Characterization of in vitro proteolytic processing of β-endorphin by reversed-phase HPLC

Thomas P. Davis, Hans Schoemaker, Alison J. Culling-Berglund

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

In vitro, central and peripheral proteolytic processing of β-endorphin by membrane-bound enzymes results in the formation of specific active fragments that have been recently shown to function in behavior, intestinal motility and in the central control of urinary bladder activity. A high resolution, reversed phase high performance liquid chromatography system capable of separating 28 β-endorphin related fragments simultaneously was used to study the time-course processing of β-endorphin by membrane associated peptidases in the brain and regions of the small intestine. The hypothesis we tested was that a homeostatic balance between α- and γ-type endorphins exists in these tissues. The results of the study show that the rate and quantity of fragments produced between the mucosa and nerve-muscle regions of the small intestine are significantly different. Metabolic rates, pattern, and the ratio of α/γ-type endorphins in the brain were very similar to the nerve-muscle region of the small intestine. This suggests that β-endorphin processing to active fragments is occurring at the nerves of the small intestine and that a specific and similar balance of α/γ-type endorphin exists in the brain and gastrointestinal system at neutral pH.

Original languageEnglish (US)
Pages (from-to)1037-1042
Number of pages6
JournalPeptides
Volume5
Issue number6
DOIs
StatePublished - Jan 1 1984

Keywords

  • High performance liquid chromatography
  • Intestinal motility
  • Membrane associated proteolytic processing
  • Peptide processing
  • α-Endorphin
  • β-Endorphin
  • γ-Endorphin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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