parallel with an increase in the degradation of Aβ peptides 259,280 . PubMed:30116051

Appears in Networks:

path(MESH:"Alzheimer Disease") decreases p(HGNC:IDE) View Subject | View Object

Cerebral levels of IDE are reduced in early AD and in mouse models of AD, whereas, mirroring AD amyloidosis, Aβ42 accumulates in mice genetically depleted of IDE. PubMed:30116051

Appears in Networks:
Annotations
MeSH
Cerebrum

a(CHEBI:"all-cis-5,8,11,14,17-icosapentaenoic acid") increases act(p(HGNC:IDE)) View Subject | View Object

For example, eicosapentaenoic acid (EPA) can induce the activity of IDE and increase its gene expression, and docosahexaenoic acid (DHA) also directly elevates IDE activity and affects sorting by boosting exosome release of IDE (Grimm et al. 2016) PubMed:29626319

Appears in Networks:

a(CHEBI:"docosahexaenoic acid") increases act(p(HGNC:IDE)) View Subject | View Object

For example, eicosapentaenoic acid (EPA) can induce the activity of IDE and increase its gene expression, and docosahexaenoic acid (DHA) also directly elevates IDE activity and affects sorting by boosting exosome release of IDE (Grimm et al. 2016) PubMed:29626319

Appears in Networks:

a(CHEBI:somatostatin) increases p(HGNC:IDE) View Subject | View Object

Somatotatin also up-regulates the expression and secretion of IDE in order to enhance Aβ clearance (Tundo et al.2012) PubMed:29626319

Appears in Networks:

a(CHEBI:statin) increases sec(p(HGNC:IDE)) View Subject | View Object

Statin can lead to extracellular IDE secretion from astrocytes in an autophagy-based unconventional secretory pathway (Glebov and Walter 2012), thus enhancing the extracellular removal of Aβ PubMed:29626319

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte

bp(GO:aging) negativeCorrelation p(HGNC:IDE) View Subject | View Object

Meanwhile, an animal experiment showed that IDE expression will descend with age and diabetes, then resulting in Aβ deposition (Kochkina et al. 2015) PubMed:29626319

Appears in Networks:

path(MESH:"Diabetes Mellitus") negativeCorrelation p(HGNC:IDE) View Subject | View Object

Meanwhile, an animal experiment showed that IDE expression will descend with age and diabetes, then resulting in Aβ deposition (Kochkina et al. 2015) PubMed:29626319

Appears in Networks:

a(PUBCHEM:135316034) increases p(HGNC:IDE) View Subject | View Object

In Alzheimer disease, 66 genes were identified that are also modulated by Protandim at the gene expression level. Of these 66 genes, the first 43 of them (65%) were regulated by Protandim in the opposing direction to that taken by the Alzheimer disease process. The beneficial effect of Protandim is further supported by the fact that of the 10 gene products currently targeted by drug therapies, eight of them are modulated by Protandim in the same direction that is proposed to be beneficial and caused by the drug. PubMed:22020111

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

path(MESH:"Alzheimer Disease") decreases p(HGNC:IDE) View Subject | View Object

In Alzheimer disease, 66 genes were identified that are also modulated by Protandim at the gene expression level. Of these 66 genes, the first 43 of them (65%) were regulated by Protandim in the opposing direction to that taken by the Alzheimer disease process. The beneficial effect of Protandim is further supported by the fact that of the 10 gene products currently targeted by drug therapies, eight of them are modulated by Protandim in the same direction that is proposed to be beneficial and caused by the drug. PubMed:22020111

Appears in Networks:

Out-Edges 14

p(HGNC:IDE) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

They were able to show that the lipidation of ApoE enhanced the degradation of soluble species of Ab by neprilysin in the endolytic compartments of microglia as well as extracellularly through the actions of the insulindegrading enzyme (IDE) [13]. PubMed:21718217

Appears in Networks:
Annotations
Confidence
High

p(HGNC:IDE) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

Aβ42 and amylin (a pancreas-derived, AD-associated protein found in brain) are substrates for degradation by IDE, which also irreversibly traps Aβ42 and α-synuclein, preventing their aggregation and promoting ALN and UPS elimination 259 . PubMed:30116051

Appears in Networks:

p(HGNC:IDE) increases deg(p(HGNC:IAPP)) View Subject | View Object

Aβ42 and amylin (a pancreas-derived, AD-associated protein found in brain) are substrates for degradation by IDE, which also irreversibly traps Aβ42 and α-synuclein, preventing their aggregation and promoting ALN and UPS elimination 259 . PubMed:30116051

Appears in Networks:

p(HGNC:IDE) decreases a(HBP:HBP00016) View Subject | View Object

Aβ42 and amylin (a pancreas-derived, AD-associated protein found in brain) are substrates for degradation by IDE, which also irreversibly traps Aβ42 and α-synuclein, preventing their aggregation and promoting ALN and UPS elimination 259 . PubMed:30116051

Appears in Networks:

p(HGNC:IDE) decreases a(HBP:HBP00018) View Subject | View Object

Aβ42 and amylin (a pancreas-derived, AD-associated protein found in brain) are substrates for degradation by IDE, which also irreversibly traps Aβ42 and α-synuclein, preventing their aggregation and promoting ALN and UPS elimination 259 . PubMed:30116051

Appears in Networks:

p(HGNC:IDE) decreases a(HBP:HBP00092) View Subject | View Object

IDE also degrades and prevents the forma- tion of α-synuclein fibrils 259 . PubMed:30116051

Appears in Networks:

p(HGNC:IDE) decreases a(CHEBI:"amyloid-beta", loc(GO:intracellular)) View Subject | View Object

Extracellular Aβ can also be degraded by proteases, such as neprily- sin (a membrane-anchored zinc metalloendopeptidase that degrades the Aβ monomers Aβ1-40 and Aβ1-42, and Aβ oligomers),119 matrix metalloproteinases 2, 3 and 9,120 glutamate carboxypeptidase II,121 endothelin-converting enzyme,122 tissue plasminogen activator,123 plasmin,120 angiotensin-converting enzyme,120 and insulin-degrading enzyme. PubMed:26195256

Appears in Networks:

p(HGNC:IDE) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

Extracellular Aβ degrading enzymes include neprilysin (NEP), insulin-degrading enzyme (IDE), matrix metalloproteinases (MMPs), angiotensin converting enzyme (ACE), endothelin-converting enzyme (ECE), and plasmin (Baranello et al. 2015) PubMed:29626319

Appears in Networks:

p(HGNC:IDE) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

IDE, a zinc endopeptidase, can degrade extracellular Aβ (Vekrellis et al. 2000) PubMed:29626319

Appears in Networks:

p(HGNC:IDE) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

Exercise training can increase extracellular Aβ clearance in the brains of Tg2576 mice in a dose-dependent manner through up-regulating NEP, IDE, MMP9, LRP1, and HSP70 (Moore et al. 2016) PubMed:29626319

Appears in Networks:

p(HGNC:IDE) negativeCorrelation bp(GO:aging) View Subject | View Object

Meanwhile, an animal experiment showed that IDE expression will descend with age and diabetes, then resulting in Aβ deposition (Kochkina et al. 2015) PubMed:29626319

Appears in Networks:

p(HGNC:IDE) negativeCorrelation path(MESH:"Diabetes Mellitus") View Subject | View Object

Meanwhile, an animal experiment showed that IDE expression will descend with age and diabetes, then resulting in Aβ deposition (Kochkina et al. 2015) PubMed:29626319

Appears in Networks:

p(HGNC:IDE) decreases a(CHEBI:"amyloid-beta") View Subject | View Object

The combined effect of the increased IDE production and phagocytic Abeta clearance reduced the cerebral Abeta load substantially, even at late life. Since immunohistochemistry found NLRP3 exclusively expressed in microglial cells, it has been concluded that the observed changes were entirely due to NLRP3 inflammasome modulation in these cells PubMed:28019679

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Neurons
NeuroMMSigDB
Amyloidogenic subgraph
NeuroMMSigDB
Insulin signal transduction

p(HGNC:IDE) regulates complex(GO:"NLRP3 inflammasome complex") View Subject | View Object

The combined effect of the increased IDE production and phagocytic Abeta clearance reduced the cerebral Abeta load substantially, even at late life. Since immunohistochemistry found NLRP3 exclusively expressed in microglial cells, it has been concluded that the observed changes were entirely due to NLRP3 inflammasome modulation in these cells PubMed:28019679

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Neurons
NeuroMMSigDB
Amyloidogenic subgraph
NeuroMMSigDB
Insulin signal transduction

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.