Dipeptidyl peptidase IV inhibitors: how do they work as new antidiabetic agents?

Regul Pept. 2005 Jun 15;128(2):159-65. doi: 10.1016/j.regpep.2004.06.001.

Abstract

A number of new approaches to diabetes therapy are currently undergoing clinical trials, including those involving stimulation of the pancreatic beta-cell with the gut-derived insulinotropic hormones (incretins), GIP and GLP-1. The current review focuses on an approach based on the inhibition of dipeptidyl peptidase IV (DP IV), the major enzyme responsible for degrading the incretins in vivo. The rationale for this approach was that blockade of incretin degradation would increase their physiological actions, including the stimulation of insulin secretion and inhibition of gastric emptying. It is now clear that both GIP and GLP-1 also have powerful effects on beta-cell differentation, mitogenesis and survival. By potentiating these pleiotropic actions of the incretins, DP IV inhibition can therefore preserve beta-cell mass and improve secretory function in diabetics.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Diabetes Mellitus, Type 2 / drug therapy*
  • Dipeptidyl Peptidase 4 / metabolism*
  • Gastric Inhibitory Polypeptide / metabolism
  • Glucagon / metabolism
  • Glucagon-Like Peptide 1
  • Humans
  • Hypoglycemic Agents / therapeutic use*
  • Peptide Fragments / metabolism
  • Protease Inhibitors / therapeutic use*
  • Protein Precursors / metabolism

Substances

  • Hypoglycemic Agents
  • Peptide Fragments
  • Protease Inhibitors
  • Protein Precursors
  • Gastric Inhibitory Polypeptide
  • Glucagon-Like Peptide 1
  • Glucagon
  • Dipeptidyl Peptidase 4