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Identifying neuropeptide Y (NPY) as the main stress-related substrate of dipeptidyl peptidase 4 (DPP4) in blood circulation

: Wagner, L.; Kaestner, F.; Wolf, R.; Stiller, H.; Heiser, U.; Manhart, S.; Hoffmann, T.; Rahfeld, J.-U.; Demuth, H.-U.; Rothermundt, M.; Hörsten, S. von


Neuropeptides 57 (2016), S.21-34
ISSN: 0143-4179 (print)
ISSN: 1532-2785 (online)
Fraunhofer IZI ()

Background: Dipeptidyl peptidase 4 (DPP4; EC; CD26) is a membrane-bound or shedded serine protease that hydrolyzes dipeptides from the N-terminus of peptides with either proline or alanine at the penultimate position. Substrates of DPP4 include several stress-related neuropeptides implicated in anxiety, depression and schizophrenia. A decline of DPP4-like activity has been reported in sera from depressed patient, but not fully characterized regarding DPP4-like enzymes, therapeutic interventions and protein. Methods: Sera from 16 melancholic- and 16 non-melancholic-depressed patients were evaluated for DPP4-like activities and the concentration of soluble DPP4 protein before and after treatment by anti-depressive therapies. Post-translational modification of DPP4-isoforms and degradation of NPY, Peptide YY (PYY), Galanin-like peptide (GALP), Orexin B (OrxB), OrxA, pituitary adenylate cyclase-activating polypeptide (PACAP) and substance P (SP) were studied in serum and in ex vivo human blood.