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Tissue distribution of a dynorphin-processing endopeptidase

L Devi1

  • 1Department of Pharmacology, New York University Medical Center, New York 10016.

Endocrinology
|March 1, 1993
PubMed
Summary

A novel dynorphin (Dyn)-converting enzyme (DCE) activity, likely a thiol protease, processes prodynorphin in rat tissues. This enzyme

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Endocrinology

Background:

  • Many peptide hormones and neurotransmitters undergo post-translational modification at monobasic cleavage sites.
  • Previous studies reported dynorphin (Dyn)-converting enzyme (DCE) activity in rat brain and bovine pituitary, processing prodynorphin.

Purpose of the Study:

  • To investigate the tissue distribution and biochemical properties of the dynorphin (Dyn)-converting enzyme (DCE) activity in rats.
  • To characterize the DCE activity and explore its role in peptide hormone processing.

Main Methods:

  • Assessed DCE activity across various adult rat tissues (brain, ileum, pituitary, adrenal, liver, heart, etc.).
  • Examined protease inhibitor profiles, including the effect of p-chloromercuriphenyl sulfonic acid (PCMPS).
  • Utilized ion exchange chromatography (diethylaminoethyl-cellulose) to analyze DCE activity from rat ileum and brain.

Main Results:

  • High DCE activity was found in rat brain, ileum, neurointermediate pituitary, and adrenal gland.
  • The enzyme activity was significantly inhibited by the thiol protease inhibitor PCMPS, indicating it's a thiol protease.
  • Chromatographic behavior, inhibitor profile, and pH optima were consistent with previously reported bovine pituitary DCE.

Conclusions:

  • The dynorphin (Dyn)-converting enzyme (DCE) is a thiol protease with a specific tissue distribution, suggesting a role in peptide processing.
  • DCE activity is present in tissues involved in hormone and neurotransmitter synthesis and secretion, supporting its involvement in peptide maturation.
  • The findings suggest DCE is crucial for the post-translational modification of dynorphin and potentially other peptide hormones and neuropeptides.

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