Dipeptidyl peptidase-4 family (DPP4 family) (DPP4 family)

The Dipeptidyl peptidase-4 (DPP4) family consists of serine proteases, including DPP4, fibroblast activation protein (FAP), DPP8, and DPP9, which play critical roles in regulating various physiological processes through the cleavage of N-terminal dipeptides (PMID: 29334305). DPP4, also known as CD26, is the most prominent member and serves as a key regulator of glucose metabolism by degrading incretin hormones like GLP-1 and GIP (UniProt P27487). In the context of Type 2 diabetes, DPP4 inhibitors are widely used to prolong the half-life of these incretins, thereby improving glycemic control (StatPearls: Dipeptidyl Peptidase 4 Inhibitors). Beyond metabolic regulation, members of this family are involved in immune system modulation, cell signaling, and tumor biology, with FAP being a significant target in cancer research due to its expression in the tumor microenvironment (PMID: 16505345). While highly effective for diabetes management, therapeutic development must ensure selectivity to avoid the potential toxicities associated with the inhibition of intracellular family members like DPP8 and DPP9 (PMID: 15713750). Overall, the DPP4 family represents a versatile group of enzymes with significant implications in metabolic, immunological, and oncological therapeutic strategies.

Other names

DPP-IV familyS9B family of serine peptidasesCD26 familyDipeptidyl peptidase IV-like proteins

Inhibition of the DPP4 enzyme prevents the proteolytic degradation of incretin hormones, such as glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which enhances glucose-dependent insulin secretion and suppresses glucagon release (StatPearls: Dipeptidyl Peptidase 4 Inhibitors; PMID: 16505345).