Dipeptidyl peptidase 2 (DPPII)

Dipeptidyl peptidase 2 (DPPII) is an intracellular serine protease that localizes primarily to the vesicular system of cells[1][7]. It releases N-terminal dipeptides from oligopeptides, particularly when Pro or Ala is in the penultimate position, and acts optimally at acidic pH[1][7]. While its precise physiological role is not fully understood, evidence suggests involvement in the regulation of peptide hormone signaling, degradation of collagen fragments, myofibrillar proteins, and short neuropeptides. In addition, its roles are hypothesized to include cell differentiation processes, protection from cell death, and influences in disease-related processes such as cancer and neurodegenerative disorders[1][3]. Unlike DPPIV (DPP4), fewer natural substrates and validated drug interactions are currently known for DPPII, and it has not been as widely targeted therapeutically[1][3]. Note: This target is distinct from Dipeptidyl peptidase 4 (DPP4), the latter being the pharmacological target of gliptin-class antidiabetic drugs. Current knowledge indicates Dipeptidyl peptidase 2 is a real protein/enzyme target, but its therapeutic and biomarker potential is less validated and may shift as more research emerges[1][3][7].

Other names

Dipeptidyl peptidase IIDPPIIDPP2Dipeptidyl aminopeptidase II

Inhibition of enzymatic activity (e.g., by UAMC00039) may induce apoptosis in certain lymphocyte subsets and may modulate peptide signaling