General Information:
Id: | 427 |
Diseases: |
Alzheimer disease
- [OMIM]
|
Mus musculus | |
BTO:0000165 C2C12 cell | |
article | |
Reference: | Lee HK et al.(2009) The insulin/Akt signaling pathway is targeted by intracellular beta-amyloid Mol. Biol. Cell 20: 1533-1544 [PMID: 19144826] |
Interaction Information:
Comment | In cell culture, intraneuronal beta-amyloid expression inhibited both insulin-induced Akt phosphorylation and activity. |
Formal Description Interaction-ID: 1867 |
gene/protein decreases_phosphorylation of gene/protein |
Drugbank entries | Show/Hide entries for AKT1 |
Comment | In cell culture, intraneuronal beta-amyloid expression inhibited both insulin-induced Akt phosphorylation and activity. |
Formal Description Interaction-ID: 1868 |
gene/protein decreases_activity of gene/protein |
Drugbank entries | Show/Hide entries for AKT1 |
Comment | Intraneuronal beta-amyloid blocked the association between PDK and Akt in cell-based and in vitro experiments. |
Formal Description Interaction-ID: 1869 |
|
Drugbank entries | Show/Hide entries for PDPK1 |
Comment | Beta-amyloid did not interrupt Akt or PI3K activities (once stimulated) nor did it affect more proximal signal events. |
Formal Description Interaction-ID: 1879 |
gene/protein NOT decreases_activity of |
Comment | Intraneuronal beta-amyloid blocked the association between PDK and Akt in cell-based and in vitro experiments. |
Formal Description Interaction-ID: 1883 |
|
Drugbank entries | Show/Hide entries for AKT1 or PDPK1 |
Comment | Intraneuronal beta-amyloid blocked the association between PDK and Akt in cell-based and in vitro experiments. The interaction of PDK with Akt1 is interrupted by intracellular beta-amyloid42. |
Formal Description Interaction-ID: 1884 |
gene/protein decreases_activity of complex/PPI AKT1-PDPK1 interaction |
Comment | Intracellular beta-amyloid expression decreases myotube length and caliber and increases pyknotic nuclei. |
Formal Description Interaction-ID: 1993 |
|
Comment | Intracellular beta-amyloid expression decreases myotube length and caliber and increases pyknotic nuclei. |
Formal Description Interaction-ID: 1994 |
gene/protein decreases_activity of process |
Comment | Immunoblot of p-GSK-3alpha/beta shows significantly inhibited phosphorylation in cultures treated with insulin. p-Akt (Ser473) and p-GSK-3A/B levels were increased by insulin treatment. |
Formal Description Interaction-ID: 1997 |
complex/PPI Insulin increases_phosphorylation of gene/protein |
Drugbank entries | Show/Hide entries for GSK3B |
Comment | The stimulated activity of Akt1 on the GSK substrate is markedly inhibited in the presence of intracellular beta-amyloid42. |
Formal Description Interaction-ID: 2001 |
gene/protein decreases_activity of gene/protein |
Drugbank entries | Show/Hide entries for AKT1 |
Comment | Intraneuronal beta-amyloid blocked the association between PDK and Akt in cell-based and in vitro experiments. The interaction of PDK with Akt1 is interrupted by intracellular beta-amyloid42. |
Formal Description Interaction-ID: 2004 |
|
Drugbank entries | Show/Hide entries for AKT1 |
Comment | In cell culture, intraneuronal beta-amyloid expression inhibited both insulin-induced Akt phosphorylation and activity. |
Formal Description Interaction-ID: 129312 |
|
Drugbank entries | Show/Hide entries for AKT1 |
Comment | Immunoblot of p-GSK-3alpha/beta shows significantly inhibited phosphorylation in cultures treated with insulin. p-Akt (Ser473) and p-GSK-3A/B levels were increased by insulin treatment. |
Formal Description Interaction-ID: 134713 |
protein modification GSK3B-phos decreases_activity of gene/protein |
Drugbank entries | Show/Hide entries for GSK3B |
Comment | Immunoblot of p-GSK-3alpha/beta shows significantly inhibited phosphorylation in cultures treated with insulin. p-Akt (Ser473) and p-GSK-3A/B levels were increased by insulin treatment. |
Formal Description Interaction-ID: 134773 |
protein modification GSK3A-phos decreases_activity of gene/protein |
Comment | In cell culture, intraneuronal beta-amyloid expression inhibited both insulin-induced Akt phosphorylation and activity. |
Formal Description Interaction-ID: 134774 |
gene/protein decreases_activity of complex/PPI Insulin |
Comment | In cell culture, intraneuronal beta-amyloid expression inhibited both insulin-induced Akt phosphorylation and activity. |
Formal Description Interaction-ID: 134775 |
complex/PPI Insulin increases_quantity of protein modification AKT1-phos |
Comment | The stimulated activity of Akt1 on the GSK substrate is markedly inhibited in the presence of intracellular beta-amyloid42. |
Formal Description Interaction-ID: 134776 |
|
Drugbank entries | Show/Hide entries for GSK3B |
Comment | The stimulated activity of Akt1 on the GSK substrate is markedly inhibited in the presence of intracellular beta-amyloid42. |
Formal Description Interaction-ID: 134777 |
protein modification AKT1-phos increases_quantity of protein modification GSK3B-phos |
Comment | p-Akt (Ser473) and p-GSK-3A/B levels were increased by insulin treatment. |
Formal Description Interaction-ID: 134778 |
complex/PPI Insulin increases_quantity of protein modification GSK3B-phos |
Comment | p-Akt (Ser473) and p-GSK-3A/B levels were increased by insulin treatment. |
Formal Description Interaction-ID: 134779 |
complex/PPI Insulin increases_quantity of protein modification GSK3A-phos |
Comment | In cell culture, intraneuronal beta-amyloid expression inhibited both insulin-induced Akt phosphorylation and activity. |
Formal Description Interaction-ID: 134780 |
protein modification AKT1-phos increases_activity of gene/protein |
Drugbank entries | Show/Hide entries for AKT1 |