Dipeptidyl peptidase 3 (DPP3)

Dipeptidyl peptidase 3 is a **zinc-dependent cytoplasmic metalloaminopeptidase** that specifically hydrolyzes dipeptides from the N-terminus of peptides that are typically 4-10 amino acids in length. It plays a critical role in the degradation of several physiologically active peptides, such as angiotensins and opioid peptides (enkephalins, endomorphins), influencing processes including blood pressure regulation, pain signal modulation, protein turnover, and cellular oxidative stress response. DPP3 is a key modulator of the renin-angiotensin system, cell protection pathways (e.g., Keap1-Nrf2), and is implicated in cardiovascular, oncological, and inflammatory diseases. DPP3 is considered both a biomarker and a potential therapeutic target, with current research aiming to develop specific inhibitors and evaluate their physiological effects[1][2][4][6][8].

Other names

DPP IIIDipeptidyl peptidase IIIDipeptidyl-peptidase 3DPP-3

Inhibition of DPP3 reduces degradation of angiotensin peptides, increasing their levels and thereby modulating the renin-angiotensin system[1][4]. Inhibition can decrease renal blood flow via effects on Angiotensin II and associated pathways[1]. DPP3 modulation affects Keap1-Nrf2 signaling and oxidative stress[4][6].