A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro

被引：28

作者：

Lambeir, AM

Proost, P

Scharpé, S

De Meester, I

机构：

[1] Univ Instelling Antwerp, Med Biochem Lab, Dept Pharmaceut Sci, B-2610 Antwerp, Belgium

[2] Katholieke Univ Leuven, Rega Inst Med Res, Lab Mol Immunol, B-3000 Louvain, Belgium

来源：

BIOCHEMICAL PHARMACOLOGY | 2002年 / 64卷 / 12期

关键词：

glucagon-like peptides; GLP-1; GLP-2; incretins; dipeptidyl peptidase IV; CD26;

D O I：

10.1016/S0006-2952(02)01415-6

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

In vivo inactivation of glucagon-like peptide-1 (GLP-1) and glucagon-like peptide-2 (GLP-2) was found to be associated with the proteolytic removal of their N-terminal dipeptide by the ectopeptidase dipeptidyl peptidase TV (DPP IV). Previous studies suggested that the in vivo metabolism of GLP-1 is much faster than that of GLP-2. In this paper, we investigated the in vitro truncation of GLP-2 and GLP-1 by DPP IV. The slower conversion rate observed for GLP-2 compared to GLP-1 was due to an approximately 10-fold reduction in catalytic rate constant. The selectivity of DPP IV for the glucagon-like peptides was compared with data obtained for other natural substrates using the same enzyme source in identical conditions. (C) 2002 Elsevier Science Inc. All rights reserved.

引用

页码：1753 / 1756

页数：4

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