PDE1C
PDE1C (phosphodiesterase 1C, also known as Hcam3) is a calmodulin-dependent cyclic nucleotide phosphodiesterase that hydrolyses the second messengers cAMP and cGMP. It helps control smooth muscle cell proliferation, sensory signalling and growth factor receptor stability. Browse Assay Genie's current range of PDE1C research reagents below, or read on for the biology behind the target.
PDE1C is a calmodulin-dependent cyclic nucleotide phosphodiesterase with dual specificity for the second messengers cAMP and cGMP, and it has a high affinity for both. Like other members of the 3',5'-cyclic nucleotide phosphodiesterase family, it catalyses the hydrolysis of these cyclic nucleotides to the corresponding nucleoside 5'-monophosphates. In this way it shapes the amplitude and duration of cyclic nucleotide signals, which regulate many physiological processes.
In sensory cilia, PDE1C modulates the cAMP signal in response to odorant stimulation, contributing to the generation of action potentials. In kidney juxtaglomerular granular cells it inhibits renin release by decreasing cAMP levels. It also regulates smooth muscle cell proliferation, and the enzyme is described as regulating the proliferation and migration of vascular smooth muscle cells and neointimal hyperplasia.
PDE1C also regulates the stability of growth factor receptors, including PDGFRB (PDGF-receptor-beta), and through this it plays a role in pathological vascular remodelling. UniProt lists its subcellular location as the lysosome. The protein belongs to the cyclic nucleotide phosphodiesterase family, PDE1 subfamily, and HGNC places the PDE1C gene in the phosphodiesterases group. Earlier names include phosphodiesterase 1C, calmodulin-dependent (70kD), and the alias Hcam3. Mouse and rat both have a Pde1c ortholog.
PDE1C hydrolyses both cAMP and cGMP with high affinity, making it a useful enzyme for studying how second messenger signals are shaped and terminated.
PDE1C regulates vascular smooth muscle cell proliferation and migration, and neointimal hyperplasia, linking it to studies of vascular remodelling.
PDE1C regulates the stability of growth factor receptors such as PDGFRB, which is relevant to pathological vascular remodelling.
PDE1C modulates cAMP signals in olfactory cilia and inhibits renin release from kidney juxtaglomerular granular cells.
PDE1C is a calmodulin-dependent phosphodiesterase that hydrolyses both cAMP and cGMP. It modulates cAMP signalling in sensory cilia, regulates smooth muscle cell proliferation, controls the stability of growth factor receptors including PDGFRB, and inhibits renin release in juxtaglomerular granular cells.
The HGNC name is phosphodiesterase 1C, and the alias Hcam3 is also used. Earlier names were phosphodiesterase 1C, calmodulin-dependent (70kD) and its 70kDa variant. UniProt names it dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C, EC 3.1.4.17.
Yes. Both mouse and rat have an ortholog named Pde1c, so the human protein can be studied in rodent models. Check the datasheet of any product for its validated reactivity. PDE1C belongs to the PDE1 subfamily, alongside PDE1A and PDE1B.
Other phosphodiesterases, including the PDE1 subfamily, and related cyclic nucleotide signalling enzymes.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14123; product specifications from Assay Genie datasheets.