Kinetic Study of the Processing by Dipeptidyl-peptidase IV/CD26 of Neuropeptides Involved in Pancreatic Insulin Secretion

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2001 Nov 7

PMID 11696365

Citations 23

Authors

A M Lambeir

C Durinx

P Proost

J Van Damme

S Scharpe

I De Meester

Affiliations

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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.

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