The GH, prolactin, ACTH and cortisol responses to Hexarelin, a synthetic hexapeptide, undergo different age-related variations

Arvat, Emanuela; Ramunni, J.; Bellone, J.; Vito, Lidia Di; Baffoni, Claudia; Broglio, Fabio; Deghenghi, Romano; Bartolotta, E; Ghigo, Ezio

doi:10.1530/eje.0.1370635

Cited by 45 publications

(17 citation statements)

References 53 publications

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“…The provocative tests of GH have been introduced in human medicine to assess the hypothalamic and/or pituitary functional integrity and a whole series of pharmacological stimuli has been used to test GH secretion [28]. In this study we chose to stimulate GH axis with GHRH, HEX and GAL, at concentrations that induce the maximal response according to our preliminary studies that agree well with data recently reported in prepubertal children [2,8,9]. Our results clearly indicate that the growth rate in piglets does not depend on GH secretory status: in both control and under weight piglets, mean GH concentration, number and amplitude of peaks were not different.…”

Section: Discussionsupporting

confidence: 55%

IGF-I, IGFBP-2 and -3 but not GH concentrations are different in normal and poor growing piglets

et al. 2001

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-In this study we investigated the somatotropic axis in piglets with evident growth delay. Female Suffolk crossbred piglets (30 days old; N = 12) were divided into normal weight (10 ± 0.9 kg) and poor growing subjects (7 ± 0.5 kg) and bled for growth hormone (GH), Insulin-like growth factor-I (IGF-I), Insulin-like growth factor binding protein 2 and 3 (IGFBP-2 and -3) determination. Basal and induced-GH levels were not different in the groups. Plasma IGF-I concentrations were significantly different (p < 0.001): 101.8 ± 9.8 ng . mL -1 (normal weight group) and 39.5 ± 4.0 ng . mL -1 (poor growing group). IGFBP-2 and -3 concentrations were significantly (p < 0.001) lower in poor growing than in normal piglets. Piglet weight was positively correlated (r = 0.98, p < 0.001) with IGF-I and IGFBP-2 or -3 concentrations. Our data indicate that growth rate was not correlated to basal or secretagogue-induced GH secretion. growth hormone / somatotropic axis / insulin-like growth factor I / insulin-like growth factor binding protein / pigletRésumé -Les concentrations de IGF-I, IGFBP-2 et -3 sont différentes chez les porcelets normaux et chez les porcelets qui présentent un retard de croissance ; cette différence n'existe pas pour la GH. L'objet de cette étude est l'axe somatotrope chez les porcelets présentant un retard de croissance manifeste. Douze porcelets femelles croisés Suffolk (âgés de 30 jours) ont été subdivisés en deux groupes : sujets de poids normal (10 ± 0,9 kg ; N = 6) et sujets avec retard de croissance (7 ± 0,5 kg ; N = 6) : des prélèvement sanguins ont été effectués pour la détermination de l'hormone de croissance (GH), de l'Insulin-like growth factor I (IGF-I), et des Insulin-like growth factor binding protein-2 et -3 (IGFBP-2 et -3). Aucune différence n'a été observée entre les concentrations basale et induite

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Section: Discussionsupporting

confidence: 55%

IGF-I, IGFBP-2 and -3 but not GH concentrations are different in normal and poor growing piglets

et al. 2001

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“…When ghrelin was used in either the same system, or in hypothalamic slices, both AVP and CRH stimulation was observed (71). Interestingly, the effect of ghrelin on ACTH secretion is even more pronounced than that elicited by GHS (62,72). These results indicate that ghrelin stimulates the HPA axis independent of the pituitary, via the hypothalamus, involving both CRH and AVP stimulation.…”

Section: Gastric Functionsmentioning

confidence: 75%

Biological, Physiological, and Pharmacological Aspects of Ghrelin

2006

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Abstract. Ghrelin, identified as an endogenous ligand for the growth hormone secretagogue receptor, functions as a somatotrophic and orexigenic signal from the stomach. Ghrelin has a unique post-translational modification: the hydroxyl group of the third amino acid, usually a serine but in some species a threonine, is esterified by octanoic acid and is essential for ghrelin's biological activities. The secretion of ghrelin increases under conditions of negative energybalance, such as starvation, cachexia, and anorexia nervosa, whereas its expression decreases under conditions of positive energy-balance such as feeding, hyperglycemia, and obesity. In addition to having a powerful effect on the secretion of growth hormone, ghrelin stimulates food intake and transduces signals to hypothalamic regulatory nuclei that control energy homeostasis. Thus, it is interesting to note that the stomach may play an important role in not only digestion but also pituitary growth hormone release and central feeding regulation. We summarized recent findings on the integration of ghrelin into neuroendocrine networks that regulate food intake, energy balance, gastrointestinal function and growth.

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“…Native AG , Tassone et al 2003, Vestergaard et al 2007, Milosevic et al 2013 or the synthetic GHSs (Korbonits et al 1995, Bowers & Granda-Ayala 1996, Arvat et al 1997, Clark et al 1997 have been shown to stimulate ACTH secretion in several species, such as humans and rats. However, this effect could depend on the metabolic/ energy status, as AG-induced ACTH secretion has been shown to be impaired in obesity (Milosevic et al 2013).…”

Section: Observations)mentioning

confidence: 99%

Ghrelin gene products, receptors, and GOAT enzyme: biological and pathophysiological insight

Gahete

Rincón-Fernández

Villa-Osaba

et al. 2013

Journal of Endocrinology

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Ghrelin is a 28-amino acid acylated hormone, highly expressed in the stomach, which binds to its cognate receptor (GHSR1a) to regulate a plethora of relevant biological processes, including food intake, energy balance, hormonal secretions, learning, inflammation, etc. However, ghrelin is, in fact, the most notorious component of a complex, intricate regulatory system comprised of a growing number of alternative peptides (e.g. obestatin, unacylated ghrelin, and In1-ghrelin, etc.), known (GHSRs) and, necessarily unknown receptors, as well as modifying enzymes (e.g. ghrelin-O-acyl-transferase), which interact among them as well as with other regulatory systems in order to tightly modulate key (patho)-physiological processes. This multiplicity of functions and versatility of the ghrelin system arise from a dual, genetic and functional, complexity. Importantly, a growing body of evidence suggests that dysregulation in some of the components of the ghrelin system can lead to or influence the development and/or progression of highly concerning pathologies such as endocrine-related tumors, inflammatory/cardiovascular diseases, and neurodegeneration, wherein these altered components could be used as diagnostic, prognostic, or therapeutic targets. In this context, the aim of this review is to integrate and comprehensively analyze the multiple components and functions of the ghrelin system described to date in order to define and understand its biological and (patho)-physiological significance.

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The GH, prolactin, ACTH and cortisol responses to Hexarelin, a synthetic hexapeptide, undergo different age-related variations

Cited by 45 publications

References 53 publications

IGF-I, IGFBP-2 and -3 but not GH concentrations are different in normal and poor growing piglets

IGF-I, IGFBP-2 and -3 but not GH concentrations are different in normal and poor growing piglets

Biological, Physiological, and Pharmacological Aspects of Ghrelin

Ghrelin gene products, receptors, and GOAT enzyme: biological and pathophysiological insight

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