Prolylcarboxypeptidase (PRCP)

Prolylcarboxypeptidase (PRCP) is a membrane-associated serine exopeptidase of the peptidase S28 family, highly expressed in endothelial cells. PRCP catalyzes the removal of C-terminal amino acids linked to proline from peptides such as angiotensin II, angiotensin III, and des-Arg9-bradykinin, primarily in lysosomes at acidic pH, but with some activity at neutral pH. This regulatory enzyme plays key roles in vascular homeostasis by modulating blood pressure and electrolyte balance through processing of vasoactive peptides, and it activates plasma prekallikrein when associated with high–molecular weight kininogen. PRCP influences angiogenesis, vascular repair, and endothelial function and is implicated in several diseases such as essential hypertension, stroke, renal disease, and metabolic disorders. Genetic variability in PRCP may affect disease susceptibility and therapeutic responses, making it an emerging drug target

Other names

Lysosomal Pro-X carboxypeptidaseAngiotensinase CLysosomal carboxypeptidase CProline carboxypeptidasePCPHUMPCP

Drugs/inhibitors may act by blocking PRCP’s serine protease activity, preventing cleavage of vasoactive peptides (e.g., angiotensin II), thereby influencing blood pressure, inflammation, and metabolic outcomes