Elsevier

Life Sciences

Volume 37, Issue 11, 16 September 1985, Pages 985-992
Life Sciences

Minireview
Peptidases that terminate the action of enkephalins. Consideration of physiological importance for amino-, carboxy-, endo-, and pseudoenkephalinase

https://doi.org/10.1016/0024-3205(85)90586-7Get rights and content

Abstract

The term “enkephalinase” has been frequently applied to enzyme activity in a variety of tissue preparations. In some cases there has been the implication that cleavage of a specific peptide bond in the enkephalin molecule results from the action of a single enzyme with the major responsibility of inactivating synaptic enkephalin. It is not known to what extent diverse enkephalin-degrading enzymes, with differing peptide bond specificities, may act in concert at any given synapse. There do exist, however, enzymes having known characteristic specificities with respect both to peptide substrates, including enkephalins, and to identifiable peptide bonds. Thus, at any given site of enkephalin release there probably resides a characteristic assembly of peptidases concerned with inactivation of this neuromediator. We propose that the term “enkephalinase” be used to encompass the entire family of enkephalin-degrading enzymes, and that “aminoenkephalinase”, “carboxyenkephalinase”, “endoenkephalinase” and “pseudoenkephalinase” should designate enzymes of known specificities with respect to both peptide substrates and particular peptide bonds.

References (70)

  • R.C.A. Frederickson et al.

    Prog. Neurobiol.

    (1982)
  • N. Marks et al.

    Biochem. Biophys. Res. Commun.

    (1977)
  • A. Dupont et al.

    Life Sci.

    (1977)
  • M. Knight et al.

    J. Biol. Chem.

    (1978)
  • J.L. Meek et al.

    Neuropharmacol.

    (1977)
  • J.K. Chang et al.

    Life Sci.

    (1976)
  • B.M. Austen et al.

    Biochem. Biophys. Res. Commun.

    (1977)
  • M. Benuck et al.

    Biochem. Biophys. Res. Commun.

    (1979)
  • C. Gorenstein et al.

    Life Sci.

    (1979)
  • A.T. McKnight et al.

    European J. Pharmacol.

    (1983)
  • S. de la Baume et al.

    Neuroscience

    (1983)
  • P. Chaillet et al.

    European J. Pharmacol.

    (1983)
  • J. Hughes

    Brain Res.

    (1975)
  • J.C. Schwartz et al.

    Life Sci.

    (1981)
  • S. Sullivan et al.

    Peptides

    (1980)
  • W.H. Simmons et al.

    Pharmacol. Biochem. and Behav.

    (1980)
  • L.H. Traficante et al.

    Life Sci.

    (1980)
  • E. Weber et al.

    Brain Res.

    (1978)
  • A. Patthy et al.

    Biochem. Biophys. Res. Commun.

    (1977)
  • B. Desbuquois et al.

    Biochem. Biophys. Acta.

    (1974)
  • C.-M. Lee et al.

    J. Biol. Chem.

    (1982)
  • B. Malfroy et al.

    J. Biol. Chem.

    (1984)
  • R. Matsas et al.
  • K.-S. Hui et al.
  • W.L. Scott et al.

    Life Sci.

    (1985)
  • A.-Z. Zhang et al.

    Neuropharmacology

    (1982)
  • N.A. Belyaev et al.

    Biokhimia

    (1984)
  • S. Mousa et al.

    Neuropharmacology

    (1985)
  • K-B. Augustinsson

    Cholinesterases and Anticholinesterase Agents

  • A.K. Dua
  • A.K. Dua et al.
  • Y. Jacquet et al.
  • A. Pert et al.

    Biochem. Biophys. Res. Commun.

    (1977)
  • Z. Vogel et al.
  • G.L. Craviso et al.

    Life Sci.

    (1978)
  • Cited by (27)

    • Endogenous opioid regulation of hippocampal function

      1996, International Review of Neurobiology
    View all citing articles on Scopus
    View full text