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

Biochem Pharmacol. 2002 Dec 15;64(12):1753-6. doi: 10.1016/s0006-2952(02)01415-6.

Abstract

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 IV (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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Dipeptidyl Peptidase 4 / metabolism*
  • Glucagon / metabolism*
  • Glucagon-Like Peptide 1
  • Glucagon-Like Peptide 2
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Peptide Fragments / metabolism*
  • Peptides / metabolism*
  • Protein Precursors / metabolism*
  • Time Factors

Substances

  • Glucagon-Like Peptide 2
  • Peptide Fragments
  • Peptides
  • Protein Precursors
  • Glucagon-Like Peptide 1
  • Glucagon
  • Dipeptidyl Peptidase 4