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Development of a cysteine-deprived and C-terminally truncated GLP-1 receptor

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Authors:
  • Underwood, Christina Rye ;
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    Department of Chemistry, Technical University of Denmark
  • Knudsen, Lotte Bjerre ;
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    Novo Nordisk A/S
  • Garibay, Patrick W. ;
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    Novo Nordisk A/S
  • Peters, Günther H.J. ;
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    Orcid logo0000-0001-9754-2663
    Department of Chemistry, Technical University of Denmark
  • Reedtz-Runge, Steffen
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    Novo Nordisk A/S
DOI:
10.1016/j.peptides.2013.09.001
Abstract:
The glucagon-like peptide-1 receptor (GLP-1R) belongs to family B of the G-protein coupled receptors (GPCRs), and has become a promising target for the treatment of type 2 diabetes. Here we describe the development and characterization of a fully functional cysteine-deprived and C-terminally truncated GLP-1R. Single cysteines were initially substituted with alanine, and functionally redundant cysteines were subsequently changed simultaneously. Our results indicate that Cys174, Cys226, Cys296 and Cys403 are important for the GLP-1-mediated response, whereas Cys236, Cys329, Cys341, Cys347, Cys438, Cys458 and Cys462 are not. Extensive deletions were made in the C-terminal tail of GLP-1R in order to determine the limit for truncation. As for other family B GPCRs, we observed a direct correlation between the length of the C-terminal tail and specific binding of 125I-GLP-1, indicating that the membrane proximal part of the C-terminal is involved in receptor expression at the cell surface. The results show that seven cysteines and more than half of the C-terminal tail can be removed from GLP-1R without compromising GLP-1 binding or function.
Type:
Journal article
Language:
English
Published in:
Peptides, 2013, Vol 49, p. 100-108
Keywords:
G-protein coupled receptor; Glucagon-like peptide-1; Agonist; Cysteine; Mutagenesis
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2013
Scientific Level:
Scientific
ID:
254757160

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