It is generally accepted that human
beta-melanocyte-stimulating hormone (h
beta MSH) does not normally exist in humans but was merely an artifactually generated 22-amino
acid peptide corresponding to a
lipotropin (LPH) fragment (residues 35-56). We examined whether the shorter 18-amino
acid peptide h beta MSH-(5-22) could be detected in some human tissues. Normal human pituitaries and hypothalami as well as
corticotropin-secreting pituitary and nonpituitary
tumors were extracted and chromatographed on
Sephadex G-50, and the fractions were measured with two radioimmunoassays using either a COOH-terminal human
gamma LPH (h
gamma LPH) antiserum that recognized equally h
gamma LPH, h
beta MSH, and h beta MSH-(5-22) or a mid-portion h
gamma LPH antiserum that recognized h
gamma LPH and h
beta MSH but not h beta MSH-(5-22). Normal pituitaries and
pituitary tumors contained a single immunoreactive material coeluting with h
gamma LPH. The hypothalami and the nonpituitary
tumors all contained h
gamma LPH and a smaller molecular weight material that was only detected in the COOH-terminal h
gamma LPH radioimmunoassay; its elution volume (Ve/V, 0.75) was identical to that of h beta MSH-(5-22) but different from that of h
beta MSH (Ve/V, 0.60); on reversed-phase HPLC, it coeluted with synthetic h beta MSH-(5-22) with a retention time different from that of h
beta MSH. It is concluded that h beta MSH-(5-22) that corresponds to the 18-amino
acid peptide h beta LPH-(39-56), flanked by two pairs of
basic amino acids within the h
beta LPH molecule, is a normal maturation product of
proopiomelanocortin in human nonpituitary tissues.