3′,5′-cyclic-nucleotide phosphodiesterase (PDE (or sometimes PDE1–PDE11 for specific isoforms))

3′,5′-cyclic-nucleotide phosphodiesterase is the canonical name for a family of enzymes (EC 3.1.4.17) collectively known as phosphodiesterases (PDEs), which catalyze the hydrolysis of 3′,5′-cyclic nucleotides such as cAMP and cGMP into their non-cyclic 5′-monophosphate forms[1][3][5][7]. These enzymes are key regulators of cellular concentrations of second messengers cAMP and cGMP, thus critically controlling the amplitude and duration of intracellular signaling triggered by a variety of extracellular signals, including hormones, neurotransmitters, and sensory stimuli[5][8]. There are 11 characterized mammalian PDE subfamilies, each with distinct tissue distribution, regulatory mechanisms, and inhibitor sensitivities[1][7]. PDEs are important therapeutic targets for multiple diseases, with several approved and investigational drugs acting as isoform-selective inhibitors[2][4][6][8]. Dysregulation of PDE function or expression is implicated in a wide range of clinical conditions, including heart failure, erectile dysfunction, pulmonary hypertension, neurodegeneration, and inflammatory diseases[2][4][6].

Other names

3′,5′-cyclic nucleotide phosphodiesterasePDEcyclic 3′,5′-mononucleotide phosphodiesterasecyclic 3′,5′-nucleotide phosphodiesterasecyclic 3′,5′-phosphodiesterase3′,5′-nucleotide phosphodiesterase3':5'-cyclic nucleotide 5′-nucleotidohydrolase3′,5′-cyclonucleotide phosphodiesterase3′,5′-cyclic nucleoside monophosphate phosphodiesterasenucleoside 3′,5′-cyclic phosphate diesterase3′,5′-cyclic-nucleotide 5'-nucleotidohydrolase

Inhibition of phosphodiesterase activity increases cAMP and/or cGMP levels, amplifying effects of associated signaling pathways (e.g., vasodilation, anti-inflammatory effects)[2][4][6][8]. Selective inhibition of specific PDE isoforms modulates particular physiological responses (e.g., PDE5 inhibition leads to smooth muscle relaxation in erectile tissue).