Cloned (Comment) | Organism |
---|---|
enzyme overexpression in transgenic mmice | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Mus musculus | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q64430 | - |
- |
Mus musculus C57/BL6J | Q64430 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
aorta | - |
Mus musculus | - |
blood vessel | - |
Mus musculus | - |
endothelium | - |
Mus musculus | - |
Synonyms | Comment | Organism |
---|---|---|
ATP7A | - |
Mus musculus |
copper transporter | - |
Mus musculus |
Organism | Comment | Expression |
---|---|---|
Mus musculus | copper transporter ATP7A protein expression is significantly reduced in blood vessels from type 1 diabetes mellitus mice | down |
Mus musculus | insulin treatment, but not high glucose, increases enzyme ATP7A expression in vascular smooth muscles cells | up |
General Information | Comment | Organism |
---|---|---|
malfunction | role of extracellular superoxide dismutase SOD3 and ATP7A in endothelial dysfunction in type 1 diabetes mellitus. Type 1 diabetes mellitus-induced endothelial dysfunction and decrease of SOD3 activity are rescued in transgenic mice overexpressing the enzyme ATP7A, a copper transporter. Copper transporter ATP7A protein expression is significantly reduced in blood vessels from type 1 diabetes mellitus mice in part due to the insulin deficiency but not high glucose. Transgenic mice overexpressing ATP7A restore type 1 diabetes mellitus-induced impaired SOD3 activity and endothelial function by reducing superoxide levels | Mus musculus |
physiological function | the enzyme ATP7A plays a critical role in delivering cofactor copper to extracellular superoxide dismutase SOD3 for its full activation | Mus musculus |