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  • Title: The isolated N-terminal extracellular domain of the glucagon-like peptide-1 (GLP)-1 receptor has intrinsic binding activity.
    Author: Wilmen A, Göke B, Göke R.
    Journal: FEBS Lett; 1996 Nov 25; 398(1):43-7. PubMed ID: 8946950.
    Abstract:
    The glucagon-like peptide 1 (7-37)/(7-36) amide (GLP-1) receptor belongs to a new subclass of seven transmembrane domain, G-protein coupled receptors comprising several receptors for peptide hormones. The receptors of this family share many common motifs including a relatively large N-terminal extracellular domain. The GLP-1 receptor is presently attracting much attention, since it is the target protein of the antidiabetic gut hormone GLP-1. To establish the functional significance of the N-terminal part of the GLP-1 receptor for ligand binding, the extracellular domain was isolated and purified. Utilizing CHL cells expressing the cloned GLP-1 receptor, we demonstrate that the isolated, solubilized N-terminal part of the receptor protein competes for GLP-1 binding with the intact wild-type receptor. Moreover, in cross-linking experiments radiolabeled GLP-1 was covalently attached to the isolated N-terminus, thereby demonstrating direct physical interaction of both components. By Western blot analysis two specific bands were detectable, representing the N-terminal receptor protein in the presence or absence of bound ligand. These data underline the significance of the N-terminal domain of the GLP-1 receptor for ligand binding.
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