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1

Matrix metalloproteinase activity regulates LTP through L-type voltage-gated calcium channel modulation

100%
Wiera G., Mozrzymas J. W.
Acta Neurobiologiae Experimentalis
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2014
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tom 74
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nr 3
Long-term synaptic plasticity at hippocampal CA3-CA1 synapses exhibit NMDAR- and L-type calcium channel (VDCC)- dependent components. To address the role of MMP proteases in mechanism of LTP induction, we used field potentials recordings in acute mice brain slices. LTP was induced by 200 Hz tetanus. We have found that MMP inhibitor (NNGH, inhibits mainly MMP-3) disrupts 200 Hz-LTP (CTR: 164±11%, n=9; NNGH: 117±7%, n=7, P<0.01). Next, we dissected two components of 200 Hz-LTP using nifedipine (L-type blocker) and APV (NMDAR inhibitor). MMP blockade with NNGH prevented only vdccLTP (nmdaLTP in the presence of nifedipine: 140±6%, n=8; nifedipine+NNGH: 141±8%, n=6 P=0.93; vdccLTP in the presence of APV: 168±27%, n=7; APV+NNGH: 110±13%, n=6, P<0.05). Our observations show that MMP activity (presumably MMP3) specifically regulates VDCC-dependent component of hippocampal LTP. Supported by NCN grants: NN401541540 and ETIUDA 2013/08/T/ NZ3/00999.
2

MMP-3 and MMP-9 divergently regulate LTP in hippocampal mosy fiber-CA3 and CA3-CA1 projections

100%
Wiera G., Mozrzymas J. W.
Acta Neurobiologiae Experimentalis
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2013
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tom 73
|
nr Suppl.1
Matrix metalloproteinases (MMPs) comprise a family of proteolytic enzymes that modify membrane and extracellular matrix proteins. Broad-spectrum MMP inhibitors were shown to impair LTP consolidation in two hippocampal projections: mossy fiber (MF)-CA3 and CA3-CA1 which deeply differ in LTP induction as well as in expression sites and induction mechanisms. The aim of this study was to address the specific roles of MMP-3 and gelatinases in LTP in these projections. Using field potentials recording in acute mice brain slices we have shown that specific MMP-3 inhibitor (NNGH) disrupts LTP late phase in CA3-CA1 pathway (NNGH: 119 ± 10% of baseline two hours after induction, n=9; CTR: 177 ± 29%, n=8; P=0.01) but does not affect LTP in MF-CA3 (NNGH: 186 ± 27%, n=7; CTR: 172 ± 11%; n=7, P=0.34). Another MMP-3 inhibitor UK356618 gave similar results. Interestingly, knock-out mice without functional MMP-9 show impaired long term plasticity in MF-CA3 pathway (KO: 115 ± 17%, n=8; CTR 181 ± 13%, n=13; P<0.01) and a weak if any change in LTP in CA3-CA1 projection (KO: 139 ± 8%, n=7; CTR: 159 ± 13%, n=8; P=0.22). These results suggest that the role of particular MMPs in LTP expression is not universal in considered projections. Moreover, we provide the first evidence that MMP-3 and MMP-9 proteases differentially modify LTP consolidation in the MF-CA3 and CA3-CA1 pathways. Support: NCN grant N N401541540.
3

Impact of metaloproteases on synaptic and E+S plasticity in the hippocampal mosy fiber–CA3 and AC path ways

81%
Morrzymas J. W., Wiera G., Wojtowicz T.
Acta Neurobiologiae Experimentalis
|
2013
|
tom 73
|
nr Suppl.1
Learning and synaptic plasticity is known to involve activity of metalloproteinases (MMPs). Recently, we investigated impact of MMPs on mossy fiber-CA3 (mf-CA3) projection, where LTP is NMDAR-independent and presynaptic, and showed that MMP blockade disrupted LTP maintenance. Using in situ zymography we showed that LTP induction enhances gelatinases activity. Moreover, by means of gelatin zymography, immunohistochemistry and immunofluorescent staining we have shown that this was due to de novo synthesis and activation of MMP-9 (but not MMP-2). Next we found that manipulations in endogenous MMP-9 affected LTP in the mf-CA3 projection. Intriguingly, in slices from both MMP-9 KO and overexperssing rodents, LTP maintenance was nearly abolished. In KO group, LTP could be rescued by administration of active MMP-9. This suggests that LTP maintenance in mf-CA3 pathway requires fine-tuned MMP-9 activity. Neuronal plasticity may involve also changes in excitability and we addressed this issue in associational/commissural synapses formed between CA3 pyramidal neurons. We found that MMPs (MMP-3 and gelatinases) inhibition significantly reduced EPSP-to-spike (E-S) and spike coherence upon LTP indution. Altogether, we show that MMPs play a crucial role in controlling various facets of neuronal plasticity in the mf-CA3 hippocampal projection. Support: NCN grant NN401541540.
4

Fine-tuned MMP-9 activity level is a premissive factor for induction and maintenance of LTP in hippocampal mossy fiber-CA3 pathway

81%
Wiera G., Dziegiel P., Kaczmarek L., Mozrzymas J. W.
Acta Neurobiologiae Experimentalis
|
2012
|
tom 72
|
nr 2
Matrix metalloproteinases have been implicated in physiological and pathological functions of neuronal networks. To get an insight into the specific role of protease MMP-9 in the plasticity of the mossy fiber-CA3 pathway (mf-CA3), we used field recordings to measure LTP in slices from wild type, MMP-9 KO and overexpressing (OVX) animals. Both lack of protease (KO) and its overexpression impaired the early and maintenance phase of mf-CA3 LTP (128% vs. 181% of respective baseline in KO and WT mice; and 136% vs. 189% in OVX and WT rats respectively, P<0.05). Importantly, impaired LTP in transgenic rodents could be rescued by administration of recombinant MMP-9 to the KO slices (152% of respective baseline). Moreover, autoactive MMP-9 protein application induced a stable autopotentiation of synaptic response in KO and WT mice. β-dystroglycan is a synaptic membrane protein and its MMP-mediated cleavage has been described during pathological, epileptic activity. In mf-CA3 pathway we observed a MMP-dependent significant decrease in 30 kDa β-dystroglycan digestion product as early as 5 minutes after LTP induction. Altogether, these results suggest that in mfCA3 pathway during first minutes after tetanus fine-tuned level of MMP-9 activity acts as a permissive factor for LTP establishment. Supported by Polish Ministry for Science and Higher Education grant N N401 541540.
5

GABAergic plasticity in hippocampus depends on the activity of matrix metalloprotease‑3

81%
Lech A., Buszka A., Mozrzymas J. W., Wiera G.
Acta Neurobiologiae Experimentalis
|
2019
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tom 79
|
nr Suppl.1
INTRODUCTION: Formation of memory traces, and thus learning, strongly relies on the interplay between different forms of neuronal plasticity. While much is known about the plasticity of glutamatergic synapses, plasticity of synaptic inhibition awaits deeper investigations. AIM(S): The aim of this study was to address the function of extracellular proteolysis mediated by matrix metalloprotease‑3 (MMP‑3) in GABAergic plasticity. METHOD(S): We recorded mIPSCs in hippocampal culture and induced inhibitory LTP (iLTP) using NMDA in the presence of MMP‑3 inhibitor UK‑356618. Additionally, we studied changes in morphology of GABAergic synapses and membrane lateral mobility of GABAARs. RESULTS: Obtained results clearly show that, in the presence of UK or in MMP-3 deficient neurons, iLTP is abolished (WT: 116%; UK: 96%, n=8‑9, p=0.02). Concurrently, we observed a significant increase in synaptic gephyrin cluster area after iLTP induction in controls (WT: 121%, n=23) but not in the presence of UK (98%, n=25, p<0.01). We also investigated the effects of exogenous active MMP-3 on synaptic morphology, membrane mobility of GABAA receptors, and the amplitude of mIPSC. Short‑term MMP‑3 application augments mIPSC amplitude up to 121% of initial value (n=11, p<0.01) and increases the average size of synaptic gephyrin cluster (108%, n=16, p<0.05). In addition, analysis of membrane mobility of synaptic GABAARs showed a decrease in their diffusion coefficient after MMP-3 treatment (before: 0.019µm2 /s; after MMP‑3: 0.015µm2 /s, p<0.01) indicating the strengthening of inhibitory synapses through receptor trapping. CONCLUSIONS: These results demonstrate a crucial role of MMP-3 in the induction of iLTP both at functional and morphological level opening new avenues in the study of plasticity cross-talk between different synapses. Additionally, presented results significantly expand our knowledge on the local interplay between extracellular matrix and inhibitory synapses. FINANCIAL SUPPORT: NCN grant 2017/26/D/ NZ4/00450.
6

Activity of MMP-3 protease affects exicitatory and inhibitory synaptic transmission in hippocampus

81%
Wiera G., Petrini E., Barberis A., Mozrzymas J. W.
Acta Neurobiologiae Experimentalis
|
2015
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tom 75
|
nr Supl.
BACKGROUND AND AIMS: Several neuronal processes are regulated by matrix metalloproteinases (MMPs), a family of zincdependent proteases. It is well established that long-term synaptic plasticity, learning and memory involve extracellular activity of MMPs but the role of some of them is not fully identified. The aim of this study was to address the functions of MMP-3 in synaptic plasticity of excitatory and inhibitory synaptic transmission. METHODS: Field potentials recordings in acute mice hippocampal slices and single molecule-tracking of GABAA receptors in neuronal cultures. RESULTS: We have shown that in MMP-3 knock-out mice lateLTP is impaired in CA3-CA1 projection (WT: 180±10% of baseline 2 h after induction, n=15; KO: 134±12%, n=16; P<0.01). Treatment of wild-type slices with SB3CT (a specific MMP-9 inhibitor) also blocked late-LTP, without affecting early phase of LTP These observations suggest that both MMP-9 and MMP-3 together may regulate the maintenance of LTP. We next determined whether impaired late-LTP in MMP-3 KO slices is further weakened by MMP-9 inhibition with SB3CT. Knockout of MMP-3 together with MMP-9 blockade (SB-3CT) caused a strong reduction in  both early and late LTP phases [WT: 170±8% of baseline 20 min after induction, n=16; MMP-3 KO: 157±8%, n=17; MMP-3 KO+SB-3- CT: 138±6%, n=8; P(WT vs. MMP-3 KO)=0.26, P(WT vs. MMP-3 KO+SB-3CT)=0.01]. Additionally, we studied the role of MMP-3 in inhibitory transmission using single molecule tracking of GABAA receptors (α1 subunit). We have found that 10 or 45 min treatment with active MMP-3 protein decreased the diffusion coefficient of both synaptic and extrasynaptic GABAA receptors (P<0.01). CONCLUSIONS: Our observations indicate that activity of MMP-3 is necessary for LTPmaintenance and suggest that MMP-3 regulates membrane mobility of GABA receptors. Future work is needed to elucidate the impact of MMP-3 on plasticity of inhibitory synapses. Support: NCN grants NN401541540, 2013/08/T/NZ3/00999.
7

GABAergic hippocampal plasticity critically depends on matrix metalloproteinase 3

71%
Mozrzymas J. W., Brzdak P., Lebida K., Lech A., Wiera G.
Acta Neurobiologiae Experimentalis
|
2019
|
tom 79
|
nr Suppl.1
Matrix metalloproteinases (MMPs) are known to play a crucialrole in neuronal plasticity. In particular, MMP‑3 has been reported to be involved in glutamatergic plasticity and related cognitive processes. Recently, a growing body of evidence indicates that GABAergic synapses are also plastic, but the underlying mechanisms remain elusive. Herein we addressed the question if the activity of MMP-3 is involved in GABAergic synaptic plasticity in mice acute hippocampal slices or in neuronal cultures. The presentation at symposium aims to offer an overview of experimental evidence obtained by our research group while more details will be presented at the posters. We performed whole‑cell patch‑clamp recordings of miniature inhibitory postsynaptic currents (mIPSCs) from hippocampal CA1 pyramidal neurons. To induce inhibitory LTP (iLTP), we applied NMDA in bath solution (3 min, 20µM) in the presence of 20 μM DNQX and 1μM TTX to slices or neuronal cultures from wild‑type (WT) animals and mice lacking mmp‑3 gene (MMP‑3 KO). To block the activity of MMP-3 we used inhibitor UK 356618 (2 μM). Besides functional manifestations, iLTP induction was associated with a significant increase in synaptic gephyrin cluster area. We found that, in both slices and neuronal cultures, iLTP evoked in MMP-3 KO mice was completely abolished in contrast to WT. An analogous effect was observed when using UK356618. Interestingly, administration of active MMP-3 to neuronal cultures resulted in iLTP and an increase in average size of synaptic gephyrin cluster. In addition, analysis of membrane mobility of synaptic GABAARs showed a decrease in their diffusion coefficient after MMP-3 treatment indicating a strengthening of inhibitory synapses through receptor trapping. We show that the activity of MMP-3 plays a crucial role in iLTP in the hippocampal CA1 region. FINANCIAL SUPPORT: Supported by Polish National Science Centre grant SONATA 2017/26/D/NZ4/00450 and PB is supported by Polish National Science Centre scholarship ETIUDA 2018/28/T/NZ4/00344.
8

Role of metalloproteinases in synoptic plasticity in hippocampal mossy fiber-CA3 pathway

61%
Mozrzymas J. W., Wojtowicz T., Wiera G., Gendosz D., Chmielewska M., Wawrzyniak M.
Acta Neurobiologiae Experimentalis
|
2011
|
tom 71
|
nr S
Matrix metalloproteinases (MMPs) are widely recognized as endopeptidases involved in remodeling of extracellular matrix. Last decade studies revealed these enzymes as important regulators of synaptic plasticity and cognitive processes. In particular, MMPs inhibition led to impairment of hippocampus-dependent learning and to down regulation of long-term potentiation (LTP) maintenance in the Schaffer collateral– CA1 (SC-CA1) pathway. However, the impact of MMPs on plasticity in other hippocampal paths was not known. In our recent studies, we have we addressed the impact of MMPs on plasticity in mossy fiber-CA3 (mf-CA3) projection in which, in contrast to SC-CA1, LTP expression in presynaptic. We found that pharmacological blockade of MMPs nearly abolished the late phase of LTP. Induction of LTP resulted in increased immunoreactivity for MMP-9 and enhanced gelatinase activity (in situ zymography) and these effects were associated with up regulation of de novo expression of active and latent MMP-9 forms (gel zymography). Interestingly, the late phase of LTP in the mf-CA3 pathway was reduced both in the MMP-9 KO mice and in rats overexpressing MMP-9. This finding indicates that maintenance of synaptic plasticity requires an optimal, finely tuned MMP-9 activity level. Pyramidal neurons in the CA3 region form a dense autoassociative network due to associational/commissural (AC) projections and plasticity mechanisms in AC and mf-CA3 synapses are different. Recently, we found that the late LTP phase in the AC synapses is also impaired by MMPs inhibition. Moreover, EPSC-spike potentiation in the CA3 region is strongly down regulated by MMPs blockade. In conclusion, MMPs appear to play a universal role in consolidation of synaptic plasticity in various hippocampal pathways characterized by different mechanisms of synaptic plasticity. Supported by Ministry for Science and Higher Education grants PN/030/2006 and N N401 541540.
9

STIM1, STIM2 and Orai1-overexpression of key store operated calcium entry in transgenic mice brain

61%
Majewski L., Wiera G., Wojtowicz T., Boguszewski P. M., Mozrzymas J., Kuznicki J.
Acta Neurobiologiae Experimentalis
|
2015
|
tom 75
|
nr Supl.
BACKGROUND AND AIMS: Alzheimer’s disease (AD) is the most common age-related neurodegenerative disorder. At least two types of AD can be distinguished: sporadic AD (SAD) of unknown etiology, which accounts for most cases, and genetically encoded familial AD (FAD), which affects up to 5% of all patients. Altered calcium homeostasis in neurons is proposed to be one of the early events responsible for AD. Disturbances in Ca2+ signaling are found in SAD patients before any obvious extracellular Aβ pathology; moreover, Ca2+ dysfunction augments Aβ formation and Tau hyperphosphorylation. One of the objectives of our present project is to understand how elevated basal Ca2+ level in neurons contributes to neurodegeneration. METHODS: Generation of transgenic mice using DNAmicroinjection technique. RESULTS: We have generated three transgenic mouse lines independently overexpressing,specifically in brain neurons, key proteins of SOCE – STIM1, STIM2 and Orai1. The phenotype of these mice is being analyzed by electrophysiology, behavior and Ca2+ imaging. Our group has shown that the cytoplasmic resting Ca2+ level in cultured neurons can be modulated by overexpression of STIM proteins, ER Ca2+ sensors involved in the Store Operated Calcium Entry (SOCE). We also detected the enhanced magnitude of Ca2+ influx during SOCE in human lymphocytes from SAD patients, and decreased level of STIM2 protein in human lymphocytes from FAD patients in parallel to an attenuation of SOCE. CONCLUSIONS: The obtained lines can be a suitable model to verify the hypothesis that brain dysfunction during ageing is induced by changes in Ca2+ homeostasis.
10

Fine - tuned MMP-9 level is critical for LTP maintenance in mossy fiber - CA3 hippocampal pathway

61%
Wiera G., Wojtowicz T., Chmielewska M., Wawrzyniak M., Kaczmarek L., Dziegiel P., Mozrzymas J.
Acta Neurobiologiae Experimentalis
|
2011
|
tom 71
|
nr S
Matrix metalloproteinases (MMPs) are a family of endopeptidases involved in degradation and turnover of extracellular matrix proteins. Among them, MMP-9 is implicated in learning and synaptic plasticity. We have shown using inhibitor FN-439 that MMPs play a critical role in LTP maintenance in the mossy fiber - CA3 hippocampal projection (Wójtowicz and Mozrzymas 2010). In the present study we address the specific role of MMP-9 in the plasticity of this pathway. Gel zymography revealed an up regulation of pro- and active form of MMP-9 in homogenates from slice fragments containing mf-CA3 projection, fixed 2 h after LTP induction. Interestingly, this effect was abolished when LTP was induced in the presence of protein synthesis inhibitor (cycloheximide). Moreover, the effects of cycloheximide and FN-439 on fEPSPs were indistinguishable for up to 2 h after LTP induction. Additionally, we observed on western blot a significant decrease in 30 kDa β-dystroglycan digestion product 2 hours after LTP induction. To further explore the mechanism of MMP-9 action, LTP was induced in slices from MMP-9-/- and MMP-9 overexpressing rodents. In slices from KO mice, the late phase of LTP was severely impaired, although not abolished (136% vs. 189% in WT). Surprisingly, in slices from MMP-9 overexpressing rats, LTP was impaired in a similar manner as in KO mice (113% vs. 171%). Moreover, in MMP-9 overexpressing rats, LTP induction was accompanied by increase in MMP-9 level (shown by gel zymography) similar to what was observed in WT rats. These results indicate that fine-tuned MMP-9 balance is critical for LTP consolidation in mf-CA3 pathway, as in the absence of MMP-9 or in conditions of its excess, LTP is impaired. These results may raise a possibility that impairment of optimal MMP-9 activity (implicated in schizophrenia or bipolar mood disorder) may be detrimental for cognitive processes. Supported by Ministry for Science and Higher Education grants PN/030/2006 and N N401 541540.
11
Content available remote

Impact of matrix metalloproteinase-9 overexpression on synaptic excitatory transmission and its plasticity in rat Ca3-Ca1 hippocampal pathway

61%
Wiera G., Szczot M., Wojtowicz T., Lebida K., Koza P., Mozrzymas J. W.
Journal of Physiology and Pharmacology
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2015
|
tom 66
|
nr 2
12

Long-term gabaergic synaptic plasticity in hippocampus strongly depends on the activity of matrix metalloproteinase-3

61%
Brzdak P., Lebida K., Lech A., Nowak D., Wiera G., Mozrzymas J. W.
Acta Neurobiologiae Experimentalis
|
2018
|
tom 78
|
nr Suppl.1
It is well established that matrix metalloproteinases (MMPs) play an important role in mechanisms of excit‑ atory plasticity, learning, and memory, especially those dependent on hippocampus. Recently, we have demon‑ strated that MMP-9, but not MMP-3, is involved in spike timing-dependent plasticity in mouse barrel cortex, and that MMP-3 supports NMDA-dependent LTP in the hip‑ pocampus. However, the contribution of these enzymes to GABAergic plasticity has not been investigated. To ad‑ dress this issue, we recorded miniature inhibitory post‑ synaptic currents (mIPSC) in acute hippocampal slices (P18-P21) and induced inhibitory LTP (iLTP) using NMDA treatment (3 min, 20 μM) in control conditions and in the presence of MMP inhibitors: FN-439 (180 µM), SB3‑CT (10 μM) and UK356618 (2 μM). Additionally, we performed immunostaining (against gephyrin and vGAT) of cultured hippocampal neurons and examined the level of MMP-3 using Western blot in hippocampal slice homogenates af‑ ter iLTP. We have shown that, in control conditions, ac‑ tivation of NMDA receptor significantly potentiated am‑ plitude (122±8%) and prolonged decay kinetics (125±7%) of mIPSC and also increased pro-MMP-3 levels (116±4%). Application of pan-MMP inhibitor (FN‑439) prevent‑ ed induction of iLTP (CTR: 122±8%, n=7; FN-439: 98±6%, n=7; p<0.05). Interestingly, MMP-3 inhibitor treatment (UK356618) blocked iLTP, but MMP‑9 inhibitor (SB3-CT) had no effect on iLTP (UK356618: 92±3%; n=7, p<0.05; SB3CT: 121±12%, n=6, p>0.05; in comparison to CTR: 122±8%, n=7). Thus, our data show that MMP‑3, but not gelatinases, supports iLTP. Moreover, in the hippocampal slices from mice lacking the Mmp-3 gene (MMP-3 KO) iLTP is also af‑ fected by MMP-3 deficiency (CTR: 122±6%, n=8; MMP-3 KO: 99±4%, n=13; p<0.05). Intriguingly, we ascertained that in this model the decay kinetics of mIPSCs were significant‑ ly slowed down with respect to control measurements (CTR: 14.81±0.61 ms, n=11; MMP-3 KO: 18.31±0.99 ms, n=12; p<0.05). Similarly, iLTP was impaired in the MMP-3 KO group in hippocampal neuronal cultures. In addition, we observed a significant increase in synaptic gephyrin clus‑ ter area after iLTP (120±3%), but not after UK356618 treat‑ ment (99±3%) in neuronal cultures. Taken together, these data reveal that GABAergic LTP depends on extracellular proteolysis mediated by MMP-3. Supported by Polish Na‑ tional Science Centre grant OPUS/2014/15/B/NZ4/01689 and OPUS/2013/11/B/NZ3/00983.
13

Induction of long term potentiation in DG-CA3 hippocampal pathway results in increased MMP-2/9 gelatinolysis in target hilar and CA3 neurons

51%
Wojtowicz T., Gendosz D., Lebida K., Drulis-Fajdasz D., Wiera G., Caponga M., Wilczynski G., Dziegiel P., Mozrzymas J. W.
Acta Neurobiologiae Experimentalis
|
2011
|
tom 71
|
nr S
Matrix metalloproteinases (MMPs) are capable of remodeling extracellular matrix and have been implicated in synaptic plasticity, learning and memory. In particular, upregulation of gelatinases (MMP-2 and 9) accompanies long-term potentiation (LTP) in hippocampal Schaeffer collateral-CA1 pathway. However, the role of gelatinases in synaptic plasticity in other hippocampal pathways remains unknown. Recently, we have found that MMPs blockade by FN-439 abolishes LTP consolidation in the dentate gyrus-CA3 (DG-CA3) projection (where LTP expression is presynaptic, Wójtowicz and Mozrzymas 2010). To address the involvement of gelatinases in the plasticity of this pathway, we have combined high resolution in situ zymography with DQ-gelatin (DQ-G) and immunofluorescence in hippocampal sections from slices used in electrophysiological experiments. LTP was evoked by high frequency stimulation (HFS, 4×100 Hz) while baseline (control) stimulation was applied at 0.1 Hz. Following fixation, slices were cut into thin sections, treated with DQ-G and stained against a neuronal marker MAP-2. The intensity of DQ-G fluorescence was quantified for MAP-2 positive neurons using confocal microscopy. Computer- and visually-guided analysis of cytoplasm and proximal dendrites of target hilar and CA3 neurons revealed that LTP induction was associated with a significant increase in DQ-G fluorescence (30% and 35% increase, respectively, n=6 animals, p<0.05). Importantly, cytoplasmic DQ-G fluorescence profile corroborated with immunoreactivity for MMP-9. The overall DQ-G fluorescence signal in MAP-2 and GFAP-negative extracellular space did not differ between control and HFS-stimulated preparations (n=6 animals, p=0.89). In conclusion, we provide evidence that stimulation pattern that evokes LTP in the DG-CA3 pathway, induces a significant up regulation of gelatinases in the cytoplasm of postsynaptic hilar and CA3 neurons. Support: Grants NN401541540 and UDA-POKL.04.01.01-00-010/08-01.
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