Dipeptidyl peptidase-4 expression is reduced in Crohn's disease

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Background: Dipeptidyl peptidase 4 (DP4) is a serine protease that preferentially cleaves N-terminal dipeptides from polypeptides containing proline or alanine as the penultimate amino acid. DP4 inactivates glucagon like peptide-2 (GLP-2), a trophic peptide with cytoprotective and reparative properties in the injured gut; therefore DP4 potentially inhibits repair processes. DP4 also modulates the activity of GLP-1 and polypeptide YY (PYY) which regulate appetite and motility. No data are yet available on the tissue and plasma expression of DP4 in inflammatory bowel disease (IBD). Methods: Tissue and plasma were studied from active CD and healthy controls for DP4 quantification. Experiments were also carried out in a reductionist Caco-2 cell line model of intestinal inflammation with TNFα incubation. DP4 expression was studied by tissue Western blotting and plasma enzymelinked immunosorbent assay (ELISA), in addition to quantitative polymerase chain reaction (qPCR). Results: There was a ~. 2.7-fold decrease in DP4 protein in CD tissue (p=0.05). Plasma DP4 in CD was also significantly lower than the control group. A negative correlation between plasma DP4 levels and inflammatory activity as measured by C-reactive protein was observed. In Caco-2 cells an ~. 18-fold increase (p

Bibliographical metadata

Original languageEnglish
Pages (from-to)40-45
Number of pages5
JournalRegulatory Peptides
Issue number1-3
Publication statusPublished - 20 Aug 2012