Functional characterization of N-terminally GFP-tagged GLP-1 receptor

J Biomed Biotechnol. 2009:2009:498149. doi: 10.1155/2009/498149. Epub 2009 Oct 22.

Abstract

The glucagon-like peptide-1 receptor (GLP-1 receptor) mediates important effects on peripheral tissues and the central nervous system. It seems one of the most promising therapeutic targets for treatment of diabetes mellitus type 2. Surprisingly, very little is known about the cellular mechanisms that regulate its function in vivo. One of the approaches to study receptor dynamics, expression, or signaling is using GFP-tagged fluorescent proteins. In this study, we synthesized and characterized N-terminally GFP-tagged GLP-1 (GFP-GLP-1) receptor in CHO cells. We demonstrated that GFP-GLP-1 receptor is weakly expressed in the plasma membranes and is functionally coupled to adenylyl cyclase via heterotrimeric G-proteins, similarly as its wild type.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • CHO Cells
  • Cell Line
  • Cell Membrane / metabolism
  • Cricetinae
  • Cricetulus
  • Cyclic AMP / biosynthesis
  • Gene Expression
  • Glucagon-Like Peptide-1 Receptor
  • Green Fluorescent Proteins / chemistry
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
  • Heterotrimeric GTP-Binding Proteins / metabolism
  • Humans
  • Insulin / metabolism
  • Insulin Secretion
  • Molecular Sequence Data
  • Rats
  • Receptors, Glucagon / chemistry*
  • Receptors, Glucagon / genetics
  • Receptors, Glucagon / metabolism*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism

Substances

  • GLP1R protein, human
  • Glp1r protein, rat
  • Glucagon-Like Peptide-1 Receptor
  • Insulin
  • Receptors, Glucagon
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Cyclic AMP
  • Heterotrimeric GTP-Binding Proteins
  • Adenylyl Cyclases