Differential in vitro metabolism of β-endorphin in schizophrenia

Hans Schoemaker, Thomas P. Davis

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Biologically active peptide fragments derived from the proteolytic cleavage of β-endorphin (βE) have been shown to be present in the brain. Based on clinical results using some of these fragments in neuropsychiatric disease studies we investigated the in vitro metabolism of βE by twice-washed membrane homogenates of postmortem putamen from sex and age matched controls versus subjects with a diagnosis of schizophrenia. The present study demonstrates that frozen (-80°C) postmortem human tissues are viable for these studies and that metabolism in control tissue proceeds similarly to fresh tissues. Furthermore, a significant increase in the formation of the putative neuroleptic-like peptide fragment desenkephalin-γ-endorphin in postmortem schizophrenic putamen versus controls was shown. A significant decrease in the formation of βE 6-21 was also reported. These data suggest that an approach using postmortem human brain is possible in studying β-endorphin catabolism and is therefore applicable to other neuropeptide systems.

Original languageEnglish (US)
Pages (from-to)1049-1054
Number of pages6
Issue number6
StatePublished - 1984


  • High performance liquid chromatography
  • Proteolytic processing
  • Schizophrenia
  • α-Endorphin
  • β-Endorphin
  • γ-Endorphin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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