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Dynorphin converting enzyme in the rat spinal cord. Decreased activities during acute phase of adjuvant induced arthritis.

Abstract
This paper describes a study on a dynorphin converting enzyme in spinal cord homogenates from rats with experimental arthritis after adjuvant injection into one hindpaw. The enzyme resembles a neutral cysteine endopeptidase which cleaves the opioid peptide dynorphin B and generates its N-terminal fragment, Leu-enkephalin-Arg6 with opioid activity. It exhibits considerably lower activity against dynorphin A and alpha-neoendorphin, the two other prodynorphin derived peptides. The enzyme showed significantly higher activity in the dorsal part than in the ventral part of the spinal cord. A significant decrease in enzyme activity was observed in the dorsal spinal cord during inflammation as compared to vehicle-injected controls. This decrease paralleled a decrease in the tissue level of Leu-enkephalin-Arg6. These data thus indicate that adjuvant-induced arthritis may generate an important change in a converting enzyme acting on peptide structures, which may be involved in pain modulation. Therefore, a functional role of the present enzyme in the regulation of pain-related peptides is suggested.
AuthorsJ Silberring, T Sakurada, F Nyberg
JournalLife sciences (Life Sci) Vol. 50 Issue 12 Pg. 839-47 ( 1992) ISSN: 0024-3205 [Print] Netherlands
PMID1545665 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Serine Endopeptidases
  • dynorphin-converting endopeptidase
Topics
  • Acute Disease
  • Amino Acid Sequence
  • Animals
  • Arthritis, Experimental (enzymology)
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Male
  • Molecular Sequence Data
  • Radioimmunoassay
  • Rats
  • Rats, Inbred Strains
  • Serine Endopeptidases (isolation & purification, metabolism)
  • Spectrometry, Mass, Fast Atom Bombardment
  • Spinal Cord (enzymology)
  • Substrate Specificity

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