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Related Experiment Videos

Human beta-melanocyte-stimulating hormone revisited.

X Bertagna, F Lenne, D Comar

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1986
    PubMed
    Summary

    The study detected a shorter peptide, human beta-melanocyte-stimulating hormone (h beta MSH)-(5-22), in human nonpituitary tissues. This peptide is a normal product of proopiomelanocortin maturation, challenging previous assumptions about h beta MSH existence.

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    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Biochemistry

    Background:

    • Human beta-melanocyte-stimulating hormone (h beta MSH) was previously considered an artifact, a 22-amino acid peptide from lipotropin (LPH).
    • The existence of shorter, biologically relevant peptides derived from LPH in human tissues remained unclear.

    Purpose of the Study:

    • To investigate the presence and characteristics of the 18-amino acid peptide h beta MSH-(5-22) in human tissues.
    • To determine if h beta MSH-(5-22) is a naturally occurring peptide in humans.

    Main Methods:

    • Extraction and Sephadex G-50 chromatography of human pituitaries, hypothalami, and tumors.
    • Radioimmunoassays using specific antisera for human gamma LPH (h gamma LPH) and its fragments.
    • Reversed-phase high-performance liquid chromatography (HPLC) for peptide characterization.

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    Main Results:

    • Normal pituitaries and pituitary tumors showed immunoreactivity only for h gamma LPH.
    • Hypothalami and nonpituitary tumors contained h gamma LPH and a smaller peptide detected by a COOH-terminal h gamma LPH antiserum.
    • This smaller peptide coeluted with synthetic h beta MSH-(5-22) in HPLC, distinct from h beta MSH.

    Conclusions:

    • The 18-amino acid peptide h beta MSH-(5-22), corresponding to h beta LPH-(39-56), is a normal maturation product of proopiomelanocortin.
    • This peptide is found in human nonpituitary tissues, suggesting its biological relevance.