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path(HBP:neurotoxicity)

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Entity

Name
neurotoxicity
Namespace
HBP
Namespace Version
20181221
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/bd0996a28201cad363557315043c6392e31abf58/export/hbp-names.belns

Appears in Networks 12

albuquerque2009 v1.0.0

This file encodes the article Mammalian Nicotinic Acetylcholine Receptors: From Structure to Function by Albuquerque et al, 2009

Nicotinic acetylcholine receptor signalling: roles in Alzheimer's disease and amyloid neuroprotection. v1.0.0

M1 muscarinic acetylcholine receptor in Alzheimer’s disease v1.0.0

This file encodes the article M1 muscarinic acetylcholine receptor in Alzheimer’s disease by Jiang et al, 2014

Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system v1.0.0

This document contains the curation of the review article Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system by Taly et al. 2009

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

The Ubiquitin–Proteasome System and the Autophagic–Lysosomal System in Alzheimer Disease v1.0.0

Pathological missorting of endogenous MAPT/Tau in neurons caused by failure of protein degradation systems v1.0.0

Inhibition of tau aggregation in a novel Caenorhabditis elegans model of tauopathy mitigates proteotoxicity v1.0.0

Nuclear Factor Kappa-light-chain-enhancer of Activated B Cells (NF-κB) - a Friend, a Foe, or a Bystander - in the Neurodegenerative Cascade and Pathogenesis of Alzheimer's Disease v1.0.0

Significance of NF-κB as a pivotal therapeutic target in the neurodegenerative pathologies of Alzheimer's disease and multiple sclerosis v1.0.0

Pathological missorting of endogenous MAPT/Tau in neurons caused by failure of protein degradation systems v1.0.1

In-Edges 43

a(CHEBI:nicotine) association path(HBP:neurotoxicity) View Subject | View Object

Metabolic degradation of nicotine and rapid clearance is a mechanism that protects neurons from greater nicotine concentrations, since nicotine readily crosses the mammalian blood-brain barrier and accumulates in the lipophilic brain environment to concentrations that may exceed plasma concentrations by one order of magnitude. Nevertheless, neurotoxicity to nicotine is not uncommon, as attested to by the recent increase in hospital emergency room visits by smokers who concurrently use the transdermal nicotine patch (503). PubMed:19126755

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act(a(CHEBI:"L-glutamate(2-)")) increases path(HBP:neurotoxicity) View Subject | View Object

For example, alpha4-specific agonists protect porcine small retinal ganglion cells against L-glutamate toxicity (Thompson et al., 2006), whereas alpha7 nAChRs protect large retinal ganglion cells (Wehrwein et al., 2004) against L-glutamate toxicity. PubMed:19293145

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MeSH
Retinal Ganglion Cells

act(a(CHEBI:"L-glutamate(2-)")) increases path(HBP:neurotoxicity) View Subject | View Object

Genistein, a phytoestrogen, protects SH-SY5Y cells (Bang et al., 2004) as well as cultured hippocampal neurons (Zeng et al., 2004) from Abeta toxicity. However, in addition to its action on estrogen receptors, genistein is also a general tyrosine kinase inhibitor that protects cultured neurons from L-glutamate toxicity (Kajta et al., 2007). PubMed:19293145

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Experimental Factor Ontology (EFO)
SH-SY5Y

a(CHEBI:"N-methyl-4-phenylpyridinium") increases path(HBP:neurotoxicity) View Subject | View Object

For example, non-alpha7 nAChRs protect cultured nigral dopaminergic neurons from toxicity induced by 1-methyl-4-phenylpyridinium, a neurotoxin that selectively damages nigrostriatal dopaminergic neurons (Jeyarasasingam et al., 2002), and this effect is not mediated by alpha7 receptors. PubMed:19293145

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MeSH
Dopaminergic Neurons

act(a(CHEBI:"N-methyl-D-aspartic acid")) increases path(HBP:neurotoxicity) View Subject | View Object

There is evidence that nicotine’s neuroprotective effects can be mediated through tumor necrosis factor-alpha (TNF-alpha). Application of either nicotine or TNF-alpha protects cultured mouse embryonic cortical neurons from N-methyl-D-aspartate (NMDA) toxicity, but coapplication of both does not. PubMed:19293145

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a(CHEBI:"amyloid-beta") increases path(HBP:neurotoxicity) 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

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MeSH
Brain

act(a(CHEBI:"amyloid-beta")) increases path(HBP:neurotoxicity) View Subject | View Object

In SHSY5Y cells, RNA interference (RNAi) knockdown of alpha7 enhanced Abeta toxicity (Qi et al., 2007), and alpha7 antagonists, but not alpha4beta2 antagonists, block galantamine protection of cultured rat neurons (Kihara et al., 2004). Donepezil protects cultured rat cortical neurons against Abeta toxicity through both alpha7 and non-alpha7 nAChRs (Takada et al., 2003). It is therefore likely that alpha7 nAChRs are the primary mediators of nicotine neuroprotection, but in some cells, non-alpha7 subtypes are also likely to contribute. PubMed:19293145

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act(a(CHEBI:"amyloid-beta")) increases path(HBP:neurotoxicity) View Subject | View Object

Genistein, a phytoestrogen, protects SH-SY5Y cells (Bang et al., 2004) as well as cultured hippocampal neurons (Zeng et al., 2004) from Abeta toxicity. However, in addition to its action on estrogen receptors, genistein is also a general tyrosine kinase inhibitor that protects cultured neurons from L-glutamate toxicity (Kajta et al., 2007). PubMed:19293145

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Experimental Factor Ontology (EFO)
SH-SY5Y

act(a(CHEBI:"amyloid-beta")) increases path(HBP:neurotoxicity) View Subject | View Object

Thus, it seems that nAChRs may play a role in mediating Abeta toxicity through synergistic mechanisms; in addition to possible direct interactions (binding), nAChRs may also result in accelerated cell death through enhancing intracellular Abeta accumulation. PubMed:19293145

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a(CHEBI:donepezil) decreases path(HBP:neurotoxicity) View Subject | View Object

In addition to nicotine, donepezil and rivastigmine, AChE inhibitors currently used as treatments for mild or moderate AD under the brand names of Aricept and Exelon, also protect cultured neuroblastoma cells from the toxic effects of Abeta. Although there is evidence that, in addition to inhibiting AChE, these ligands are also allosteric modulators of nAChRs (Schrattenholz et al., 1996; Coyle et al., 2007), it has not been established whether these AChE inhibitors protect neurons by their actions on alpha7 nAChRs rather than by simply inhibiting AChE, thereby elevating ACh in the medium. PubMed:19293145

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a(CHEBI:donepezil) decreases path(HBP:neurotoxicity) View Subject | View Object

In SHSY5Y cells, RNA interference (RNAi) knockdown of alpha7 enhanced Abeta toxicity (Qi et al., 2007), and alpha7 antagonists, but not alpha4beta2 antagonists, block galantamine protection of cultured rat neurons (Kihara et al., 2004). Donepezil protects cultured rat cortical neurons against Abeta toxicity through both alpha7 and non-alpha7 nAChRs (Takada et al., 2003). It is therefore likely that alpha7 nAChRs are the primary mediators of nicotine neuroprotection, but in some cells, non-alpha7 subtypes are also likely to contribute. PubMed:19293145

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a(CHEBI:estradiol) decreases path(HBP:neurotoxicity) View Subject | View Object

In support of this notion, beta-estradiol protects PC12 cells from amyloid toxicity, and this is prevented when alpha7 nAChRs are blocked with methyllycaconitine (Svensson and Nordberg, 1999). PubMed:19293145

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Experimental Factor Ontology (EFO)
PC12

act(a(CHEBI:ethanol)) increases path(HBP:neurotoxicity) View Subject | View Object

Nicotinic neuroprotection against non-Abeta toxicity is also mediated largely through alpha7 nAChRs. alpha7 nAChRs protect PC12 cells against ethanol toxicity (Li et al., 1999a) and from cell death associated with serum depletion (Ren et al., 2005); they protect cultured neurons against glutamate-induced excitotoxicity (Kaneko et al., 1997) and hippocampal slices against oxygen and glucose deprivation (Egea et al., 2007) through the activation of alpha7 nAChRs (Rosa et al., 2006). PubMed:19293145

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Experimental Factor Ontology (EFO)
PC12

a(CHEBI:nicotine) decreases path(HBP:neurotoxicity) View Subject | View Object

The discovery that nicotine, a ligand acting at nAChRs, and its mimetics can protect neurons against Abeta toxicity (Kihara et al., 1998) is of interest, especially in view of the observation that nicotine also enhances cognition (Rusted et al., 2000). Nicotinic receptors play a particularly prominent role in nicotine protection. The protective effect is blocked by the nicotinic antagonists dihydro-beta-erythroidine and mecamylamine (Kihara et al., 2001; Takada- Takatori et al., 2006). PubMed:19293145

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a(CHEBI:rivastigmine) decreases path(HBP:neurotoxicity) View Subject | View Object

In addition to nicotine, donepezil and rivastigmine, AChE inhibitors currently used as treatments for mild or moderate AD under the brand names of Aricept and Exelon, also protect cultured neuroblastoma cells from the toxic effects of Abeta. Although there is evidence that, in addition to inhibiting AChE, these ligands are also allosteric modulators of nAChRs (Schrattenholz et al., 1996; Coyle et al., 2007), it has not been established whether these AChE inhibitors protect neurons by their actions on alpha7 nAChRs rather than by simply inhibiting AChE, thereby elevating ACh in the medium. PubMed:19293145

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a(HBP:"amyloid-beta oligomers") association path(HBP:neurotoxicity) View Subject | View Object

Early work on AD considered the fibrillar form to be the toxic species. However, a lack of correlation between plaque burden and cognitive score contrasted with a strong positive correlation between total soluble amyloid and cognitive decline pointing to soluble, oligomeric forms as the primary toxic factor (Walsh and Selkoe, 2007). PubMed:19293145

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a(HBP:"amyloid-beta oligomers") directlyIncreases path(HBP:neurotoxicity) View Subject | View Object

However, other naturally occurring oligomeric forms of Abeta are also toxic (Deshpande et al., 2006; Shankar et al., 2008), and evidence is accumulating that the capacity of Abeta, mutant Abeta, or fragments of Abeta to aggregate into oligomers is directly related to toxicity (Luheshi et al., 2007). PubMed:19293145

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a(MESH:methyllycaconitine) decreases path(HBP:neurotoxicity) View Subject | View Object

In support of this notion, beta-estradiol protects PC12 cells from amyloid toxicity, and this is prevented when alpha7 nAChRs are blocked with methyllycaconitine (Svensson and Nordberg, 1999). PubMed:19293145

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Experimental Factor Ontology (EFO)
PC12

complex(a(CHEBI:"amyloid-beta"), p(HGNC:CHRNA7)) increases path(HBP:neurotoxicity) View Subject | View Object

Paradoxically, in addition to their neuroprotective action, nAChRs may also partly mediate the toxic action of Abeta. The toxicity of Abeta on SH-SY5Y cells, as measured by a 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay, in which the health of cells is monitored by their ability of cells to reduce 3-(4,5-dimethylthiazol- 2-yl)-2,5-diphenyltetrazolium bromide, was significantly impaired when alpha7 was silenced by RNAi, suggesting that Abeta may exert its toxicity, at least in part, through a pathway that includes alpha7 nAChRs (Qi et al., 2007). PubMed:19293145

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SH-SY5Y

p(HGNCGENEFAMILY:"Cholinergic receptors nicotinic subunits") decreases path(HBP:neurotoxicity) View Subject | View Object

There is abundant evidence that Abeta also affects cholinergic signaling in the brain. Recent studies indicate that brain nAChRs are not only affected by Abeta but can also initiate signaling pathways that protect against Abeta toxicity (Kihara et al., 1997b; Takada et al., 2003; Arias et al., 2005; Akaike, 2006; Meunier et al., 2006; Dineley, 2007; Liu et al., 2007). PubMed:19293145

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MeSH
Brain

p(HGNCGENEFAMILY:"Cholinergic receptors nicotinic subunits") association path(HBP:neurotoxicity) View Subject | View Object

Thus, it seems that nAChRs may play a role in mediating Abeta toxicity through synergistic mechanisms; in addition to possible direct interactions (binding), nAChRs may also result in accelerated cell death through enhancing intracellular Abeta accumulation. PubMed:19293145

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a(CHEBI:"amyloid-beta") increases path(HBP:neurotoxicity) View Subject | View Object

Nevertheless, a compound developed later, TBPB, selectively activates M1 mAChR in cell lines and shows no agonist activity in any other mAChR subtype. Interestingly, TBPB also potentiates the NMDA-evoked current in hippocampal pyramidal neurons, which is considered to be important for the effect of M1 mAChR on improving cognition. In addition, TBPB shifts the processing of APP in the non-amyloidogenic direction and thereafter decreases neurotoxic Abeta production vitro[120]. PubMed:24590577

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MeSH
Hippocampus
MeSH
Pyramidal Cells

a(CHEBI:"amyloid-beta polypeptide 42") increases path(HBP:neurotoxicity) View Subject | View Object

As with nicotine, the weak alpha7 nAChR agonist GTS-21 is neuroprotective, specifically protecting against Abeta1–42-elicited neurotoxicity154. This effect is probably due to small, protracted increases in receptor-mediated Ca2+ influx. importantly, high concentrations of GTS-21 reduced cell survival, underlining the possible risk of over-stimulation152 PubMed:19721446

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Review

a(CHEBI:"amyloid-beta polypeptide 42") increases path(HBP:neurotoxicity) View Subject | View Object

Regardless of the exact effect of Abeta1–42 on receptor activity, it does seem to block the activation by nicotine and, consistent with the cytoprotective nature of this interaction, amyloid deposition limits neuroprotection151. This phenomenon may explain at least part of the neurotoxicity that is associated with Abeta1–42 (ReF. 156). PubMed:19721446

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Review

a(MESH:"alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid") increases path(HBP:neurotoxicity) View Subject | View Object

Choline, like nicotine, can protect neural cells from cytotoxicity that is induced by growth factor deprivation152 or exposure to the glutamate analogue AMPA (alpha-amino-3-hydroxy-5-methyl-4- isoxazole propionic acid)153. PubMed:19721446

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a(HBP:"Tau aggregates") positiveCorrelation path(HBP:neurotoxicity) View Subject | View Object

Thrombin cleavage of the repeat domain construct yielded fragments that rapidly aggregated, which closely correlated with toxicity in cell culture (15). These fragments can also induce the aggregation of full-length tau (39). PubMed:24027553

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Review

act(p(HGNC:CTSD)) decreases path(HBP:neurotoxicity) View Subject | View Object

Cathepsin D seems particularly important for degrading tau, as its expression was neuroprotective in a Drosophila tauopathy model. Levels of cathepsin D are elevated in flies expressing mutant human tau. If cathepsin D is genetically ablated, these tau flies exhibit enhanced neurotoxicity and a shorter lifespan (93). PubMed:24027553

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MeSH
Tauopathies
Text Location
Review

p(HGNC:MAPT, frag("?", "17kD")) causesNoChange path(HBP:neurotoxicity) View Subject | View Object

In contrast, another study used mass spectroscopy and sequencing to identify the “17 kDa” tau cleavage product and found it did not correspond to the recombinant fragment utilized in the above studies (19). Expression of a recombinant form of the mass spectroscopy-identified fragment in hippocampal neurons was not toxic (19). PubMed:24027553

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Review

a(CHEBI:"amyloid-beta") increases path(HBP:neurotoxicity) View Subject | View Object

Furthermore, recent evidence suggests that tau is essential for the neurotoxicity of amyloid-b, providing a possible link between these classic AD targets and suggesting that reductions in tau levels might be important via multiple, beneficial mechanisms [46–48] PubMed:21882945

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p(HGNC:MAPT) increases path(HBP:neurotoxicity) View Subject | View Object

Furthermore, recent evidence suggests that tau is essential for the neurotoxicity of amyloid-b, providing a possible link between these classic AD targets and suggesting that reductions in tau levels might be important via multiple, beneficial mechanisms [46–48] PubMed:21882945

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a(CHEBI:"amyloid-beta polypeptide 42") positiveCorrelation path(HBP:neurotoxicity) View Subject | View Object

Consistent with these findings, strong overexpression of human Ab42, but not Ab40, in Drosophila neurons induces age-related accumulation of Ab in autolysosomes and neurotoxicity (Ling et al. 2009). PubMed:22908190

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MeSH
Neurons

a(CHEBI:"amyloid-beta polypeptide 42") increases path(HBP:neurotoxicity) View Subject | View Object

Ab42-induced neurotoxicity is further enhanced by autophagy activation and is partially rescued by autophagy inhibition. PubMed:22908190

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bp(GO:autophagy) decreases path(HBP:neurotoxicity) View Subject | View Object

Consistent with these findings, rapamycin induction of autophagy reduces tau pathology in the triple transgenic AD-mouse model (Caccamo et al. 2010), whereas in other models, autophagic–lysosomal dysfunction amplifies tau pathology and tau neurotoxicity (Hamano et al. 2008; Khurana et al. 2010). PubMed:22908190

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bp(GO:autophagy) increases path(HBP:neurotoxicity) View Subject | View Object

Ab42-induced neurotoxicity is further enhanced by autophagy activation and is partially rescued by autophagy inhibition. PubMed:22908190

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bp(GO:autophagy) decreases path(HBP:neurotoxicity) View Subject | View Object

Our previous work showed that inhibition of either the proteasome or autophagy in primary neurons induces pronounced neurotoxicity [23,24], making it impossible to address this issue in conventional neuron cultures. PubMed:30145931

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act(p(FPLX:Proteasome)) decreases path(HBP:neurotoxicity) View Subject | View Object

Our previous work showed that inhibition of either the proteasome or autophagy in primary neurons induces pronounced neurotoxicity [23,24], making it impossible to address this issue in conventional neuron cultures. PubMed:30145931

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p(HGNC:MAPT, var("p.Lys280del")) increases path(HBP:neurotoxicity) View Subject | View Object

From these data, we conclude that the continued expression of FL Tau V337M and F3DK280 is toxic for the neurons and as a conse- quence, the development of the nervous system is perturbed. PubMed:22611162

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p(HGNC:MAPT, var("p.Val277Met")) increases path(HBP:neurotoxicity) View Subject | View Object

From these data, we conclude that the continued expression of FL Tau V337M and F3DK280 is toxic for the neurons and as a conse- quence, the development of the nervous system is perturbed. PubMed:22611162

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a(CHEBI:"amyloid-beta") increases path(HBP:neurotoxicity) View Subject | View Object

Furthermore, negative regulators of NF-κB such as the NAD+- dependent histone deacetylase – SIRT1, abolish the deleterious neurotoxic effects of Amyloid-β PubMed:28745240

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MeSH
Alzheimer Disease

p(HGNC:SIRT1) decreases path(HBP:neurotoxicity) View Subject | View Object

Furthermore, negative regulators of NF-κB such as the NAD+- dependent histone deacetylase – SIRT1, abolish the deleterious neurotoxic effects of Amyloid-β PubMed:28745240

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MeSH
Alzheimer Disease

p(HGNC:TNF) increases path(HBP:neurotoxicity) View Subject | View Object

Furthermore, Amyloid-β actuates NF-κB – dependent pro-inflammatory pathways in microglia culminating in TNFα expression and subsequently TNFα effectuated neurotoxicity PubMed:28745240

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MeSH
Alzheimer Disease

a(CHEBI:"amyloid-beta") increases path(HBP:neurotoxicity) View Subject | View Object

This is supported by the observation that in mixed neuronal-glial cell cultures, Aβ induces increasing degree of neurotoxicity in an NF-κB dependent manner in the presence of higher proportion of glial cells PubMed:25652642

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MeSH
Neuroglia
MeSH
Neurons
MeSH
Alzheimer Disease

act(complex(GO:"NF-kappaB complex")) increases path(HBP:neurotoxicity) View Subject | View Object

This is supported by the observation that in mixed neuronal-glial cell cultures, Aβ induces increasing degree of neurotoxicity in an NF-κB dependent manner in the presence of higher proportion of glial cells PubMed:25652642

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MeSH
Neuroglia
MeSH
Neurons
MeSH
Alzheimer Disease

Out-Edges 5

path(HBP:neurotoxicity) association a(CHEBI:nicotine) View Subject | View Object

Metabolic degradation of nicotine and rapid clearance is a mechanism that protects neurons from greater nicotine concentrations, since nicotine readily crosses the mammalian blood-brain barrier and accumulates in the lipophilic brain environment to concentrations that may exceed plasma concentrations by one order of magnitude. Nevertheless, neurotoxicity to nicotine is not uncommon, as attested to by the recent increase in hospital emergency room visits by smokers who concurrently use the transdermal nicotine patch (503). PubMed:19126755

Appears in Networks:
Annotations
Text Location
Review

path(HBP:neurotoxicity) association a(HBP:"amyloid-beta oligomers") View Subject | View Object

Early work on AD considered the fibrillar form to be the toxic species. However, a lack of correlation between plaque burden and cognitive score contrasted with a strong positive correlation between total soluble amyloid and cognitive decline pointing to soluble, oligomeric forms as the primary toxic factor (Walsh and Selkoe, 2007). PubMed:19293145

Appears in Networks:

path(HBP:neurotoxicity) association p(HGNCGENEFAMILY:"Cholinergic receptors nicotinic subunits") View Subject | View Object

Thus, it seems that nAChRs may play a role in mediating Abeta toxicity through synergistic mechanisms; in addition to possible direct interactions (binding), nAChRs may also result in accelerated cell death through enhancing intracellular Abeta accumulation. PubMed:19293145

Appears in Networks:

path(HBP:neurotoxicity) positiveCorrelation a(HBP:"Tau aggregates") View Subject | View Object

Thrombin cleavage of the repeat domain construct yielded fragments that rapidly aggregated, which closely correlated with toxicity in cell culture (15). These fragments can also induce the aggregation of full-length tau (39). PubMed:24027553

Appears in Networks:
Annotations
Text Location
Review

path(HBP:neurotoxicity) positiveCorrelation a(CHEBI:"amyloid-beta polypeptide 42") View Subject | View Object

Consistent with these findings, strong overexpression of human Ab42, but not Ab40, in Drosophila neurons induces age-related accumulation of Ab in autolysosomes and neurotoxicity (Ling et al. 2009). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Neurons

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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.