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Appears in Networks 4

In-Edges 3

a(CHEBI:"amyloid-beta polypeptide 42") increases complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) View Subject | View Object

The Abeta1-42 peptide is one of the breakdown products of the proteolytic cleavage of the amyloid precursor protein by beta- and gamma-secretases. In biopsy samples of human brain tissue obtained from AD patients and in ectopic systems overexpressing either alpha7 nAChRs or APP, Abeta1-42 coimmunoprecipitates with alpha7 nAChRs (490). The Abeta1-42 peptide also displaces binding of [3H]MLA from alpha7 nAChRs in cerebral cortical and hippocampal synaptosomes (490). PubMed:19126755

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
Text Location
Review

path(MESH:"Alzheimer Disease") association complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) View Subject | View Object

Although Aβ peptides negatively alter the cholinergic system at multiple sites, including ACh synthesis, ACh release, and muscarinic receptors (157), the discovery that Aβ1−42 binds to α7 nAChRs with high affinity suggested the potential for a causal role of nAChRs in AD (159, 160). PubMed:17009926

path(MESH:"Plaque, Amyloid") association complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) View Subject | View Object

They showed that alpha7 subunits co-localize with Abeta1-42 in senile plaques of brain slices obtained from patients that suffered from sporadic AD PubMed:25514383

Out-Edges 5

complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) decreases act(a(MESH:Bungarotoxins)) View Subject | View Object

However, it has been shown that Abeta1–42 binds with high affinity to alpha7 nAChRs in several different neuronal tissues (Wang et al., 2000a) and displaces alpha-bungarotoxin binding (Wang et al., 2000a,b) and, rather than inhibiting receptor internalization, alpha-bungarotoxin enhances internalization of heterologously expressed nAChRs (Kumari et al., 2008). PubMed:19293145

complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) association path(MESH:"Alzheimer Disease") View Subject | View Object

Although Aβ peptides negatively alter the cholinergic system at multiple sites, including ACh synthesis, ACh release, and muscarinic receptors (157), the discovery that Aβ1−42 binds to α7 nAChRs with high affinity suggested the potential for a causal role of nAChRs in AD (159, 160). PubMed:17009926

complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) association path(MESH:"Plaque, Amyloid") View Subject | View Object

They showed that alpha7 subunits co-localize with Abeta1-42 in senile plaques of brain slices obtained from patients that suffered from sporadic AD PubMed:25514383

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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.