Particular processing of pro-opiomelanocortin in Xenopus laevis intermediate pituitary. Sequencing of alpha- and beta-melanocyte-stimulating hormones

FEBS Lett. 1989 Mar 13;245(1-2):215-8. doi: 10.1016/0014-5793(89)80224-8.

Abstract

alpha- and beta-melanocyte-stimulating hormones (alpha-MSH and beta-MSH) have been isolated from Xenopus laevis neurointermediate pituitary and microsequenced. Intracellular alpha-MSH is not N-acetylated after proteolytic processing of pro-opiomelanocortin in contrast to mammalian alpha-MSHs. There is a high preservation of the melanotropic amino acid sequence common to all MSHs although in Xenopus beta-MSH a histidine residue replaces the glutamic acid residue found in position 8 of mammalian beta-MSHs.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Glutamates
  • Glutamic Acid
  • Histidine
  • Melanocyte-Stimulating Hormones / analysis*
  • Melanocyte-Stimulating Hormones / metabolism
  • Molecular Sequence Data
  • Peptide Hydrolases / metabolism
  • Pituitary Gland / analysis*
  • Pituitary Gland / metabolism
  • Pro-Opiomelanocortin / metabolism*
  • Sequence Homology, Nucleic Acid
  • Xenopus laevis / metabolism*
  • alpha-MSH / analysis*
  • alpha-MSH / metabolism

Substances

  • Glutamates
  • Glutamic Acid
  • Histidine
  • alpha-MSH
  • Pro-Opiomelanocortin
  • Melanocyte-Stimulating Hormones
  • Peptide Hydrolases