Dipeptidyl peptidase 4 (DPP-4) (DPP-4)

Dipeptidyl peptidase 4 (DPP-4), also known as CD26, is a multifunctional type II transmembrane glycoprotein that acts as both a serine exopeptidase and a T-cell costimulatory molecule [6, 12, 14]. It is widely expressed across various tissues, including the vascular endothelium, renal tubules, and immune cells [12, 14]. Its primary metabolic role is the rapid degradation of incretin hormones, such as glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which are essential for glucose-dependent insulin secretion [7, 9, 12]. In the immune system, CD26 interacts with adenosine deaminase (ADA) and caveolin-1 to modulate T-cell activation and inflammatory responses [6, 9, 12]. Pharmacological inhibition of DPP-4 is a well-established therapeutic strategy for managing type 2 diabetes, as it extends the half-life of endogenous incretins to improve glycemic control with a low risk of hypoglycemia [4, 11, 13, 15]. Beyond diabetes, DPP-4 is implicated in various cancers, cardiovascular diseases, and viral infections, making it a target of interest for broader clinical applications [3, 8, 11, 14].

Other names

CD26T-cell activation antigen CD26Adenosine deaminase complexing protein 2ADCP2Dipeptidyl peptidase IVDPPIVEC 3.4.14.5

Dipeptidyl peptidase 4 inhibition