Marco Capogna

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

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Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway. / Wiera, Grzegorz; Wójtowicz, Tomasz; Lebida, Katarzyna et al.

In: Molecular and Cellular Neuroscience, Vol. 50, No. 2, 06.2012, p. 147-59.

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

Harvard

Wiera, G, Wójtowicz, T, Lebida, K, Piotrowska, A, Drulis-Fajdasz, D, Gomułkiewicz, A, Gendosz, D, Podhorska-Okołów, M, Capogna, M, Wilczyński, G, Dzięgiel, P, Kaczmarek, L & Mozrzymas, JW 2012, 'Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway', Molecular and Cellular Neuroscience, vol. 50, no. 2, pp. 147-59. https://doi.org/10.1016/j.mcn.2012.04.005

APA

Wiera, G., Wójtowicz, T., Lebida, K., Piotrowska, A., Drulis-Fajdasz, D., Gomułkiewicz, A., Gendosz, D., Podhorska-Okołów, M., Capogna, M., Wilczyński, G., Dzięgiel, P., Kaczmarek, L., & Mozrzymas, J. W. (2012). Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway. Molecular and Cellular Neuroscience, 50(2), 147-59. https://doi.org/10.1016/j.mcn.2012.04.005

CBE

Wiera G, Wójtowicz T, Lebida K, Piotrowska A, Drulis-Fajdasz D, Gomułkiewicz A, Gendosz D, Podhorska-Okołów M, Capogna M, Wilczyński G, et al. 2012. Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway. Molecular and Cellular Neuroscience. 50(2):147-59. https://doi.org/10.1016/j.mcn.2012.04.005

MLA

Vancouver

Wiera G, Wójtowicz T, Lebida K, Piotrowska A, Drulis-Fajdasz D, Gomułkiewicz A et al. Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway. Molecular and Cellular Neuroscience. 2012 Jun;50(2):147-59. https://doi.org/10.1016/j.mcn.2012.04.005

Author

Wiera, Grzegorz ; Wójtowicz, Tomasz ; Lebida, Katarzyna et al. / Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway. In: Molecular and Cellular Neuroscience. 2012 ; Vol. 50, No. 2. pp. 147-59.

Bibtex

@article{d387ef74680d4f86acac094dd56f74fa,
title = "Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway",
abstract = "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.",
keywords = "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",
author = "Grzegorz Wiera and Tomasz W{\'o}jtowicz and Katarzyna Lebida and Aleksandra Piotrowska and Dominika Drulis-Fajdasz and Agnieszka Gomu{\l}kiewicz and Daria Gendosz and Marzena Podhorska-Oko{\l}{\'o}w and Marco Capogna and Grzegorz Wilczy{\'n}ski and Piotr Dzi{\c e}giel and Leszek Kaczmarek and Mozrzymas, {Jerzy W}",
note = "Copyright {\textcopyright} 2012 Elsevier Inc. All rights reserved.",
year = "2012",
month = jun,
doi = "10.1016/j.mcn.2012.04.005",
language = "English",
volume = "50",
pages = "147--59",
journal = "Molecular and Cellular Neuroscience",
issn = "1044-7431",
publisher = "Academic Press",
number = "2",

}

RIS

TY - JOUR

T1 - Long term potentiation affects intracellular metalloproteinases activity in the mossy fiber-CA3 pathway

AU - Wiera, Grzegorz

AU - Wójtowicz, Tomasz

AU - Lebida, Katarzyna

AU - Piotrowska, Aleksandra

AU - Drulis-Fajdasz, Dominika

AU - Gomułkiewicz, Agnieszka

AU - Gendosz, Daria

AU - Podhorska-Okołów, Marzena

AU - Capogna, Marco

AU - Wilczyński, Grzegorz

AU - Dzięgiel, Piotr

AU - Kaczmarek, Leszek

AU - Mozrzymas, Jerzy W

N1 - Copyright © 2012 Elsevier Inc. All rights reserved.

PY - 2012/6

Y1 - 2012/6

N2 - 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.

AB - 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.

KW - Animals

KW - CA3 Region, Hippocampal/enzymology

KW - Excitatory Postsynaptic Potentials/physiology

KW - Long-Term Potentiation/physiology

KW - Matrix Metalloproteinase 9/biosynthesis

KW - Matrix Metalloproteinases/metabolism

KW - Mossy Fibers, Hippocampal/enzymology

KW - Rats

KW - Rats, Wistar

U2 - 10.1016/j.mcn.2012.04.005

DO - 10.1016/j.mcn.2012.04.005

M3 - Journal article

C2 - 22555058

VL - 50

SP - 147

EP - 159

JO - Molecular and Cellular Neuroscience

JF - Molecular and Cellular Neuroscience

SN - 1044-7431

IS - 2

ER -