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Related Experiment Videos

Evidence for Pro-dermorphin processing products in rat tissues.

A Mor1, P Pradelles, A Delfour

  • 1Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, Université Paris 7, France.

Biochemical and Biophysical Research Communications
|July 16, 1990
PubMed
Summary
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Powerful opioid peptides, dermorphin and dermenkephalin, originally found in frog skin, were detected in rat brain, stomach, and intestine tissues. This suggests mammals may process similar peptide precursors.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Dermorphin and dermenkephalin are potent opioid peptides isolated from frog skin.
  • These peptides originate from a common biosynthetic precursor.
  • Amphibian skin peptides and their homologs are often found in mammalian systems.

Purpose of the Study:

  • To investigate the presence and distribution of dermorphin and dermenkephalin in rat tissues.
  • To determine if mammals process similar peptide precursors as found in frogs.

Main Methods:

  • Development of sensitive enzyme immunoassays using antibodies against dermorphin, dermenkephalin, and the spacer sequence.
  • Immunocytochemical studies on rat brain sections.
  • Molecular sieve filtration and Reverse Phase High Performance Liquid Chromatography (RP-HPLC) for peptide characterization.

Related Experiment Videos

  • Immunological analysis and chromatographic comparison with synthetic peptides.

    • Main Results:

    • Immunoreactive dermorphin, dermenkephalin, and spacer peptides were detected in rat brain, stomach, and intestine.
    • Immunocytochemistry showed similar distribution patterns for these peptides in rat brain regions and cells.
    • Higher molecular weight immunoreactive species, potentially extended or homologous peptides, were also found.

    Conclusions:

    • The dermorphin precursor is processed in various rat tissues, including the brain, stomach, and intestine.
    • Mammals may possess endogenous counterparts or homologous peptides to amphibian opioid peptides.
    • These findings suggest a conserved evolutionary pathway for opioid peptide biosynthesis.