Title: Somatoliberin
CAS Registry Number: 83930-13-6
CAS Name: Growth hormone-releasing factor
Additional Names: GH-RF; GH-RH; GRF; growth hormone-releasing hormone; hGRF; hpGRF; somatocrinin
Literature References: Stimulatory growth-hormone releasing factor of the hypothalamus that mediates, together with somatostatin, q.v., the neuroregulation of somatotropin secretion. The concept of hypothalamic regulation of growth hormone release was postulated on the basis of physiological and biochemical evidence, cf. A. V. Schally et al., Recent Prog. Horm. Res. 24, 497 (1968); J. B. Martin in Frontiers in Neuroendocrinology, L. Martini, W. F. Ganong, Eds. (Raven Press, New York, 1976) pp 129-168. Demonstration of the existence of a GH-RH: R. Deuben, J. Meites, Endocrinology 74, 408 (1964); A. V. Schally et al., ibid. 82, 271 (1968); E. Dickermann et al., Neuroendocrinology 4, 75 (1969). Isoln of a decapeptide originally believed to be GRF: A. V. Schally et al., Endocrinology 84, 1493 (1969). Review of early literature: eidem, Science 179, 341 (1973). Isoln and characterization of hpGRF, a fully bioactive, 44 amino acid peptide from human pancreatic tumor: R. Guillemin et al., Science 218, 585 (1982); J. Rivier et al., Nature 300, 276 (1982). Cloning and sequence analysis of cDNA for hpGRF precursor: U. Gubler et al., Proc. Natl. Acad. Sci. USA 80, 4311 (1983). Expression-cloning of cDNA for hpGRF: K. E. Mayo et al., Nature 306, 86 (1983). Isoln, primary structure and synthesis of native human hypothalamic GRF (hGRF), identity with hpGRF and comparison with GRF from other species: N. Ling et al., Proc. Natl. Acad. Sci. USA 81, 4302 (1984). Immunohistochemical detection of GRF in brain: B. Bloch et al., ibid. 301, 607 (1983). Potent interaction of glucocorticoids with GRF in vivo: W. B. Wehrenberg et al., Science 221, 556 (1983). Series of articles on clinical pharmacology: Horm. Res. 22, 32-57 (1985). Clinical evaluation in treatment of hypopituitary dwarfism: M. O. Thorner et al., N. Engl. J. Med. 312, 4 (1985). Reviews: R. Guillemin et al., Recent Prog. Horm. Res. 40, 233-299 (1984); W. B. Wehrenberg et al., Annu. Rev. Pharmacol. Toxicol. 25, 463-483 (1985).
Properties: Porcine GRF is destroyed by trypsin, chymotrypsin, pepsin. Biological activity remains after incubation at pH 8.5 for 4 hours at 37°, but is destroyed after similar incubation at pH 2.

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