Characterization of melanotropin-release-inhibiting factor (melanostatin) from frog brain: Homology with human neuropeptide Y

N. Chartrel, J. M. Conlon, J. M. Danger, A. Fournier, M. C. Tonon, H. Vaudry

Research output: Contribution to journalArticlepeer-review

98 Citations (Scopus)

Abstract

A polypeptide was purified from frog brain extracts on the basis of its ability to inhibit α-melanotropin release from perifused frog neurointermediate lobes. Based on Edman degradation, amino acid analysis, and peptide mapping, the primary structure of this frog melanotropin-release-inhibiting factor (melanostatin) was determined to be H-Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Glu-Asp -Met-Ala-Lys-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg- Gln-Arg-Tyr-NH2. Frog melanostatin belongs to the pancreatic polypeptide/neuropeptide Y/peptide YY family, and the structure of this peptide differs from that of human neuropeptide Y by only one amino acid substitution in position 19. A synthetic replicate of frog melanostatin is coeluted with the native peptide on HPLC and is highly potent in inhibiting α-melanotropin secretion in vitro (IC50 = 60 nM).

Original languageEnglish
Pages (from-to)3862-3866
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number9
DOIs
Publication statusPublished - 1991
Externally publishedYes

Keywords

  • control of pigmentation
  • evolution
  • peptide isolation
  • peptide mapping
  • pituitary melanotrophs

ASJC Scopus subject areas

  • General

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