Recombinant human PDE1B protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PDE1B also known as phosphodiesterase 1B is an enzyme that importantly regulates intracellular levels of cyclic nucleotides by hydrolyzing cAMP and cGMP. With a molecular mass of approximately 66 kDa PDE1B shows a widespread tissue distribution with significant expression in the brain heart and vascular smooth muscle. The enzyme functions as a calmodulin-dependent phosphodiesterase activating in the presence of calcium levels above basal.

Biological function summary

PDE1B plays an essential role in the signaling pathways that rely on cyclic nucleotides as second messengers. It regulates calcium-mediated signal transduction affecting activities of cells such as neurons and cardiac cells. While PDE1B primarily functions as a homodimer its activity interfaces with several other cellular processes through its regulation of cyclic nucleotide concentrations modulating downstream effects.

Pathways

PDE1B acts mainly in the cAMP and cGMP signaling pathways both of which are important for cellular responses to external stimuli. It modulates the degradation of these second messengers influencing associated proteins like protein kinase A (PKA) and protein kinase G (PKG). By controlling the half-life of cAMP and cGMP PDE1B plays an important role in signal cascades that govern processes such as learning memory and blood vessel relaxation.

PDE1B has associations with neurological and cardiovascular diseases. Abnormal expression of PDE1B can contribute to conditions such as schizophrenia and hypertension. Through its involvement in cyclic nucleotide signaling PDE1B is connected to proteins like D2 dopamine receptor in schizophrenia and angiotensin II receptors in hypertension where dysregulated signaling can impact disease progression and response to treatment.