Proprotein convertase enzyme (PC)

Proprotein convertase enzymes are a family of calcium-dependent serine proteases responsible for the limited proteolysis of precursor proteins, leading to their functional activation or inactivation. They play critical roles in the maturation of peptide hormones, neuropeptides, growth factors, and receptors, modulating fundamental processes such as development, metabolism, immunity, and cell signaling. Nine main mammalian proprotein convertases have been described, encoded by genes PCSK1 through PCSK9. Dysregulation of these enzymes has been implicated in diverse pathologies, including cancer progression, metabolic syndrome, cardiovascular disease, neurodegeneration, and infectious diseases. Therapeutic targeting of individual proprotein convertases is an area of active research, particularly for cancer, hypercholesterolemia (PCSK9), and viral infections (Furin). Because of their central role in proteolytic processing of many substrates, broad inhibition carries significant risks for off-target physiological effects.

Other names

Proprotein convertaseProhormone convertasePCPC1/3PC2FurinPACE4PC4PC5/6PC7SKI-1/S1PPCSK9

Inhibition of substrate cleavage, thereby preventing activation of downstream proteins (e.g., hormone precursors, viral envelope proteins); Immunomodulation via altered processing of immune-related peptides and receptors.