Name
SH-SY5Y
Namespace Keyword
CellLine
Namespace
Experimental Factor Ontology (EFO)
Namespace Version
20170511
Namespace URL
https://arty.scai.fraunhofer.de/artifactory/bel/annotation/cell-line/cell-line-20170511.belanno

Sample Annotated Edges 5

a(HBP:APP695) association p(HGNC:BACE1) View Subject | View Object

Using the same anti-peptide sera we can detect expression of endogenous Asp 2 in SH-SY5Y cells stably expressing the 695 isoform of APP (SH-SY5Y APP-695) and in COS-7 cells expressing the 751 isoform of APP (COS-7 APP-751). The level of Asp 2 is increased upon transient transfection with the protein. PubMed:10656250

Annotations
Experimental Factor Ontology (EFO)
SH-SY5Y

p(HGNC:BACE1) increases sec(a(HBP:"sAPP-beta")) View Subject | View Object

Transient transfection of SH-SY5Y APP-695 cells with Asp 2 (Fig. 2a) results in a significant increase in the secretion of sAPPb (Fig. 2b) consistent with Asp 2 being b-secretase. To demonstrate that this increase in sAPPb is linked to the proteolytic activity of Asp 2, we mutated each of the proposed catalytic aspartic residues at positions 25 and 215 (determined by comparison with the position of the known catalytic aspartyl residues in pepsin) to asparagine. Both mutants and the wild-type Asp 2 are expressed to similar levels (Fig. 2a). PubMed:10656250

Annotations
Experimental Factor Ontology (EFO)
SH-SY5Y

p(HGNC:BACE1) association a(HBP:APP695) View Subject | View Object

Using the same anti-peptide sera we can detect expression of endogenous Asp 2 in SH-SY5Y cells stably expressing the 695 isoform of APP (SH-SY5Y APP-695) and in COS-7 cells expressing the 751 isoform of APP (COS-7 APP-751). The level of Asp 2 is increased upon transient transfection with the protein. PubMed:10656250

Annotations
Experimental Factor Ontology (EFO)
SH-SY5Y

a(CHEBI:estrogen) decreases act(p(HBP:"APOE e4")) View Subject | View Object

ApoE-epsilon4, but not ApoE-epsilon3, disrupts carbachol-stimulated phosphoinositol (PI) hydrolysis and so does Abeta and Abeta/ApoE-epsilon4 complexes in SH-SY5Y cells (Cedazo- Mínguez and Cowburn, 2001). The effect of Abeta and its ApoE complex on PI hydrolysis were blocked by estrogen, and this disruption was itself blocked by wortmannin, suggesting that PI3K mediates estrogen’s effect on PI hydrolysis. PubMed:19293145

a(CHEBI:nicotine) decreases act(a(CHEBI:thapsigargin)) View Subject | View Object

Nicotine protects SH-SY5Y cells from cell death induced by thapsigargin, an inhibitor of the sarcoplasmic-reticulum calcium pump (Arias et al., 2004). PubMed:19293145

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.