Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
amyloid-beta aggregates
Namespace
HBP
Namespace Version
20181029
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/785431732a26d6809b4162d98b95687d16404e63/export/hbp-names.belns

Appears in Networks 12

In-Edges 22

path(MESH:"Alzheimer Disease") association a(HBP:"amyloid-beta aggregates") View Subject | View Object

It is generally agreed that the beta-amyloid peptide (Abeta) plays an important role in the development of AD. The brains of patients with AD contain deposits of Abeta, and Abeta is toxic to cultured neurons (Kihara et al., 1997a; Yao et al., 2005). In addition, mice transgenically overexpressing Abeta or with mutations that enhance Abeta aggregation show many of the symptoms of AD (Hsiao et al., 1996; van Groen et al., 2006). PubMed:19293145

path(MESH:"Plaque, Amyloid") association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The hallmarks of AD pathology are the accumulation of amyloid-beta (Abeta) peptide aggregates (neuritic plaques) and hyperphosphorylated tau protein (neurofibrillary tangles). PubMed:24511233

p(HGNC:CHRNA7) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

This prospect was supported by the finding that α7 nAChRs were found in plaques (159), and α7 and α4 subunits positively correlated with neurons that accumulated Aβ and hyperphosphorylated tau in AD brain tissue (161). PubMed:17009926

complex(a(CHEBI:"amyloid-beta"), a(MESH:"alpha7 Nicotinic Acetylcholine Receptor")) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

The mechanism proposed is that the Aß-alpha7 nAChR interaction could activate neuroprotective downstream pathways (Parri et al., 2011), and that at the same time the interaction engages Abeta preventing its aggregation PubMed:25514383

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

With the progression of the disease the amount of Abeta increases, it starts to accumulate, and becomes toxic for the neurons (Hernandez et al., 2010) PubMed:25514383

p(HGNC:APP, var("?")) increases a(HBP:"amyloid-beta aggregates") View Subject | View Object

They have demonstrated that AD can be caused by mutations in the APP gene, either in the vicinity of the secretase cleavage sites, causing abnormal APP processing, or in the sequence coding for Abeta, giving rise to a peptide that is more likely to self-aggregate PubMed:14556719

path(MESH:"Prion Diseases") increases a(HBP:"amyloid-beta aggregates") View Subject | View Object

Prion disease neuropathology is characterized by widespread neuronal death, accompanied by spongiform vacuolation and astrogliosis, usually combined with widespread deposits of extracellular amyloid aggregates. PubMed:14556719

path(MESH:"Alzheimer Disease") positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

AD (Alzheimer’s disease) is a progressive neurodegenerative disorder characterized by the extracellular accumulation of amyloid beta-peptide and the intracellular accumulation of tau PubMed:22817713

a(CHEBI:"methylene blue") decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

In mechanistic studies, it was proposed that methylene blue inhibits the Aβ-ABAD interaction and decreases mitochondrial dysfunction by decreasing the expression of ABAD levels, in addition to decreasing Aβ levels. PubMed:30444369

a(HBP:AG18051) decreases act(a(HBP:"amyloid-beta aggregates")) View Subject | View Object

Moreover, it has been shown to ameliorate Aβ-induced toxicity at the cellular level. 7 PubMed:30444369

a(PUBCHEM:5757) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

For example, estradiol can reduce the generation of Aβ by altering the metabolism of APP and disrupting it’s trafficking. PubMed:30444369

p(HGNC:CSNK1A1) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

p(HGNC:CRYAB) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

p(HGNC:HSPB1) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

p(HGNC:HSPB6) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

p(HGNC:HSPB8) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

act(p(HGNC:SYK)) positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

In addition, we observed that pSyk immunoreactivity is upregulated near A β plaques but neither colocalizes with microglia nor astrocytes suggesting that it could be of neuronal origin. (Fig. 1e). PubMed:28877763

act(p(HGNC:SYK)) positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

In conclusion, activated Syk is not only found in microglia but also in neurons near A β deposits, par- ticularly in dystrophic neurites of Tg APPsw and Tg PS1/APPsw mice supporting a possible role of Syk activation in the formation of dystrophic neurites. PubMed:28877763

act(p(HGNC:SYK)) positiveCorrelation a(HBP:"amyloid-beta aggregates") View Subject | View Object

We found an increase in Syk activation in DNs surrounding A β deposits as well as in neurons displaying an accumu- lation of phosphorylated Tau at Y18 and elevated levels of MC1 pathogenic tau conformers in AD brain sections whereas only weak immunoreactivity for pSyk was ob- served in brain sections from a non-demented control (Figs. 15, 16 and 17). PubMed:28877763

a(PUBCHEM:155160) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

Beneficial effects of 4-O-methylhonokinol on memory were observed by the reduction of Aaggregation in A 1-42-injected mice and memory-impaired mice with its anti-oxidative and anti-inflammatory qualities [141–143]. PubMed:29179999

a(PUBCHEM:442534) decreases a(HBP:"amyloid-beta aggregates") View Subject | View Object

Paeoniflorin improved memory impairments and lowered A accumulation in APP/PS1 trans-genic mice [1]. PubMed:29179999

p(HGNC:PTGS2) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

In addition, COX-2, mainly regulated by NF-κB, is notably upregulated in the brains of AD patients, which may be associated with the formation of Aβ plaque [65]. PubMed:27288790

Out-Edges 19

a(HBP:"amyloid-beta aggregates") association path(MESH:"Alzheimer Disease") View Subject | View Object

It is generally agreed that the beta-amyloid peptide (Abeta) plays an important role in the development of AD. The brains of patients with AD contain deposits of Abeta, and Abeta is toxic to cultured neurons (Kihara et al., 1997a; Yao et al., 2005). In addition, mice transgenically overexpressing Abeta or with mutations that enhance Abeta aggregation show many of the symptoms of AD (Hsiao et al., 1996; van Groen et al., 2006). PubMed:19293145

a(HBP:"amyloid-beta aggregates") association path(MESH:"Plaque, Amyloid") View Subject | View Object

The hallmarks of AD pathology are the accumulation of amyloid-beta (Abeta) peptide aggregates (neuritic plaques) and hyperphosphorylated tau protein (neurofibrillary tangles). PubMed:24511233

a(HBP:"amyloid-beta aggregates") association p(HGNC:CHRNA7) View Subject | View Object

This prospect was supported by the finding that α7 nAChRs were found in plaques (159), and α7 and α4 subunits positively correlated with neurons that accumulated Aβ and hyperphosphorylated tau in AD brain tissue (161). PubMed:17009926

a(HBP:"amyloid-beta aggregates") increases path(MESH:"Plaque, Amyloid") View Subject | View Object

Senile plaques consist of deposits of small peptides called beta-amyloid (Abeta). Multiple lines of evidence suggest that the overproduction/ aggregation of neurotoxic Abeta in vulnerable brain regions is the primary cause of AD PubMed:24590577

a(HBP:"amyloid-beta aggregates") increases path(MESH:"Alzheimer Disease") View Subject | View Object

Senile plaques consist of deposits of small peptides called beta-amyloid (Abeta). Multiple lines of evidence suggest that the overproduction/ aggregation of neurotoxic Abeta in vulnerable brain regions is the primary cause of AD PubMed:24590577

a(HBP:"amyloid-beta aggregates") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

With the progression of the disease the amount of Abeta increases, it starts to accumulate, and becomes toxic for the neurons (Hernandez et al., 2010) PubMed:25514383

a(HBP:"amyloid-beta aggregates") positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

AD (Alzheimer’s disease) is a progressive neurodegenerative disorder characterized by the extracellular accumulation of amyloid beta-peptide and the intracellular accumulation of tau PubMed:22817713

a(HBP:"amyloid-beta aggregates") decreases act(p(FPLX:COX)) View Subject | View Object

Accumulation of Aβ has also been associated with a decrease in the activity of cytochrome c oxidase, the terminal enzyme in the electron transport chain. PubMed:30444369

a(HBP:"amyloid-beta aggregates") association p(HGNC:CSNK1A1) View Subject | View Object

Isoforms of CK1 are responsible for tau phosphorylation. 129 The enzyme can modulate the activity of γ-secretase and consequently the production of Aβ. PubMed:30444369

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB1) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

a(HBP:"amyloid-beta aggregates") association p(HGNC:CRYAB) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB6) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB8) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

a(HBP:"amyloid-beta aggregates") positiveCorrelation act(p(HGNC:SYK)) View Subject | View Object

In addition, we observed that pSyk immunoreactivity is upregulated near A β plaques but neither colocalizes with microglia nor astrocytes suggesting that it could be of neuronal origin. (Fig. 1e). PubMed:28877763

a(HBP:"amyloid-beta aggregates") positiveCorrelation act(p(HGNC:SYK)) View Subject | View Object

In conclusion, activated Syk is not only found in microglia but also in neurons near A β deposits, par- ticularly in dystrophic neurites of Tg APPsw and Tg PS1/APPsw mice supporting a possible role of Syk activation in the formation of dystrophic neurites. PubMed:28877763

a(HBP:"amyloid-beta aggregates") positiveCorrelation act(p(HGNC:SYK)) View Subject | View Object

We found an increase in Syk activation in DNs surrounding A β deposits as well as in neurons displaying an accumu- lation of phosphorylated Tau at Y18 and elevated levels of MC1 pathogenic tau conformers in AD brain sections whereas only weak immunoreactivity for pSyk was ob- served in brain sections from a non-demented control (Figs. 15, 16 and 17). PubMed:28877763

a(HBP:"amyloid-beta aggregates") increases act(p(FPLX:"IKK_complex")) View Subject | View Object

Under different envi- ronmental conditions such as Aβ/ROS/cytokines accumulation, the IκB kinase (IKK) complex becomes activated and mediates the phosphoryla- tion of IκBs, then IκBs are degradated and the remaining NF-κB dimer is activated and thus translocates to the nucleus where it binds to the DNA consensus sequence of various target genes [9–11]. PubMed:27288790

a(HBP:"amyloid-beta aggregates") association p(HGNC:PTGS2) View Subject | View Object

In addition, COX-2, mainly regulated by NF-κB, is notably upregulated in the brains of AD patients, which may be associated with the formation of Aβ plaque [65]. PubMed:27288790

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.