Kinetic study of the processing by dipeptidyl-pept...[FEBS Lett. 2001]

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1: FEBS Lett. 2001 Nov 2;507(3):327-30. Links

Erratum in:: FEBS Lett 2002 Feb 13;512(1-3):353.

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

Lambeir AM, Durinx C, Proost P, Van Damme J, Scharpé S, De Meester I.

Laboratory of Medical Biochemistry, University of Antwerp, Belgium. lambeir@uia.ua.ac.be

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.

PMID: 11696365 [PubMed - indexed for MEDLINE]

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