Cyclic GMP-specific 3',5'-cyclic phosphodiesterase (PDE5) (PDE5)

Cyclic GMP-specific 3',5'-cyclic phosphodiesterase, commonly known as PDE5, is an enzyme responsible for the degradation of cyclic guanosine monophosphate (cGMP) in various tissues, particularly in the smooth muscle of the corpus cavernosum and pulmonary vasculature [1, 2]. By hydrolyzing cGMP into 5'-GMP, PDE5 regulates the duration and intensity of the signaling pathway initiated by nitric oxide [2, 4]. In clinical practice, PDE5 is a major therapeutic target for conditions characterized by impaired vasodilation [2]. Inhibition of this enzyme leads to increased intracellular cGMP levels, which promotes protein kinase G activation and subsequent smooth muscle relaxation [3, 4]. This mechanism is the primary basis for treating erectile dysfunction and pulmonary arterial hypertension [2, 3]. Beyond these indications, PDE5 inhibitors are also utilized for benign prostatic hyperplasia and are being investigated for potential roles in cardioprotection and neurodegeneration [2, 4].

Other names

PDE5APhosphodiesterase 5cGMP-specific phosphodiesterase type 5PDE5A1PDE5A2PDE5A3

Competitive inhibition of the PDE5 enzyme, preventing the hydrolysis of cGMP to 5'-GMP, thereby prolonging the effects of nitric oxide-mediated smooth muscle relaxation [2, 3].