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Wiley, FEBS Letters, 3(507), p. 327-330, 2001

DOI: 10.1016/s0014-5793(01)02982-9

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Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion

Journal article published in 2001 by Anne-Marie Lambeir ORCID, Christine Durinx, Paul Proost, Jo Van Damme, van Johan Damme, Simon Scharpé, Ingrid De Meester, De Ingrid Meester
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.