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A DNA sequence encoding the signal peptide and extracellular domain of human growth hormone receptor (GH R; aa 1-254) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Human growth hormone receptor (GH R) is a type I membrane protein and is a member of the class I cytokine receptor family. GH R is highly expressed in the liver and in skeletal muscle as well as in the kidney, bladder, adrenal gland, brain, bone, cartilage, lung and stomach. Activation of GH R by GH regulates an extensive variety of physiological functions relating to human growth and metabolism. Specifically, binding of GH to GH R promotes the growth of bone, cartilage, and soft tissues, which occurs maximally during puberty. GH R activation also enhances the levels of hormones and neurotransmitters in the CNS, including IGF-1 and somatostatin. GH R is synthesized as a 620 amino acid glycoprotein comprising an 18 amino acid signal peptide, a 246 amino acid single extra cellular domain (ECD), a 24 amino acid transmembrane region and a 350 amino acid cytoplasmic domain. In addition to the membrane bound form, a soluble GH R comprising the ECD has been identified in human plasma that binds GH and may act as a modulator/inhibitor of GH signaling. The GH R extracellular domain has 6 potential N-linked glycosylation sites and glycosylation at three of these sites have been shown to be necessary for maintenance of a high affinity GH binding site and for GH internalization. For further information GH R signal transduction please refer to Strous et al., (2004) Curr Top Microbiol Immunol 286:81-118.