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What is Hexarelin used for?
Hexarelin is a potent, synthetic, peptidic, orally-active, centrally-penetrant, and highly selective agonist of the ghrelin/growth hormone secretagogue receptor (GHSR) and a growth hormone secretagogue. It stimulates the secretion of growth hormone (GH) and stimulates appetite in both humans and rodents. It’s anabolic and orexigenic effects have made it an interesting substance for treating metabolic diseases and anorexia nervosa. It is currently under clinical development in a number of conditions in which the loss of lean body mass is a problem. In this review, we discuss the pharmacology, pharmacokinetics, efficacy, and safety of Hexarelin in humans. We also discuss the possible mechanism of action of Hexarelin.
Is Hexarelin a GHRH?
Hexarelin, a peptidyl analog of growth hormone secretagogue-1a (GHS-1a), is a synthetic growth hormone secretagogue that stimulates the secretion of GH, an effect that is mediated via a specific binding site on the growth hormone secretagogue receptor (GHRH). Growth hormone secretagogue (GHS)-1a is a cyclic peptide (GH~3~–GHS–NH~2~) that binds and activates the same receptor as ghrelin, a 28-amino acid hormone secreted by the stomach that stimulates the secretion of growth hormone (GH) and appetite. GHS-1a is an endogenous peptide that was initially identified as a circulating factor in the rat that stimulated the secretion of growth hormone (GH) (Kojima et al., 2001).
Later, Kojima et al. (2004) characterized a partial GHS-1a gene from the human hypothalamus and characterized a human ghrelin receptor (GHSR) that was highly homologous to the rat ghrelin receptor.
In addition, they reported the presence of the same GHS-1a gene in human pancreatic islets, suggesting that this peptide may be synthesized in the pancreas and/or in the gastrointestinal tract. Subsequently, this molecule was described in fish (Zwahlen et al., 2004).
What is the Chemical structure of Hexarelin?
The ghrelin receptor belongs to a new class of G protein-coupled receptors, which are known to mediate the secretion of GH. This receptor is located primarily in the hypothalamus and pituitary and is expressed in the arcuate nucleus, medial hypothalamus, and ventromedial nucleus. The ghrelin/GHSR system is involved in the regulation of energy balance and it was first identified in rats (Kojima et al., 2001), later in mice (Pelleymounter et al., 2002), and more recently in humans (Schuelert et al., 2002). In a series of studies using a variety of receptor subtypes and cellular signaling pathways, it was confirmed that ghrelin has a potent orexigenic effect in the brain by acting on several sites, including the arcuate nucleus (ArcN) and the ventral tegmental area (VTA). It also stimulated the release of growth hormone (GH) and stimulates feeding behavior by activating neurons in the ArcN, which may be related to the regulation of the synthesis and release of other substances in the hypothalamus.
What peptides are like HGH?
Ghrelin and GHS-1a interact with the same receptor (ghrelin receptor), which is highly homologous to the binding site of the endogenous ligand, ghrelin. It is the only peptidyl receptor described so far that does not contain a cysteine residue, unlike most receptors. In addition, the ghrelin/GHSR interaction activates signaling pathways different from the typical receptor-ligand interaction. These data indicate that this receptor is a special member of the G protein-coupled receptor family, called a selective receptor. The binding of ligands to this receptor may affect the activation of multiple receptors such as P2X purinoceptors, opioid receptors, and the adenosine-1 receptor.
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In mice, the expression of the GHSR gene and its peptide ligand was found in the pituitary, ArcN, and VTA. GHS-1a, a synthetic peptidyl agonist of the GHSR, is a highly selective ligand with a 1000-fold greater potency than ghrelin in stimulating the secretion of growth hormone (GH) and inducing food intake in rats. In addition, GHS-1a is an efficient GH secretagogue in human adipose tissue, whereas ghrelin did not stimulate the secretion of GH in human adipose tissue (Tschöp et al., 2004). These data indicate that GHS-1a and ghrelin function by binding to the same receptor and activating distinct pathways. GHS-1a has a unique pharmacological profile that is unlike that of ghrelin. Both GHS-1a and ghrelin have the same primary amino acid sequence (GH~3~–GHS–NH~2~).
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However, there are some differences in the amino acid sequences of these peptides in the C-terminus region, making these two peptides not identical. The peptides differ only in the replacement of Tyr (Tyr-3), by Phe (Phe-3) in GHS-1a, in addition to a Glu/Asp exchange in the hexarelin sequence (Phe-3–Glu–Lys–Asp–Tyr-3–His-5) in the hexarelin peptide. The GH-releasing properties of GHS-1a and its analogs, which do not include the Phe-3 sequence, have been investigated (Blevins and Kelly, 1994; Zwahlen et al., 2004). These studies indicate that the Phe-3 sequence and a positive charge are important for ghrelin\’s activity. Therefore, the Glu/Asp exchange in hexarelin (Phe-3–Glu–Lys–Asp–Tyr-3–His-5) may have contributed to the anabolic effects of hexarelin. Furthermore, a study in hypophysectomized rats (Cadet et al., 2004) found that GHS-1a can act in concert with other hypothalamic neuropeptides to enhance the secretion of GH. Thus, the hypothalamic peptides that have an anabolic effect, such as growth hormone-releasing hormone (GHRH), stimulate the synthesis of GHS-1a, which in turn stimulates the secretion of GH. Therefore, GHS-1a may function as a neurotransmitter that serves as a link between peptides and other brain cell types.
The GHSR is a member of the class B group of the rhodopsin-like family of G protein-coupled receptors, a class that includes the secretin receptor, β~2~ adrenergic receptor, and muscarinic acetylcholine receptors. This group of receptors is characterized by a seven-transmembrane domain structure, a relatively long extracellular loop and an intracellular loop. A number of important structural features of the GHSR allow its activation by ghrelin or GHS-1a (Kojima et al., 2004; Wurtman et al., 2004). These structural elements include the C-terminal sequence of the receptor, its relatively long extracellular loop, its intracellular loop, and the first two transmembrane domains. In addition, specific substitutions of amino acids are located in the loops.
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