DPP4 is expressed on the membranes of a variety of cell types as well as in soluble form, and cleaves the two N-terminal amino acids, X-ala or X-pro, from a limited number of peptide substrates, usually resulting in their inactivation. A family of DPP4 inhibitors, gliptins, have been shown to preserve the full-length active forms of GLP1 and GIP in patients with type II diabetes, enhancing antihyperglycemic activity. In addition to GLP1 and GIP, important substrates of DPP4 essential for wound healing, and altered in diabetes, include SDF-1α/β (stromal cell derived factor 1), PYY (peptide YY), NPY (neuropeptide Y), GM-CSF (granulocyte macrophage colony stimulating factor), G-CSF (granulocyte colony stimulating factor), and IL3 (interleukin 3) [8-12]. SDF, PYY, and NPY are all important for angiogenesis, while GM-CSF, G-CSF, and IL3 are necessary for leukocyte proliferation and infiltration in the wound bed. The observation that DPP4 can cleave and inactive all of these signaling molecules in vivo suggest that modulation of DPP4 activity will have a direct effect on wound healing.