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Conference Paper: Regulation of synaptic plasticity by the partnership of proheparanase with peri-synaptic heparan sulfate proteoglycan and AMPA-type glutamate receptor

TitleRegulation of synaptic plasticity by the partnership of proheparanase with peri-synaptic heparan sulfate proteoglycan and AMPA-type glutamate receptor
Authors
KeywordsLTP
Hippocampus
Heparan Sulfate
Issue Date2012
PublisherAmerican Society of Neuroscience.
Citation
The 42nd Annual Meeting of the Society for Neuroscience (SfN), New Orleans, USA, 13-17 October 2012 How to Cite?
AbstractPerineuronal heparan sulfates (HS) have been implicated in controlling the open-state of AMPA-type glutamate receptors (AMPARs) which govern excitatory synaptic transmission in the hippocampus. We hypothesize that neuronal mechanisms modulate peri-synaptic HS level and as a result regulate synaptic function. Our finding of neuronal heparanase expression in adult rats led us to test if neuronal heparanase is secreted to act on perineuronal HS, thereby contributing to synaptic plasticity. Following phorbol ester stimulation of hippocampal neurons in culture, Western blot analysis of the secreted product revealed proheparanase but not the active heparanase. Synaptosomes prepared from phorbol ester-treated cortex slices were enriched in proheparanase; co-immunoprecipitation studies further showed association of AMPAR subunits (GluA1 and GluA2/3) with both syndecan-3 (transmembrane HS-proteoglycan) and proheparanase, suggesting their clustering as a functional complex. Treatment of hippocampal neuron cultures with recombinant proheparanase triggered internalization of proheparanase, perineuronal HS-proteoglycans and AMPARs. Heparitinase pre-treated hippocampal neuron cultures showed reduced proheparanase-induced internalization of AMPARs, suggesting that proheparanase binds to syndecan-3 via the HS moiety. Consistent with these findings, treatment of hippocampal slices with exogenous proheparanase resulted in declines in both basal synaptic strength and LTP. Proheparanase treatment also prevented glutamate-induced calcium influx of the hippocampal neurons in culture. These results reveal a novel role of neuronal proheparanase in regulating synaptic plasticity by resetting AMPARs and perineuronal HS levels at the synapse. [Supported by HKRGC 774608]
DescriptionPoster Session 845.LTP: Physiology and Behavior
Program#845.23 & Poster#C18
Fulltext of the abstract in: http://www.abstractsonline.com/plan/ViewAbstract.aspx?cKey=6152216e-6e70-4272-90bb-bf96f79c83a8&mID=2964&mKey=%7b70007181-01C9-4DE9-A0A2-EEBFA14CD9F1%7d&sKey=68548d49-71b6-454f-8026-a7c9fa5670cc
Persistent Identifierhttp://hdl.handle.net/10722/165101

 

DC FieldValueLanguage
dc.contributor.authorMa, CWen_US
dc.contributor.authorLam, YLen_US
dc.contributor.authorCham, WCen_US
dc.contributor.authorChan, YSen_US
dc.contributor.authorShum, DKYen_US
dc.date.accessioned2012-09-20T08:14:46Z-
dc.date.available2012-09-20T08:14:46Z-
dc.date.issued2012en_US
dc.identifier.citationThe 42nd Annual Meeting of the Society for Neuroscience (SfN), New Orleans, USA, 13-17 October 2012en_US
dc.identifier.urihttp://hdl.handle.net/10722/165101-
dc.descriptionPoster Session 845.LTP: Physiology and Behavior-
dc.descriptionProgram#845.23 & Poster#C18-
dc.descriptionFulltext of the abstract in: http://www.abstractsonline.com/plan/ViewAbstract.aspx?cKey=6152216e-6e70-4272-90bb-bf96f79c83a8&mID=2964&mKey=%7b70007181-01C9-4DE9-A0A2-EEBFA14CD9F1%7d&sKey=68548d49-71b6-454f-8026-a7c9fa5670cc-
dc.description.abstractPerineuronal heparan sulfates (HS) have been implicated in controlling the open-state of AMPA-type glutamate receptors (AMPARs) which govern excitatory synaptic transmission in the hippocampus. We hypothesize that neuronal mechanisms modulate peri-synaptic HS level and as a result regulate synaptic function. Our finding of neuronal heparanase expression in adult rats led us to test if neuronal heparanase is secreted to act on perineuronal HS, thereby contributing to synaptic plasticity. Following phorbol ester stimulation of hippocampal neurons in culture, Western blot analysis of the secreted product revealed proheparanase but not the active heparanase. Synaptosomes prepared from phorbol ester-treated cortex slices were enriched in proheparanase; co-immunoprecipitation studies further showed association of AMPAR subunits (GluA1 and GluA2/3) with both syndecan-3 (transmembrane HS-proteoglycan) and proheparanase, suggesting their clustering as a functional complex. Treatment of hippocampal neuron cultures with recombinant proheparanase triggered internalization of proheparanase, perineuronal HS-proteoglycans and AMPARs. Heparitinase pre-treated hippocampal neuron cultures showed reduced proheparanase-induced internalization of AMPARs, suggesting that proheparanase binds to syndecan-3 via the HS moiety. Consistent with these findings, treatment of hippocampal slices with exogenous proheparanase resulted in declines in both basal synaptic strength and LTP. Proheparanase treatment also prevented glutamate-induced calcium influx of the hippocampal neurons in culture. These results reveal a novel role of neuronal proheparanase in regulating synaptic plasticity by resetting AMPARs and perineuronal HS levels at the synapse. [Supported by HKRGC 774608]-
dc.languageengen_US
dc.publisherAmerican Society of Neuroscience.-
dc.relation.ispartofNeuroscience 2012en_US
dc.subjectLTP-
dc.subjectHippocampus-
dc.subjectHeparan Sulfate-
dc.titleRegulation of synaptic plasticity by the partnership of proheparanase with peri-synaptic heparan sulfate proteoglycan and AMPA-type glutamate receptoren_US
dc.typeConference_Paperen_US
dc.identifier.emailMa, CW: cwma2010@hku.hken_US
dc.identifier.emailChan, YS: yschan@hku.hken_US
dc.identifier.emailShum, DKY: shumdkhk@hkucc.hku.hken_US
dc.identifier.authorityChan, YS=rp00318en_US
dc.identifier.authorityShum, DKY=rp00321en_US
dc.identifier.hkuros211310en_US
dc.publisher.placeUnited States-

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