Pro-opiomelanocortin (POMC) (POMC)

Pro-opiomelanocortin (POMC) is a polypeptide hormone precursor synthesized primarily in the pituitary gland and hypothalamus, as well as in melanocytes and other tissues[2]. The POMC gene encodes a large precursor protein that is post-translationally cleaved by tissue-specific enzymes (prohormone convertases) to generate multiple bioactive peptides, including adrenocorticotropic hormone (ACTH), α-melanocyte-stimulating hormone (α-MSH), β-MSH, γ-MSH, and β-endorphin[1][2]. These peptides have diverse roles: ACTH stimulates cortisol release from the adrenal cortex, regulating stress response and metabolism; α-MSH is involved in skin and hair pigmentation and suppresses appetite through hypothalamic signaling; β-MSH and γ-MSH also contribute to energy homeostasis, with γ-MSH influencing sodium balance and blood pressure; β-endorphin is an endogenous opioid peptide with roles in pain relief and reward[1][2]. POMC-derived peptides act via binding to specific melanocortin receptors (MC1R, MC3R, MC4R) and opioid receptors, making POMC a central node in endocrine, metabolic, and neurological regulation[1][2]. Mutations in the POMC gene or its processing enzymes can lead to syndromes of adrenal insufficiency, severe obesity, and altered pigmentation[1]. POMC is thus both a critical physiological regulator and a validated, though challenging, therapeutic target for metabolic and endocrine disorders.

Other names

Proopiomelanocortinpro-γ-MSH (N-POMC, N-POC)pro-ACTHpro-γ-lipotropin

Precursor processing (cleavage by prohormone convertases) yields bioactive peptides (ACTH, α-MSH, β-MSH, γ-MSH, β-endorphin) These peptides activate specific melanocortin and opioid receptors, modulating downstream physiological pathways