Metabolic stability, receptor binding, cAMP generation, insulin secretion and antihyperglycaemic activity of novel N-terminal Glu9-substituted analogues of glucagon-like peptide-1

Biol Chem. 2003 Dec;384(12):1543-51. doi: 10.1515/BC.2003.171.

Abstract

Glucagon-like peptide-1(7-36)amide (GLP-1) is an incretin hormone with therapeutic potential for type 2 diabetes. Rapid removal of the N-terminal dipeptide, His7-Ala8, by the ubiquitous enzyme dipeptidyl peptidase IV (DPP IV) curtails the biological activity of GLP-1. Chemical modifications or substitutions of GLP-1 at His7 or Ala8 improve resistance to DPP-IV action, but this often reduces potency. Little attention has focused on the metabolic stability and functional activity of GLP-1 analogues with amino acid substitution at Glu9, adjacent to the DPP IV cleavage site. We generated three novel Glu9-substituted GLP-1 analogues, (Pro9)GLP-1, (Phe9)GLP-1 and (Tyr9)GLP-1 and show for the first time that Glu9 of GLP-1 is important in DPP IV degradation, since replacing this amino acid, particularly with proline, substantially reduced susceptibility to degradation. All three novel GLP-1 analogues showed similar or slightly enhanced insulinotropic activity compared with native GLP-1 despite a moderate 4-10-fold reduction in receptor binding and cAMP generation. In addition, (Pro9)GLP-1 showed significant ability to moderate the plasma glucose excursion and increase circulating insulin concentrations in severely insulin resistant obese diabetic (ob/ob) mice. These observations indicate the importance of Glu9 for the biological activity of GLP-1 and susceptibility to DPP IV-mediated degradation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Deaminase / metabolism
  • Amino Acid Substitution
  • Animals
  • Binding, Competitive
  • Blood Glucose / drug effects
  • Blood Glucose / metabolism
  • Cell Line, Tumor
  • Cricetinae
  • Cyclic AMP / metabolism*
  • Diabetes Mellitus, Type 2 / drug therapy
  • Diabetes Mellitus, Type 2 / metabolism
  • Dipeptidyl Peptidase 4*
  • Fibroblasts / metabolism
  • Glucagon / genetics
  • Glucagon / metabolism*
  • Glucagon / pharmacology
  • Glucagon-Like Peptide 1
  • Glucagon-Like Peptide-1 Receptor
  • Glucose / pharmacology
  • Glutamine / chemistry
  • Glycoproteins / metabolism
  • Humans
  • Hypoglycemic Agents / metabolism*
  • Hypoglycemic Agents / pharmacology
  • Insulin / blood
  • Insulin / metabolism*
  • Insulin Secretion
  • Islets of Langerhans / drug effects
  • Islets of Langerhans / metabolism
  • Mice
  • Mice, Obese
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism*
  • Peptide Fragments / pharmacology
  • Phenylalanine / chemistry
  • Proline / chemistry
  • Protein Precursors / genetics
  • Protein Precursors / metabolism*
  • Protein Precursors / pharmacology
  • Rats
  • Receptors, Glucagon / metabolism
  • Spectrometry, Mass, Electrospray Ionization
  • Transformation, Genetic
  • Tyrosine / chemistry

Substances

  • Blood Glucose
  • GLP1R protein, human
  • Glp1r protein, mouse
  • Glp1r protein, rat
  • Glucagon-Like Peptide-1 Receptor
  • Glycoproteins
  • Hypoglycemic Agents
  • Insulin
  • Peptide Fragments
  • Protein Precursors
  • Receptors, Glucagon
  • Glutamine
  • Tyrosine
  • Phenylalanine
  • Glucagon-Like Peptide 1
  • Glucagon
  • Proline
  • Cyclic AMP
  • DPP4 protein, human
  • Dipeptidyl Peptidase 4
  • Adenosine Deaminase
  • Glucose