| Title : Kinetic study of the processing by dipeptidyl-peptidase IV\/CD26 of neuropeptides involved in pancreatic insulin secretion - Lambeir_2001_FEBS.Lett_507_327 |
| Author(s) : Lambeir AM , Durinx C , Proost P , Van Damme J , Scharpe S , De Meester I |
| Ref : FEBS Letters , 507 :327 , 2001 |
|
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. |
| PubMedSearch : Lambeir_2001_FEBS.Lett_507_327 |
| PubMedID: 11696365 |
Lambeir AM, Durinx C, Proost P, Van Damme J, Scharpe S, De Meester I (2001)
Kinetic study of the processing by dipeptidyl-peptidase IV\/CD26 of neuropeptides involved in pancreatic insulin secretion
FEBS Letters
507 :327
Lambeir AM, Durinx C, Proost P, Van Damme J, Scharpe S, De Meester I (2001)
FEBS Letters
507 :327