Alexamorelin is a peptide of seven amino acids. It is a GHS (growth hormone secretagogue, a compound that triggers growth hormone release). It switches on GHS-R1a (the ghrelin (the hunger hormone) receptor), a G-protein coupled receptor (a type of docking site on the cell surface) found on somatotroph cells (the growth hormone-making cells) in the anterior pituitary (the front part of the pituitary gland at the base of the brain). Switching on the receptor lets calcium flow into the cell and triggers phospholipase C signaling (an internal chain of messages). The cell becomes electrically active (depolarization) and releases GH. Alexamorelin stimulates ACTH (the hormone that tells the adrenal glands to make cortisol (the stress hormone)) more strongly than hexarelin does. This points to stronger signaling at GHS-R1a receptors on corticotroph cells (the ACTH-making cells). It also raises aldosterone (a hormone that controls salt and water balance). This suggests cross-talk with the mineralocorticoid pathways (the aldosterone system) or direct stimulation of the adrenal glands. Its stronger ACTH effect compared with its parent compound hexarelin may come from changes to its structure (an alanine at the start of the chain, and 2-methyl-D-tryptophan) that alter which receptor subtypes it favors or how strongly it signals. After injection, carboxypeptidase A (an enzyme that clips amino acids off the end of a chain) quickly removes the end alanine. Within hours this leaves hexarelin as the main breakdown product. This prodrug relationship (the body converts it into another active drug) explains why alexamorelin acts like hexarelin, while possibly activating different pathways earlier, before it is converted.