| Autor: |
Michael J. Waters, Steven A. Spencer, William I. Wood, R. Glenn Hammonds, Paul J. Godowski, David W. Leung |
| Rok vydání: |
1990 |
| Předmět: |
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| Popis: |
Publisher Summary The purification and cloning of the growth hormone (GH) receptor and the binding protein have contributed to our understanding of hormonally controlled growth in mammals. This chapter discusses the purification and cloning of growth hormone receptor and binding protein. The GH and prolactin receptors constitute a new family of signaling proteins with a single transmembrane domain. The ability of GH to promote whole-body growth has been demonstrated clinically in the treatment of GH-deficient children and in animals. The lack of easily demonstrated GH effects in cell-based assay systems has led to the somatomedin hypothesis according to which GH produced by the pituitary acts on the liver to induce synthesis and secretion into the circulation of insulin-like growth factor I (IGF-I), which is responsible for skeletal and tissue growth. The availability of the cloned receptors allows elucidation of the intracellular signaling mechanism for these hormones. In situ hybridization work suggests that the GH receptor is widely distributed on many tissues, although it is most abundant in the liver. This wide distribution suggests that direct actions of GH could play a role in the growth process instead of the indirect action suggested by the somatomedin hypothesis. The availability of the GH receptor expressed by recombinant DNA techniques have been useful in determining the amino acids in GH required for binding to the receptor. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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