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Ghrelin receptor agonists and antagonists act on the growth hormone secretagogue receptor (GHSR). The receptor was cloned in 1996 from pituitary and hypothalamus as the target of synthetic growth hormone secretagogues. Its endogenous ligand, ghrelin, was identified in 1999 as an acylated stomach peptide that releases growth hormone. GHSR signaling links growth hormone release with appetite and energy balance, which makes the receptor a frequent subject in metabolism research. Anamorelin, capromorelin and ulimorelin are small-molecule GHSR agonists, and des-Gln14-Ghrelin is a natural ghrelin variant. PF-5190457 acts as an inverse agonist, while liver-expressed antimicrobial peptide 2 (LEAP-2) antagonizes the receptor.
GHRF, porcine is a growth hormone releasing factor peptide that acts as a potent inducer of growth hormone (GH) release. By binding to the growth hormone secretagogue receptor (GHSR), it stimulates the secretion of GH from the anterior pituitary gland. This reagent is valuable in studies focused on growth hormone regulation, metabolic processes, and endocrine signaling pathways.
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