cGMP-specific phosphodiesterase (PDE (with specific isoforms such as PDE5, PDE6, and PDE9 being cGMP-specific))

cGMP-specific phosphodiesterase is an enzyme responsible for hydrolyzing cyclic guanosine monophosphate (cGMP) to 5’-GMP, thus controlling cellular cGMP levels and modulating several physiological processes[1][3][4][10]. Multiple isoforms exist—most notably PDE5 (predominant in smooth muscle, key to vascular tone regulation and drug target for erectile dysfunction and pulmonary hypertension) and PDE6 (critical for phototransduction in retinal photoreceptors)[7][10]. Inhibition of cGMP-phosphodiesterases increases intracellular cGMP, promoting smooth muscle relaxation, vasodilation, and signaling effects that are used therapeutically in cardiovascular, genitourinary, and some neurodegenerative disorders[3][2][8]. The family is recognized as a major therapeutic and research target due to its central role in second messenger signaling and disease[8][9].

Other names

cGMP phosphodiesterasecGMP-PDE3',5'-cyclic-GMP phosphodiesterasePhosphodiesterase type 5 (PDE5)Phosphodiesterase type 6 (PDE6)Phosphodiesterase type 9 (PDE9)

Inhibition leads to increased intracellular cGMP, resulting in smooth muscle relaxation, vasodilation, and modulation of signal transduction pathways[2][3][4].\nPhotoreceptor PDE (PDE6) hydrolyzes cGMP in response to light, leading to hyperpolarization of photoreceptors during visual signaling[10][7].