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- Title
Analgesic activity of lipotropin C fragment depends on carboxyl terminal tetrapeptide.
- Authors
GEISOW, M. J.; DEAKIN, J. F. W.; DOSTROVSKY, J. O.; SMYTH, D. G.
- Abstract
A SERIES of peptides with morphine-like activity has been identified in extracts of pituitary1-3 and brain4-7. With the exception of Leu-enkephalin, all those characterised represent some fraction of the 31-residue C fragment-a specific activation product of lipotropin1,8. Several attempts have been made to define the receptor requirements of opiate peptides9,10 and to make potent and stable agonists5,11,12, but essentially all the studies have been based on the easily synthesised NH2-terminal pentapeptide of C fragment, Met-enkephalin. Unlike the enkephalins, C fragment has a high potency in its central actions13-16, in vivo and in vitro, and it is relatively stable to brain peptidases17-19. C fragment is the only naturally occurring peptide to possess strong analgesic properties and have a long lasting action20. It is clear that specific regions of the molecular structure, not present in γ and α endrophin or Met-enkephalin, have a role in the expression of its central activity. We present here evidence that the COOH-terminal tetrapeptide of C fragment, Lys-Lys-Gly-Gln, is responsible for the unique affinity of C fragment for brain opiate receptors and that the presence of all four residues is essential for the high analgesic potency.
- Publication
Nature, 1977, Vol 269, Issue 5624, p167
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/269167a0