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Human β -melanocyte-Stimulating Hormone Revisited
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Human β -melanocyte-Stimulating Hormone Revisited
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Human β -melanocyte-Stimulating Hormone Revisited
Human β -melanocyte-Stimulating Hormone Revisited
Journal Article

Human β -melanocyte-Stimulating Hormone Revisited

1986
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Overview
It is generally accepted that human β -melanocyte-stimulating hormone (hβ 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 hβ 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 γ LPH (hγ LPH) antiserum that recognized equally hγ LPH, hβ MSH, and hβ MSH-(5-22) or a mid-portion hγ LPH antiserum that recognized hγ LPH and hβ MSH but not hβ MSH-(5-22). Normal pituitaries and pituitary tumors contained a single immunoreactive material coeluting with hγ LPH. The hypothalami and the nonpituitary tumors all contained hγ LPH and a smaller molecular weight material that was only detected in the COOH-terminal hγ LPH radioimmunoassay; its elution volume (Ve/V, 0.75) was identical to that of hβ MSH-(5-22) but different from that of hβ MSH (Ve/V, 0.60); on reversed-phase HPLC, it coeluted with synthetic hβ MSH-(5-22) with a retention time different from that of hβ MSH. It is concluded that hβ MSH-(5-22) that corresponds to the 18-amino acid peptide hβ LPH-(39-56), flanked by two pairs of basic amino acids within the hβ LPH molecule, is a normal maturation product of proopiomelanocortin in human nonpituitary tissues.