Journal
FEBS LETTERS
Volume 507, Issue 3, Pages 327-330Publisher
WILEY
DOI: 10.1016/S0014-5793(01)02982-9
Keywords
dipeptidyl-peptidase IV; CD26; gastrin-releasing peptide; neuropeptide Y; vasoactive intestinal peptide; pituitary adenylyl cyclase-activating peptide
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Dipeptidyl-peptidase IV (DPPIV/CD26) metabolizes neuropeptides regulating insulin secretion. We studied the in vitro steady-state kinetics of DPPIV/CD26-mediated truncation of vasoactive intestinal peptide (VIP), pituitary adenylyl cyclase-activating peptide (PACAP27 and PACAP38), gastrin-releasing peptide (GRP) and neuropeptide Y (NPY). DPPIV/CD26 sequentially cleaves off two dipeptides of VIP, PACAP27, PACAP38 and GRP. GRP situates between the best DPPIV/CD26 substrates reported, comparable to NPY. Surprisingly, the C-terminal extension of PACAP38, distant from the scissile bond, improves both PACAP38 binding and turnover. Therefore, residues remote from the scissile bond can modulate DPPIV/CD26 substrate selectivity as well as residues flanking it. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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