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Biologic properties and therapeutic potential of glucagon-like peptide-2
D J Drucker1, R P Boushey, F Wang
1Department of Medicine, Banting and Best Diabetes Centre, The Toronto Hospital, University of Toronto, Canada.
Background:
Glucagon-like peptide-2 (GLP-2), a 33 amino acid, proglucagon-derived peptide with intestinotrophic activity, is secreted from enteroendocrine cells in the small and large intestine.
Methods:
This review describes recent advances in our understanding of GLP-2 physiology from rodent experiments in vivo.
Results:
GLP-2 administration induces mucosal epithelial proliferation in small and large bowel and stomach. GLP-2 is rapidly degraded by the enzyme dipeptidyl peptidase IV (DPP-IV) to produce the biologically inactive form GLP-2(3-33), however, GLP-2 analogs that confer resistance to DPP-IV exhibit enhanced biologic activity in vivo. GLP-2-treated bowel retains normal to enhanced functional absorptive capacity. Furthermore, GLP-2 infusion prevents total parenteral nutrition (TPN)-associated intestinal hypoplasia, and enhances bowel adaptation and nutrient absorption in rats following small bowel resection. GLP-2 also reverses weight loss and improves histologic and biochemical parameters of disease activity in mice with experimental colitis.
Conclusions:
GLP-2 is an intestine-derived peptide with intestinotrophic properties that may be therapeutically useful in diseases characterized by intestinal damage or insufficiency.