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Construction of a soluble human GH-receptor/EGF-receptor hybrid and its activation by GH

Journal article
Authors Gunnel Hellgren
Chatarina Löfqvist
Kerstin Albertsson-Wikland
Björn Carlsson
Lena M S Carlsson
Published in Cytokine
Volume 25
Issue 6
Pages 260-4
Publication year 2004
Published at Institute for the Health of Women and Children, Dept of Paediatrics
Institute of Internal Medicine, Dept of Body Composition and Metabolism
Pages 260-4
Language en
Links file:///U:/EndNoteRefs/PDF_arkiv/Cy...
Subject categories Medical and Health Sciences

Abstract

To develop a cell-free system that can be used to measure cytokine bioactivity we have designed a soluble hybrid molecule consisting of the extracellular domain of the GH-receptor (GHR) and the intracellular domain of the epidermal growth factor receptor (EGFR). A DNA construct encoding this hybrid-receptor was inserted into a baculoviral expression vector and expressed in Sf9-cells. Activation of the hybrid-receptor by ligand-induced dimerization can be measured as the incorporation of radiolabeled phosphate into a biotinylated tyrosine kinase peptide substrate. The kinase activity in samples stimulated with GH (10 ng/ml) increased 5-fold compared to samples without addition of GH. This is the first example of a functional hybrid-receptor where the transmembrane domain has been deleted. Our results suggest that such hybrid-receptors may be used for detection of GH and other cytokine-receptor activating substances in biological fluids.

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