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
收藏
页码：1753 / 1756
页数：4
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