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Journal of Endocrinology (1996) 148, 381-386       DOI: 10.1677/joe.0.1480381
© 1996 Society for Endocrinology
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Signal transduction systems employed by synthetic GH-releasing peptides in somatotrophs

C Chen, D Wu and I J Clarke

Introduction: Around the time when the endogenous hypothalamic releasing factor for growth hormone (GH) was isolated, a new range of synthetic peptides were also shown to be specific releasors of GH. These peptides were originally developed in the late 1970s by Bowers et al. (1980) who synthesized the enkephalin analogue Tyr-D-Trp-Gly-Phe-Met-NH2 and found that it specifically stimulated GH secretion. Although this pentapeptide was a weak GH secretagogue it was the first non-GH-releasing hormone (GHRH) found to act on the anterior pituitary to specifically release GH and was used as a model to design more potent forms of GH-releasing peptides (GHRPs) (Momany et al. 1981). The most potent of the first generation analogues was GHRP-6 (Bowers et al. 1984, Momany et al. 1984), a hexapeptide which stimulates GH release in a variety of animal species and in man (Bowers et al. 1984, 1991, Wu et al. 1994a). Since then, a range




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