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p(HGNC:LRP1)

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Entity

Name
LRP1
Namespace
HGNC
Namespace Version
20180215
Namespace URL
https://arty.scai.fraunhofer.de/artifactory/bel/namespace/hgnc/hgnc-20180215.belns

Appears in Networks 6

APP processing in Alzheimer's disease v1.0.1

APP processing in Alzheimer's disease

Proteolytic processing of Alzeimer's beta-amyloid precursor protein v1.0.1

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

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 11

act(a(HBP:HBP00071), ma(tscript)) regulates p(HGNC:LRP1) View Subject | View Object

In a similar fashion, released AICD has been shown to possess transactivation activity and can regulate transcription of multiple genes including APP, GSK- 3b, KAI1, neprilysin, BACE1, p53, EGFR, and LRP1 [127-132] PubMed:21214928

Appears in Networks:
Annotations
MeSH
Endosomes
Confidence
Medium
MeSH
Neurons

complex(p(HGNC:APBB1), p(HGNC:APP), p(HGNC:LRP1)) hasComponent p(HGNC:LRP1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:APP), p(HGNC:LRP1)) hasComponent p(HGNC:LRP1) View Subject | View Object

Appears in Networks:

complex(p(HBP:HBP00071), p(HGNC:APBB1), p(HGNC:KAT5)) regulates p(HGNC:LRP1) View Subject | View Object

Although Tip60 does not bind to AICD directly, an indirect interaction between AICD and Tip60 is mediated by Fe65. Upon forming this complex, AICD is stabilized and can be translocated into the nucleus to regulate expression of genes such as KAI1, Neprilysin, LRP1, p53, GSK-3b and EGF receptor (Baek et al. 2002; Kim et al. 2003; Cao and Sudhof 2004; Pardossi-Piquard et al. 2005; Alves da Costa et al. 2006; Liu et al. 2007; Zhang et al. 2007) PubMed:22122372

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Neurons

a(CHEBI:rifampicin) increases act(p(HGNC:LRP1)) View Subject | View Object

The antibiotic rifampicin likewise promoted Aβ42 clearance by induc- ing BBB-localized LRP1 and P glycoprotein 1 (REFS273,292) . PubMed:30116051

Appears in Networks:
Annotations
MeSH
Blood-Brain Barrier

path(MESH:"Alzheimer Disease") decreases p(HGNC:LRP1) View Subject | View Object

In AD, these factors are impaired in a number of ways. First, expression of the blood efflux transporters LRP1123 and ABCB1147 is decreased, whereas expression of the blood influx transporter RAGE is upregulated. PubMed:26195256

Appears in Networks:
Annotations
MeSH
Hippocampus
MeSH
Temporal Lobe

a(CHEBI:calcitriol) increases p(HGNC:LRP1) View Subject | View Object

1,25(OH)2D3, the active form of vitamin D, plays a key role in enhancing transport of Aβ1–40 from the brain to the blood by reducing RAGE levels at the BBB, and also in contributing to periphery clearance by increasing levels of LRP1 both in vivo and in vitro (Guo et al. 2016b) PubMed:29626319

Appears in Networks:

a(CHEBI:donepezil) increases p(HGNC:LRP1) View Subject | View Object

Cholinesterase inhibitors donepezil and rivastigmine, upregulating transport proteins P-glycoprotein and LRP1, may improve Aβ clearance in the liver of rats (Mohamed et al. 2015) PubMed:29626319

Appears in Networks:

a(CHEBI:oleocanthal) increases p(HGNC:LRP1) View Subject | View Object

Oleocanthal, a special component of extra-virgin olive oil, increases cerebral clearance of Aβ across the BBB by enhancing the expression of important efflux transport proteins at the BBB containing LRP1 and P-gp, and activating the APOE-dependent Aβ clearance pathway in mice brains (Qosa et al. 2015) PubMed:29626319

Appears in Networks:
Annotations
MeSH
Blood-Brain Barrier

a(CHEBI:rivastigmine) increases p(HGNC:LRP1) View Subject | View Object

Cholinesterase inhibitors donepezil and rivastigmine, upregulating transport proteins P-glycoprotein and LRP1, may improve Aβ clearance in the liver of rats (Mohamed et al. 2015) PubMed:29626319

Appears in Networks:

p(HGNC:SLC2A1) increases p(HGNC:LRP1) View Subject | View Object

GLUT1, glucose transporter expressed in the BBB, regulates LRP1-dependent Aβ clearance via increasing the expression of LRP1 PubMed:29626319

Appears in Networks:
Annotations
MeSH
Blood-Brain Barrier

Out-Edges 10

p(HGNC:LRP1) increases tloc(a(CHEBI:"amyloid-beta")) View Subject | View Object

Some evidence suggests that LRP1 is the main transporter for Aβ efflux at the BBB, whereas other studies have demonstrated its role to be quite minor. PubMed:26195256

Appears in Networks:
Annotations
MeSH
Hippocampus
MeSH
Temporal Lobe

p(HGNC:LRP1) increases tloc(a(CHEBI:"amyloid-beta"), fromLoc(MESH:"Nephritis, Interstitial"), toLoc(MESH:Brain)) View Subject | View Object

Specifically, local soluble Aβ is transferred from the interstitium to the brain by LDL receptor (LDLR) family members such as LRP1, and ATP-binding cassette transporters (ABC transporters). PubMed:26195256

Appears in Networks:
Annotations
MeSH
Hippocampus
MeSH
Temporal Lobe

p(HGNC:LRP1) increases tloc(a(CHEBI:"amyloid-beta")) View Subject | View Object

ApoE is a cholesterol transporter that competes with Aβ for efflux by LRP1 from the interstitium into the circula- tion; PubMed:26195256

Appears in Networks:
Annotations
MeSH
Hippocampus
MeSH
Temporal Lobe

p(HGNC:LRP1) increases tloc(a(CHEBI:"amyloid-beta"), fromLoc(MESH:Brain), toLoc(MESH:Blood)) View Subject | View Object

LRP1, efflux transporter protein, is expressed mainly at the abluminal membrane of the BBB and highly expressive LRP1 can elevate the rate of Aβ clearance from brain to blood (Pflanzner et al. 2011) PubMed:29626319

Appears in Networks:

p(HGNC:LRP1) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

GLUT1, glucose transporter expressed in the BBB, regulates LRP1-dependent Aβ clearance via increasing the expression of LRP1 PubMed:29626319

Appears in Networks:
Annotations
MeSH
Blood-Brain Barrier

p(HGNC:LRP1) 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:LRP1) increases bp(GO:"heme catabolic process") View Subject | View Object

Hx inhibits the oxidative property of heme (Eskew et al., 1999) and mediates heme transportation to intracellular compartments through the macrophage receptor CD91 (Hvidberg et al., 2005), a critical step on heme catabolism. PubMed:24904418

Appears in Networks:
Annotations
Text Location
Review

p(HGNC:LRP1) increases deg(complex(a(CHEBI:heme), p(HGNC:HPX))) View Subject | View Object

Normally, haemopexin safely transports haem away from the vessel wall to ligate LRP1 (also termed CD91) on hepatocytes and macrophages, where the haem–haemopexin complex is endocytosed and haem is degraded intracellularly (Hvidberg et al, 2005). PubMed:25307023

Appears in Networks:
Annotations
Cell Ontology (CL)
macrophage
Text Location
Review

p(HGNC:LRP1) decreases complex(a(CHEBI:heme), p(HGNC:HPX)) View Subject | View Object

Free heme in blood is sequestered by hemopexin (Hpx) [23,24] and the Hpx-heme complex is cleared from the circulation by the hepatocyte receptor CD91 [25]. PubMed:26368565

Appears in Networks:
Annotations
Cell Ontology (CL)
hepatocyte
MeSH
Placenta
Text Location
Introduction

p(HGNC:LRP1) increases deg(a(CHEBI:heme)) View Subject | View Object

Normally, haemopexin safely transports haem away from the vessel wall to ligate LRP1 (also termed CD91) on hepatocytes and macrophages, where the haem–haemopexin complex is endocytosed and haem is degraded intracellularly (Hvidberg et al, 2005). PubMed:25307023

Appears in Networks:
Annotations
Cell Ontology (CL)
macrophage
Text Location
Review

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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.