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Metabolism of Tachykinins by Cell-Surface Peptidases

  • A. J. Turner
  • N. M. Hooper
Conference paper

Abstract

Tachykinins are rapidly metabolised by tissue preparations and their inactivation is believed to occur through hydrolysis by cell-surface ecto-peptidases [1]. Enzymic and immunocytochemical studies in our laboratory have previously implicated endopeptidase-24.11 (‘ enkephalinase’, EC 3.4.24.11) in the metabolism of substance P [2–4]. The ability of pig striatal synaptic membranes to hydrolyse substance P was abolished by phosphoramidon and by an antiserum to the endopeptidase [2]. Furthermore, substance P was the best substrate identified for the enzyme in vitro [3]. We have also been able to demonstrate immunohistochemically the co-localisation of endopeptidase and substance P in specific brain regions, including globus pallidus and nucleus interpeduncular is [4]. More recently, neurokinins A and B have also been shown to be good substrates for endopeptidase-24.11, implicating this enzyme in their metabolism [5,6].

Keywords

Angiotensin Converting Enzyme Angiotensin Converting Enzyme Inhibitor Nucleus Interpeduncular Striatonigral Pathway Angiotensin Converting Enzyme Inhibitor Captopril 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 1987

Authors and Affiliations

  • A. J. Turner
    • 1
  • N. M. Hooper
    • 1
  1. 1.MRC Membrane Peptidase Research Group, Department of BiochemistryUniversity of LeedsLeedsUK

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