What is the Origin of Dipeptidyl Peptidase-IV?

The term is derived from the enzyme's biochemical function, specifically its ability to cleave dipeptides from the N-terminus of a polypeptide chain at the fourth position (Peptidase-IV). Its physiological role in metabolism became a major focus in endocrinology with the discovery and characterization of incretin hormones. The identification of its role paved the way for a new class of anti-diabetic medications.

What is the Mechanism of Dipeptidyl Peptidase-IV?

The enzyme's primary mechanism involves the hydrolytic cleavage of the Ala-Pro or Gly-Pro dipeptide from the active forms of incretins, such as GLP-1 and Glucose-dependent Insulinotropic Polypeptide (GIP). This rapid enzymatic degradation converts the active hormones into inactive metabolites, effectively limiting their half-life and duration of action. Pharmacological inhibitors of DPP-IV are designed to block this cleavage, thereby extending the therapeutic action of endogenous incretins to enhance postprandial insulin release and improve glycemic control.

Dipeptidyl Peptidase-IV ∞ Area

Dipeptidyl Peptidase-IV

Meaning

Dipeptidyl Peptidase-IV (DPP-IV) is a ubiquitous serine protease enzyme found on the surface of various cell types, including endothelial cells and immune cells, and also circulating in the bloodstream as a soluble form. This enzyme plays a significant regulatory role in glucose homeostasis by rapidly inactivating the incretin hormones, such as Glucagon-like Peptide-1 (GLP-1), which are essential for stimulating insulin secretion after a meal. Clinically, the activity of DPP-IV is a key therapeutic target in the management of type 2 diabetes. Its swift action limits the duration of incretin signaling.