Endocrine Abstracts

Introduction: The growth hormone receptor (GHR) consists of 620 residues and belongs to the class I cytokine receptor family. It is a single membrane spanning protein that binds its ligand, GH, via the extracellular domain. GH binding to GHR induces a conformational change in the preformed receptor dimer, which leads to intracellular signalling. Correct functional dimerisation of two GHR molecules is essential for GH signalling. We have previously shown that membrane bound tru...

We have previously demonstrated that a truncated GHR lacking the cytoplasmic domain of the receptor acts as a dominant negative regulator of receptor signalling. Glycosylphosphatidylinositol (GPI) anchors are a common mechanism by which cells direct and anchor proteins in the cell membrane. We have generated a GHR extracellular domain-GPI fusion protein and tested its biological activity as a receptor antagonist. The extracellular domain of GHR (growth hormone binding protein-...

Introduction: We have generated a truncated Growth Hormone Receptor (GHR) fused to the cell membrane by a glycosyl phosphatidylinositol anchor (GHR-GPI). The protein consists of the complete extracellular domain of the GHR, but lacks the intracellular domain, and we predict it would act as a GH antagonist. Aim: To test if partially-purified soluble GHR-GPI could re-insert into CHO cell membranes. Material and methods: Membrane preparations were made from CHO cells stably expre...