Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates in vivo | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Rattus norvegicus Sprague-Dawley | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
artery | PDE 1 vascular expression is increased in arteries from angiotensin II hypertensive rats | Rattus norvegicus | - |
vascular smooth muscle cell | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
guanosine 3',5'-cyclic phosphate + H2O | - |
Rattus norvegicus | guanosine 5'-phosphate | - |
? | |
guanosine 3',5'-cyclic phosphate + H2O | - |
Rattus norvegicus Sprague-Dawley | guanosine 5'-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PDE1 | - |
Rattus norvegicus |
phosphodiesterase 1 | - |
Rattus norvegicus |
Organism | Comment | Expression |
---|---|---|
Rattus norvegicus | angiotensin II is able to increase PDE1 expression in vascular smooth muscle cells | up |
General Information | Comment | Organism |
---|---|---|
malfunction | phosphodiesterase-1 inhibition decreases vascular contraction in arteries from angiotensin II hypertensive, but not control, rats. The inhibition of PDE1 in smooth muscle cells isolated from normal aorta or from atherosclerotic lesions results in suppression of smooth muscle cell proliferation | Rattus norvegicus |
additional information | three different isoforms of calmodulin-dependent PDE isoforms are reported, PDE1A and PDE1B, which display higher affinity to hydrolyze cGMP compared to cAMP, and PDE1C, which has a similar ability to hydrolyze cGMP and cAMP | Rattus norvegicus |
physiological function | when Ca2 is high, PDE1 is activated, resulting in lower levels of cGMP, which theoretically facilitates the smooth muscle cell contraction | Rattus norvegicus |