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Conference Paper: Regulatory role of proheparanase with peri-synatpic heparan sulfate proteoglycan and AMPA-type glutamate receptor in synaptic plasticity

TitleRegulatory role of proheparanase with peri-synatpic heparan sulfate proteoglycan and AMPA-type glutamate receptor in synaptic plasticity
Authors
Issue Date2012
PublisherHKSN & BPHK.
Citation
The Hong Kong-Taiwan Physiology Symposium 2012 and Joint Scientific Meeting of Hong Kong Society of Neurosciences & The Biophysical Society of Hong Kong, Hong Kong, 14-15 June 2012. In Program Book of the Joint Scientific Meeting, 2012, p. 73-74, abstract P59 How to Cite?
AbstractAMPA-type glutamate receptors (AMPAR) govern excitatory synaptic transmission. Perineuronal heparan sulfates (HS) have been implicated in controlling the open-state of AMPAR. Our finding of neuronal heparanase expression in adult rats led us to test (1) if neuronal heparanase is secreted and (2) if the secreted form acts on perineuronal HS to modulate synaptic plasticity. Neuronal secretion of heparanase was triggered by phorbol ester of rat hippocampal neurons in culture. Western blot analysis of the secreted product revealed enzymatically inactive proheparanase, but not the enzymatically active heparanase. Synaptosomes prepared from phorbol ester-treated rat cortex slices showed enrichment in proheparanase; co-immunoprecipitation studies further showed association of AMPAR subunits (GluA1 and GluA2/3) with both syndecan-3 (a transmembrane HS-proteoglycan) and proheparanase, suggesting their partnership in the peri-synaptic environment. Treatment of hippocampal neurons in culture with recombinant proheparanase triggered internalization of proheparanase, perineuronal HS-proteoglycans and AMPARs, suggesting their clustering as a functional complex. Heparitinase pre-treatment of hippocampal neuron cultures reduced proheparanase-induced internalization of AMPARs, suggesting that the HS moiety is critical for effecting the partnership. Treatment of hippocampal slices with recombinant proheparanase resulted in down-regulation of both basal synaptic strength and LTP at Schaffer collateral synapses. These results reveal a novel role of neuronal proheparanase in resetting AMPAR and perineuronal HS levels at the synapse and thus the modulation of synaptic plasticity.
DescriptionPoster Presentation: P59
Persistent Identifierhttp://hdl.handle.net/10722/165081

 

DC FieldValueLanguage
dc.contributor.authorLam, YLen_US
dc.contributor.authorCham, WCen_US
dc.contributor.authorMa, CWen_US
dc.contributor.authorChan, YSen_US
dc.contributor.authorShum, DKYen_US
dc.date.accessioned2012-09-20T08:14:39Z-
dc.date.available2012-09-20T08:14:39Z-
dc.date.issued2012en_US
dc.identifier.citationThe Hong Kong-Taiwan Physiology Symposium 2012 and Joint Scientific Meeting of Hong Kong Society of Neurosciences & The Biophysical Society of Hong Kong, Hong Kong, 14-15 June 2012. In Program Book of the Joint Scientific Meeting, 2012, p. 73-74, abstract P59en_US
dc.identifier.urihttp://hdl.handle.net/10722/165081-
dc.descriptionPoster Presentation: P59-
dc.description.abstractAMPA-type glutamate receptors (AMPAR) govern excitatory synaptic transmission. Perineuronal heparan sulfates (HS) have been implicated in controlling the open-state of AMPAR. Our finding of neuronal heparanase expression in adult rats led us to test (1) if neuronal heparanase is secreted and (2) if the secreted form acts on perineuronal HS to modulate synaptic plasticity. Neuronal secretion of heparanase was triggered by phorbol ester of rat hippocampal neurons in culture. Western blot analysis of the secreted product revealed enzymatically inactive proheparanase, but not the enzymatically active heparanase. Synaptosomes prepared from phorbol ester-treated rat cortex slices showed enrichment in proheparanase; co-immunoprecipitation studies further showed association of AMPAR subunits (GluA1 and GluA2/3) with both syndecan-3 (a transmembrane HS-proteoglycan) and proheparanase, suggesting their partnership in the peri-synaptic environment. Treatment of hippocampal neurons in culture with recombinant proheparanase triggered internalization of proheparanase, perineuronal HS-proteoglycans and AMPARs, suggesting their clustering as a functional complex. Heparitinase pre-treatment of hippocampal neuron cultures reduced proheparanase-induced internalization of AMPARs, suggesting that the HS moiety is critical for effecting the partnership. Treatment of hippocampal slices with recombinant proheparanase resulted in down-regulation of both basal synaptic strength and LTP at Schaffer collateral synapses. These results reveal a novel role of neuronal proheparanase in resetting AMPAR and perineuronal HS levels at the synapse and thus the modulation of synaptic plasticity.-
dc.languageengen_US
dc.publisherHKSN & BPHK.-
dc.relation.ispartofProgram Book of the Joint Scientific Meetingen_US
dc.titleRegulatory role of proheparanase with peri-synatpic heparan sulfate proteoglycan and AMPA-type glutamate receptor in synaptic plasticityen_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.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros209416en_US
dc.identifier.spage73-
dc.identifier.epage74-
dc.publisher.placeHong Kong-

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