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Related Experiment Video

Updated: Jun 12, 2026

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus
09:22

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus

Published on: May 31, 2022

Neuropeptides and their peptidases: Functional considerations.

G M Littlewood1, L L Iversen, A J Turner

  • 1MRC Membrane Peptidase Research Group, Department of Biochemistry, University of Leeds, Leeds LS2 9JT, U.K.

Neurochemistry International
|May 27, 2010
PubMed
Summary

Endopeptidase-24.11 plays a key role in inactivating neuropeptides like substance P in the brain. This finding helps understand neuropeptide regulation and potential therapeutic targets.

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Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

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Last Updated: Jun 12, 2026

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus
09:22

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus

Published on: May 31, 2022

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Brain membrane peptidases are crucial for neuropeptide metabolism.
  • Endopeptidase-24.11 and angiotensin converting enzyme are key enzymes involved in neuropeptide degradation.

Purpose of the Study:

  • To review the properties of brain membrane peptidases, focusing on endopeptidase-24.11 and angiotensin converting enzyme.
  • To define substrate specificities and assess the contribution of these enzymes to tachykinin degradation.
  • To investigate the physiological roles of peptidases using selective inhibitors and brain slice preparations.

Main Methods:

  • Review of peptidase properties and substrate specificities.
  • In vitro studies on tachykinin degradation.
  • Application of peptidase inhibitors to study neuropeptide release from rat substantia nigra brain slices.

Main Results:

  • Endopeptidase-24.11 inhibition significantly increased substance P recovery from rat brain slices.
  • Angiotensin converting enzyme inhibition had no significant effect on substance P recovery.
  • Endopeptidase-24.11's specificity and distribution align with a role in inactivating tachykinins and enkephalins.

Conclusions:

  • Endopeptidase-24.11 is implicated in the physiological inactivation of tachykinins and enkephalins in the brain.
  • Luteinizing hormone-releasing hormone (LHRH) and atrial natriuretic peptide may be peripheral substrates for endopeptidase-24.11.
  • The endogenous neuropeptide substrates for striatal angiotensin converting enzyme require further investigation.