Marco Capogna

Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Grzegorz Wiera, Laboratory of Neuroscience, Department of Biophysics, Wroclaw Medical University, Chalubinskiego 3, 50-368, Wroclaw, Poland. gwiera@biol.uni.wroc.pl
  • ,
  • Tomasz Wójtowicz
  • ,
  • Katarzyna Lebida
  • ,
  • Aleksandra Piotrowska
  • ,
  • Dominika Drulis-Fajdasz
  • ,
  • Agnieszka Gomułkiewicz
  • ,
  • Daria Gendosz
  • ,
  • Marzena Podhorska-Okołów
  • ,
  • Marco Capogna
  • Grzegorz Wilczyński
  • ,
  • Piotr Dzięgiel
  • ,
  • Leszek Kaczmarek
  • ,
  • Jerzy W Mozrzymas

Matrix Metalloproteinases (MMPs) are a family of endopeptidases known to process extracellular proteins. In the last decade, studies carried out mainly on the Schaffer collateral-CA1 hippocampal projection have provided solid evidence that MMPs regulate synaptic plasticity and learning. Recently, our group has shown that MMP blockade disrupts LTP maintenance also in the mossy fiber-CA3 (mf-CA3) projection (Wojtowicz and Mozrzymas, 2010), where LTP mechanisms are profoundly different (NMDAR-independent and presynaptic expression site). However, how plasticity of this pathway correlates with activity and expression of MMPs remains unknown. Interestingly, several potential MMP substrates (especially of gelatinases) are localized intracellularly but little is known about MMP activity in this compartment. In the present study we have asked whether LTP is associated with the expression and activity of gelatinases in apparent intra- and extracellular compartments along mf-CA3 projection. In situ zymography showed that LTP induction was associated with increased gelatinases activity in the cytoplasm of the hilar and CA3 neurons. Using gelatin zymography, immunohistochemistry and immunofluorescent staining we found that this effect was due to de novo synthesis and activation of MMP-9 which, 2-3h after LTP induction was particularly evident in the cytoplasm. In contrast, MMP-2 was localized preferentially in the nuclei and was not affected by LTP induction. In conclusion, we demonstrate that LTP induction in the mf-CA3 pathway correlates with increased expression and activity of MMP-9 and provide the first evidence that this increase is particularly evident in the neuronal cytoplasm and nucleus.

Original languageEnglish
JournalMolecular and Cellular Neuroscience
Volume50
Issue2
Pages (from-to)147-59
Number of pages13
ISSN1044-7431
DOIs
Publication statusPublished - Jun 2012

Bibliographical note

Copyright © 2012 Elsevier Inc. All rights reserved.

    Research areas

  • Animals, CA3 Region, Hippocampal/enzymology, Excitatory Postsynaptic Potentials/physiology, Long-Term Potentiation/physiology, Matrix Metalloproteinase 9/biosynthesis, Matrix Metalloproteinases/metabolism, Mossy Fibers, Hippocampal/enzymology, Rats, Rats, Wistar

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