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671st Meeting

Neuropeptidases regulating gonadal function

A. I. Smith, C. N. Shrimpton, U. M. Norman, I. J. Clarke, A. J. Wolfson, R. A. Lew
Biochemical Society Transactions Aug 01, 2000, 28 (4) 430-434; DOI: 10.1042/bst0280430
A. I. Smith
Baker Medical Research Institute, PO Box 6492, St Kilda Road Central, Melbourne, Victoria 8008, Australia
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C. N. Shrimpton
Baker Medical Research Institute, PO Box 6492, St Kilda Road Central, Melbourne, Victoria 8008, Australia
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U. M. Norman
Baker Medical Research Institute, PO Box 6492, St Kilda Road Central, Melbourne, Victoria 8008, Australia
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I. J. Clarke
Prince Henry's Institute for Medical Research, Monash Medical Centre, Clayton, Victoria 3168, Australia
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A. J. Wolfson
Department of Chemistry, Wellesley College, Wellesley, MA 02181, U.S.A.
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R. A. Lew
Baker Medical Research Institute, PO Box 6492, St Kilda Road Central, Melbourne, Victoria 8008, Australia
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Abstract

The generation and metabolism of bioactive peptides involves a series of highly ordered proteolytic events. This post-translational processing can occur either within the cell, at the cell surface or after secretion. In the central nervous system a number of extracellular peptidases have been implicated in the regulated processing of peptides, particularly in the regulation of neuroendocrine function. The aim of this study has been to identify the peptidases involved in the metabolism of gonadotropin-releasing hormone (GnRH) and to characterize the factors and the mechanisms by which the activity of these peptidases are regulated. We have shown that both prolylendo-peptidase and the thimet oligopeptidase EC 3.4.24.15 are involved in GnRH metabolism and that both oestrogen and thiol-based reductants could be involved in the physiological regulation of their activities.

  • gonadal axis
  • gonadotropin-releasing hormone
  • oestrogen
  • prolylendopeptidase
  • CSF, cerebrospinal fluid
  • GnRH, gonadotropin-releasing hormone
  • LH, luteinizing hormone
  • ME, median eminence
  • OVX, ovariectomized
  • PEP, prolylendopeptidase
  • QFS, quenched fluorescent substrate [7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-d-Lys(2,4-dinitrophenyl)]
  • © 2000 Biochemical Society
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August 2000

Volume: 28 Issue: 4

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Neuropeptidases regulating gonadal function
A. I. Smith, C. N. Shrimpton, U. M. Norman, I. J. Clarke, A. J. Wolfson, R. A. Lew
Biochemical Society Transactions Aug 2000, 28 (4) 430-434; DOI: 10.1042/bst0280430
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Neuropeptidases regulating gonadal function
A. I. Smith, C. N. Shrimpton, U. M. Norman, I. J. Clarke, A. J. Wolfson, R. A. Lew
Biochemical Society Transactions Aug 2000, 28 (4) 430-434; DOI: 10.1042/bst0280430

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Keywords

gonadal axis
gonadotropin-releasing hormone
oestrogen
prolylendopeptidase
CSF, cerebrospinal fluid
GnRH, gonadotropin-releasing hormone
LH, luteinizing hormone
ME, median eminence
OVX, ovariectomized
PEP, prolylendopeptidase
QFS, quenched fluorescent substrate [7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-d-Lys(2,4-dinitrophenyl)]

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