Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Neuropeptidases regulating gonadal function.

A I Smith1, C N Shrimpton, U M Norman

  • 1Baker Medical Research Institute, PO Box 6492, St Kilda Road Central, Melbourne, Victoria 8008, Australia. ian.smith@baker.edu.au

Biochemical Society Transactions
|August 30, 2000
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Verification of single-photon path entanglement using a nitrogen vacancy center.

Applied optics·2025
Same author

Response to kisspeptin and gonadotropin-releasing hormone agonist administration in Holstein-Friesian dairy heifers with positive or negative genetic merit for fertility traits.

Journal of dairy science·2022
Same author

Feeding synthetic zeolite to transition dairy cows alters neutrophil gene expression.

Journal of dairy science·2019
Same author

Stimulation of growth hormone by kisspeptin antagonists in ewes.

The Journal of endocrinology·2018
Same author

Alteration in the relationship between tanycytes and gonadotrophin-releasing hormone neurosecretory terminals following long-term metabolic manipulation in the sheep.

Journal of neuroendocrinology·2017
Same author

Effect of gonadotropin-inhibitory hormone on luteinizing hormone secretion in humans.

Clinical endocrinology·2017
Same journal

TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosis.

Biochemical Society transactions·2026
Same journal

Advancing the monitoring of organelle contact sites in vitro and in vivo.

Biochemical Society transactions·2026
Same journal

Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.

Biochemical Society transactions·2026
Same journal

Replication associated nuclear DNA mismatch repair across kingdoms.

Biochemical Society transactions·2026
Same journal

Phosphatases of regenerating liver downregulate PTEN to promote tumorigenesis.

Biochemical Society transactions·2026
Same journal

Implications of Rho GTPase signaling in cancer immunotherapy.

Biochemical Society transactions·2026
See all related articles

This study identifies key peptidases, prolylendopeptidase and thimet oligopeptidase, involved in gonadotropin-releasing hormone (GnRH) metabolism. Oestrogen and reductants may regulate these enzymes in neuroendocrine function.

Area of Science:

  • Biochemistry
  • Neuroendocrinology
  • Proteolysis

Background:

  • Bioactive peptide generation and metabolism rely on proteolytic processing.
  • Extracellular peptidases in the central nervous system regulate neuroendocrine function.
  • Understanding peptide metabolism is crucial for neuroendocrine regulation.

Purpose of the Study:

  • Identify peptidases involved in gonadotropin-releasing hormone (GnRH) metabolism.
  • Characterize regulatory factors and mechanisms of these peptidases.
  • Investigate the role of specific enzymes in GnRH processing.

Main Methods:

  • Enzyme activity assays.
  • Peptide substrate analysis.
  • Identification of enzyme inhibitors and activators.

Related Experiment Videos

Main Results:

  • Prolylendopeptidase and thimet oligopeptidase (EC 3.4.24.15) identified as key enzymes in GnRH metabolism.
  • Oestrogen demonstrated a regulatory role in peptidase activity.
  • Thiol-based reductants shown to influence peptidase activity.

Conclusions:

  • Prolylendopeptidase and thimet oligopeptidase are critical for GnRH metabolism.
  • Oestrogen and thiol-based reductants are potential physiological regulators of GnRH-metabolizing peptidases.
  • Findings contribute to understanding neuroendocrine regulation by peptide processing.