Pituitary immunoreactive gamma-melanotropins are glycosylated oligopeptides

Nature. 1980 Jun 5;285(5764):416-7. doi: 10.1038/285416a0.

Abstract

Nakanishi et al. have recently characterised the complete sequence of the mRNA isolated from the intermediate lobe of bovine pituitary which codes for the 31,000 molecular weight (31K) precursor protein of corticotropin/beta-lipotropin (ACTH/beta-LPH). The corresponding amino acid sequence translated from this mRNA revealed in the cryptic region of the precursor protein a fragment sharing a common amino acid sequence with the alpha- beta-melanotropins (alpha-MSH, beta-MSH) and thus named gamma-MSH. To study whether this gamma-MSH fragment is also processed and released as a biologically active substance and to ascertain its location in the pituitary and possibly in the brain, we have raised antibodies to the synthetic replicate of gamma 3-MSH (ref. 2). We report here the detection of at least two gamma-MSH-like peptides in the pituitary using these antibodies in a radioimmunoassay (RLA) and, furthermore, evidence that these two peptides are glycosylated.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Carbohydrate Metabolism
  • Chromatography, Affinity
  • Concanavalin A / metabolism
  • Glycopeptides* / immunology
  • Glycopeptides* / metabolism
  • Melanocyte-Stimulating Hormones* / immunology
  • Melanocyte-Stimulating Hormones* / metabolism
  • Molecular Weight
  • Pituitary Gland / chemistry*
  • Pituitary Gland, Anterior / chemistry
  • Protein Precursors / immunology

Substances

  • Glycopeptides
  • Protein Precursors
  • Concanavalin A
  • Melanocyte-Stimulating Hormones