Abstract
A SERIES of peptides derived from lipotropin has been reported to possess morphinomimetic properties. The C fragment (or β endorphin, residues 61–91) was isolated from pituitary1,2 and shown to be present in brain3, the C′ fragment (61–87) occurs in pituitary1, γ endorphin (61–77) and α endorphin (61–76) were obtained after acid extraction of tissue of hypothalamic and pituitary origin4, and Met-enkephalin (61–65) was found in extracts of brain5,6. Examination of the ability of these peptides to displace specifically bound 3H-naloxone from brain opiate receptors showed that C fragment was much more potent than the shorter peptides7 and investigation of the antinociceptive properties showed that C fragment alone produces profound and long-lasting analgesia8–11. In addition, various other central activities are exhibited by C fragment12–14. We report here that C fragment can be degraded by membrane bound enzymes from rat brain to form the smaller opiate-like peptides.
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References
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AUSTEN, B., SMYTH, D. & SNELL, C. γ Endorphin, α endorphin and Met-enkephalin are formed extracellularly from lipotropin C fragment. Nature 269, 619–621 (1977). https://doi.org/10.1038/269619a0
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DOI: https://doi.org/10.1038/269619a0
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