TY  - JOUR
AU  - Varga, Edina
AU  - Juhász, Gábor
AU  - Bozsó, Zsolt
AU  - Penke, Botond
AU  - Fülöp, Lívia
AU  - Szegedi, Viktor
TI  - Abeta(1-42) Enhances Neuronal Excitability in the CA1 via NR2B Subunit-Containing NMDA Receptors
JF  - NEURAL PLASTICITY
J2  - NEURAL PLAST
VL  - 2014
PY  - 2014
PG  - 12
SN  - 2090-5904
DO  - 10.1155/2014/584314
UR  - https://m2.mtmt.hu/api/publication/2755870
ID  - 2755870
AB  - Neuronal hyperexcitability is a phenomenon associated with early Alzheimer's disease. The underlying mechanism is considered to involve excessive activation of glutamate receptors; however, the exact molecular pathway remains to be determined. Extracellular recording from the CA1 of hippocampal slices is a long-standing standard for a range of studies both in basic research and in neuropharmacology. Evoked field potentials (fEPSPs) are regarded as the input, while spiking rate is regarded as the output of the neuronal network; however, the relationship between these two phenomena is not fully clear. We investigated the relationship between spontaneous spiking and evoked fEPSPs using mouse hippocampal slices. Blocking AMPA receptors (AMPARs) with CNQX abolished fEPSPs, but left firing rate unchanged. NMDA receptor (NMDAR) blockade with MK801 decreased neuronal spiking dose dependently without altering fEPSPs. Activating NMDARs by small concentration of NMDA induced a trend of increased firing. These results suggest that fEPSPs are mediated by synaptic activation of AMPARs, while spontaneous firing is regulated by the activation of extrasynaptic NMDARs. Synaptotoxic Abeta(1-42) increased firing activity without modifying evoked fEPSPs. This hyperexcitation was prevented by ifenprodil, an antagonist of the NR2B NMDARs. Overall, these results suggest that Abeta(1-42) induced neuronal overactivity is not dependent on AMPARs but requires NR2B.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Papp, Edit
AU  - Rivera, C
AU  - Kaila, K
AU  - Freund, Tamás
TI  - Relationship between neuronal vulnerability and potassium-chloride cotransporter 2 immunoreactivity in hippocampus following transient forebrain ischemia
JF  - NEUROSCIENCE
J2  - NEUROSCIENCE
VL  - 154
PY  - 2008
IS  - 2
SP  - 677
EP  - 689
PG  - 13
SN  - 0306-4522
DO  - 10.1016/j.neuroscience.2008.03.072
UR  - https://m2.mtmt.hu/api/publication/109992
ID  - 109992
N1  - Cited By :52            
            Export Date: 12 March 2020            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: Academy of Finland            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institutes of Health, NIH, NS30549            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
Cited By :52            
            Export Date: 24 May 2020            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: Academy of Finland            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institutes of Health, NIH, NS30549            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
Cited By :52            
            Export Date: 28 May 2020            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: Academy of Finland            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institutes of Health, NIH, NS30549            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
Cited By :54            
            Export Date: 30 December 2020            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: Academy of Finland            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institutes of Health, NIH, NS30549            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
Cited By :55            
            Export Date: 1 April 2021            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: National Institutes of Health, NIH            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institute of Neurological Disorders and Stroke, NINDS, R01NS030549            
            Funding details: Academy of Finland            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
Cited By :55            
            Export Date: 6 April 2021            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: National Institutes of Health, NIH            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institute of Neurological Disorders and Stroke, NINDS, R01NS030549            
            Funding details: Academy of Finland            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
Cited By :55            
            Export Date: 20 April 2021            
            CODEN: NRSCD            
            Correspondence Address: Freund, T.F.; Institute of Experimental Medicine, P.O.B. 67, Budapest, H-1450, Hungary; email: freund@koki.hu            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; parvalbumin, 56094-12-3, 83667-75-8; Chlorides; gamma-Aminobutyric Acid, 56-12-2; HSP72 Heat-Shock Proteins; sodium-potassium chloride cotransporter 2 protein; Sodium-Potassium-Chloride Symporters            
            Funding details: National Institutes of Health, NIH            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: National Institute of Neurological Disorders and Stroke, NINDS, R01NS030549            
            Funding details: Academy of Finland            
            Funding details: Hungarian Scientific Research Fund, OTKA, T46820            
            Funding text 1: The excellent technical assistance of E. Simon and Gy Goda is also acknowledged. This study was supported by the Howard Hughes Medical Institute (T.F.F.), Szentágothai Knowledge Centre (T.F.F.), NIH, NS30549 (T.F.F.), OTKA T46820 (T.F.F.), and by the Academy of Finland (K.K., C.R.) E. P. is a grantee of the János Bólyai scholarship.
AB  - Cation chloride cotransporters have been reported to be expressed in neurons in the hippocampus and to regulate intracellular Cl(-) concentration. The neuron-specific K-Cl cotransporter 2 (KCC2) is necessary for maintaining the low intracellular chloride concentration required for the hyperpolarizing actions of GABA. In this study we examined the vulnerability of KCC2-containing neurons as well as the changes in the pattern of KCC2 distribution in the rat hippocampus following 15 min ischemia induced by four-vessel occlusion. Immunostaining for the 72 kDa heat shock protein (HSP-72) was used to investigate the extent of damage in neuronal populations previously shown to be vulnerable to ischemia. At 6-24 h after ischemia, when the pyramidal cells in the CA1 (subfield of cornu Ammonis) region showed no morphological signs of damage, a small rise of KCC2 immunoreactivity was already observed. After 2 days, when the CA1 pyramidal cells started to degenerate, a progressive downregulation of the KCC2 protein was visible. Interestingly, in the same areas, the parvalbumin containing interneurons showed no signs of ischemic damage, and KCC2 immunoreactivity was retained on their membrane surface. In CA1 pyramidal cells, the reduction in KCC2 expression may lead to an elevation of intracellular Cl(-) concentration, which causes a shift in equilibrium potential toward more positive levels. Consequently, the reduction of the inhibitory action of GABA through downregulation of KCC2 function may be involved in the pathomechanisms of delayed neuronal death in the CA1 subfield.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Rivera, C
AU  - Voipio, J
AU  - Thomas-Crusells, J
AU  - Li, H
AU  - Emri, Zsuzsa
AU  - Sipila, S
AU  - Payne, JA
AU  - Minichiello, L
AU  - Saarma, M
AU  - Kaila, K
TI  - Mechanism of activity-dependent downregulation of the neuron-specific K-Cl cotransporter KCC2.
JF  - JOURNAL OF NEUROSCIENCE
J2  - J NEUROSCI
VL  - 24
PY  - 2004
IS  - 19
SP  - 4683
EP  - 4691
PG  - 9
SN  - 0270-6474
DO  - 10.1523/JNEUROSCI.5265-03.2004
UR  - https://m2.mtmt.hu/api/publication/2287575
ID  - 2287575
N1  - Megjegyzés-25140151
N1 Molecular Sequence Numbers: GENBANK: AA982489;
Megjegyzés-25140616
N1 Molecular Sequence Numbers: GENBANK: AA982489;
Department of Biosciences, University of Helsinki, Helsinki, FIN-00014, Finland            
            Institute of Biotechnology, University of Helsinki, Helsinki, FIN-00014, Finland            
            Department of Human Physiology, Univ. of California Sch. of Medicine, Davis, CA 95616, United States            
            Europ. Molecular Biology Laboratory, 00016 Monterotondo, Italy            
            Institute of Biotechnology, P.O. Box 56, University of Helsinki, FIN-00014, Finland            
            Chemical Research Center, H-1025 Budapest, Hungary            
            Cited By :336            
            Export Date: 12 March 2020            
            CODEN: JNRSD            
            Correspondence Address: Rivera, C.; Institute of Biotechnology, P.O. Box 56, University of Helsinki, FIN-00014, Finland; email: Claudio.Rivera@helsinki.fi            
            Molecular Sequence Numbers: GENBANK: AA982489;            
            Chemicals/CAS: brain derived neurotrophic factor, 218441-99-7; cyclic AMP responsive element binding protein binding protein, 190209-80-4; phospholipase C, 9001-86-9; potassium ion, 24203-36-9; Adaptor Proteins, Signal Transducing; Adaptor Proteins, Vesicular Transport; Brain-Derived Neurotrophic Factor; Chlorides; Cyclic AMP Response Element-Binding Protein; Magnesium, 7439-95-4; Phospholipase C gamma, EC 3.1.4.3; Phospholipase C, EC 3.1.4.3; potassium-chloride symporters; Receptor, trkB, EC 2.7.1.112; RNA, Messenger; Src homology 2 domain-containing, transforming protein 1; Symporters
Department of Biosciences, University of Helsinki, Helsinki, FIN-00014, Finland            
            Institute of Biotechnology, University of Helsinki, Helsinki, FIN-00014, Finland            
            Department of Human Physiology, Univ. of California Sch. of Medicine, Davis, CA 95616, United States            
            Europ. Molecular Biology Laboratory, 00016 Monterotondo, Italy            
            Institute of Biotechnology, P.O. Box 56, University of Helsinki, FIN-00014, Finland            
            Chemical Research Center, H-1025 Budapest, Hungary            
            Cited By :357            
            Export Date: 6 April 2021            
            CODEN: JNRSD            
            Correspondence Address: Rivera, C.; Institute of Biotechnology, P.O. Box 56, University of Helsinki, FIN-00014, Finland; email: Claudio.Rivera@helsinki.fi            
            Molecular Sequence Numbers: GENBANK: AA982489;            
            Chemicals/CAS: brain derived neurotrophic factor, 218441-99-7; cyclic AMP responsive element binding protein binding protein, 190209-80-4; phospholipase C, 9001-86-9; potassium ion, 24203-36-9
AB  - GABA-mediated fast-hyperpolarizing inhibition depends on extrusion of chloride by the neuron-specific K-Cl cotransporter, KCC2. Here we show that sustained interictal-like activity in hippocampal slices downregulates KCC2 mRNA and protein expression in CA1 pyramidal neurons, which leads to a reduced capacity for neuronal Cl- extrusion. This effect is mediated by endogenous BDNF acting on tyrosine receptor kinase B (TrkB), with down-stream cascades involving both Shc/FRS-2 (src homology 2 domain containing transforming protein/FGF receptor substrate 2) and PLCgamma (phospholipase Cgamma)-cAMP response element-binding protein signaling. The plasmalemmal KCC2 has a very high rate of turnover, with a time frame that suggests a novel role for changes in KCC2 expression in diverse manifestations of neuronal plasticity. A downregulation of KCC2 may be a general early response involved in various kinds of neuronal trauma.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Coull, JA
AU  - Boudreau, D
AU  - Bachand, K
AU  - Prescott, SA
AU  - Nault, F
AU  - Sík, Attila
AU  - De Koninck, P
AU  - De Koninck, Y
TI  - Trans-synaptic shift in anion gradient in spinal lamina I neurons as a mechanism of neuropathic pain.
JF  - NATURE
J2  - NATURE
VL  - 424
PY  - 2003
IS  - 6951
SP  - 938
EP  - 942
PG  - 5
SN  - 0028-0836
DO  - 10.1038/nature01868
UR  - https://m2.mtmt.hu/api/publication/3301448
ID  - 3301448
N1  - Export Date: 27 January 2024; CODEN: NATUA
AB  - Modern pain-control theory predicts that a loss of inhibition (disinhibition) in the dorsal horn of the spinal cord is a crucial substrate for chronic pain syndromes. However, the nature of the mechanisms that underlie such disinhibition has remained controversial. Here we present evidence for a novel mechanism of disinhibition following peripheral nerve injury. It involves a trans-synaptic reduction in the expression of the potassium-chloride exporter KCC2, and the consequent disruption of anion homeostasis in neurons of lamina I of the superficial dorsal horn, one of the main spinal nociceptive output pathways. In our experiments, the resulting shift in the transmembrane anion gradient caused normally inhibitory anionic synaptic currents to be excitatory, substantially driving up the net excitability of lamina I neurons. Local blockade or knock-down of the spinal KCC2 exporter in intact rats markedly reduced the nociceptive threshold, confirming that the reported disruption of anion homeostasis in lamina I neurons was sufficient to cause neuropathic pain.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Nusser, Zoltán
AU  - Hájos, Norbert
AU  - Somogyi, Péter Pál
AU  - Mody, I
TI  - Increased number of synaptic GABA~A receptors underlies potentiation at hippocampal inhibitory synapses
JF  - NATURE
J2  - NATURE
VL  - 395
PY  - 1998
IS  - 6698
SP  - 172
EP  - 177
PG  - 6
SN  - 0028-0836
DO  - 10.1038/25999
UR  - https://m2.mtmt.hu/api/publication/108650
ID  - 108650
AB  - Changes in synaptic efficacy are essential far neuronal development(1), learning and memory formation(2) and for pathological slates of neuronal excitability, including temporal-lobe epilepsy(3), At synapses, where there is a high probability of opening of postsynaptic receptors(4), all of which are occupied by the released transmitter(5-9), the most effective means of augmenting postsynaptic responses is to increase the number of receptors(2,10,11). Here we combine quantal analysis of evoked inhibitory postsynaptic currents with quantitative immunogold localization of synaptic GABA(A) receptors in hippocampal granule cells in order to clarify the basis of inhibitory synaptic plasticity induced by an experimental model of temporal-lobe epilepsy (a process known as kindling)(10). We find that the larger amplitude (66% increase) of elementary synaptic currents (quantal size) after kindling results directly from a 75% increase in the number of GABA(A) receptors at inhibitory synapses on somata and axon initial segments. Receptor density was up by 34-40% and the synaptic junctional area was expanded by 31%. Presynaptic boutons were enlarged, which may account for the 39% decrease in the average number of released transmitter packets (quantal content). Our findings establish the postsynaptic insertion of new GABA(A) receptors and the corresponding increase in postsynaptic responses augmenting the efficacy of mammalian inhibitory synapses.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Nusser, Zoltán
AU  - Sieghart, W
AU  - Somogyi, Péter Pál
TI  - Segregation of different GABA~A receptors to synaptic and extrasynaptic membranes of cerebellar granule cells
JF  - JOURNAL OF NEUROSCIENCE
J2  - J NEUROSCI
VL  - 18
PY  - 1998
IS  - 5
SP  - 1693
EP  - 1703
PG  - 11
SN  - 0270-6474
DO  - 10.1523/jneurosci.18-05-01693.1998
UR  - https://m2.mtmt.hu/api/publication/108772
ID  - 108772
AB  - Two types of GABA(A) receptor-mediated inhibition (phasic and tonic) have been described in cerebellar granule cells, although these cells receive GABAergic input only from a single cell type, the Golgi cell. In adult rats, granule cells express six GABA(A) receptor subunits abundantly (alpha 1, alpha 6, beta 2, beta 3, gamma 2, and delta), which are coassembled into at least four to six distinct GABA(A) receptor subtypes. We tested whether a differential distribution of GABA(A) receptors on the surface of granule cells could play a role in the different forms of inhibition, assuming that phasic inhibition originates from the activation of synaptic receptors, whereas tonic inhibition is provided mainly by extrasynaptic receptors. The alpha 1, alpha 6, beta 2/3, and gamma 2 subunits have been found by immunogold localizations to be concentrated in GABAergic Golgi synapses and also are present in the extrasynaptic membrane at a lower concentration. In contrast, immunoparticles for the delta subunit could not be detected in synaptic junctions, although they were abundantly present in the extrasynaptic dendritic and somatic membranes. Gold particles for the alpha 6, gamma 2, and beta 2/3, but not the alpha 1 and delta, subunits also were concentrated in some glutamatergic mossy fiber synapses, where their colocalization with AMPA-type glutamate receptors was demonstrated. The exclusive extrasynaptic presence of the delta subunit-containing receptors, together with their kinetic properties, suggests that tonic inhibition could be mediated mainly by extrasynaptic alpha(6) beta(2/3)delta receptors, whereas phasic inhibition is attributable to the activation of synaptic alpha(1) beta(2/3)gamma(2), alpha(6) beta(2/3)gamma(2), and alpha(1) alpha(6) beta(2/3)gamma(2) receptors.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Nusser, Zoltán
AU  - Cull-Candy, S
AU  - Farrant, M
TI  - Differences in synaptic GABA~A receptor number underlie variation in GABA mini amplitude
JF  - NEURON
J2  - NEURON
VL  - 19
PY  - 1997
SP  - 697
EP  - 709
PG  - 13
SN  - 0896-6273
DO  - 10.1016/S0896-6273(00)80382-7
UR  - https://m2.mtmt.hu/api/publication/108773
ID  - 108773
N1  - Department of Pharmacology, University College London, London WC1E 6BT, United Kingdom            
            Medical Research Council, Anatomical Neuropharmacology Unit, University of Oxford, Oxford 0X1 3TH, United Kingdom            
            Cited By :369            
            Export Date: 3 August 2023            
            CODEN: NERNE            
            Correspondence Address: Nusser, Z.; Department of Pharmacology, , London WC1E 6BT, United Kingdom            
            Chemicals/CAS: 4 aminobutyric acid, 28805-76-7, 56-12-2; bicuculline methobromide, 66016-70-4; flurazepam, 1172-18-5, 17617-23-1; tetrodotoxin, 4368-28-9, 4664-41-9            
            Funding details: Howard Hughes Medical Institute, HHMI            
            Funding details: Wellcome Trust, WT            
            Funding details: Medical Research Council, MRC            
            Funding text 1: This work was supported by the Medical Research Council, the Wellcome Trust, the Howard Hughes Medical Institute (International Scholars Award to S. C.-C.), and a European Commission Shared Cost RTD Programme Grant (number BIO 4 CT96–0585). We are grateful to Werner Sieghart and Peter Somogyi for providing antibody P16 and antiserum GABA number 9, respectively. We would like to thank Brian Edmonds, Matthew Frerking, Michael Häusser, David Rossi, Angus Silver, and Peter Somogyi for valuable discussions and David Attwell, Stephen Brickley, Akiko Momiyama, Angus Silver, and Peter Somogyi for comments on the manuscript. We would also like to thank Stephen Traynelis and Ioana Vais for provision of software and Zahida Ahmad, Juliann Thomas, Paul Jays, and Frank Kennedy for technical assistance.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Nusser, Zoltán
AU  - Sieghart, W
AU  - Stephenson, FA
AU  - Somogyi, Péter Pál
AU  - Sieghart, W
TI  - Theα6 subunit of the GABA~A receptor is concentrated in both inhibitory and excitatory synapses on cerebellar granule cells
JF  - JOURNAL OF NEUROSCIENCE
J2  - J NEUROSCI
VL  - 16
PY  - 1996
IS  - 1
SP  - 103
EP  - 114
PG  - 12
SN  - 0270-6474
DO  - 10.1523/jneurosci.16-01-00103.1996
UR  - https://m2.mtmt.hu/api/publication/108778
ID  - 108778
LA  - English
DB  - MTMT
ER  -