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Article: Functional characteristics of skate connexin35, a member of the γ subfamily of connexins expressed in the vertebrate retina

TitleFunctional characteristics of skate connexin35, a member of the γ subfamily of connexins expressed in the vertebrate retina
Authors
KeywordsGap junction
Neuron
Oocyte
Quinine
Voltage
Issue Date1999
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJN
Citation
European Journal Of Neuroscience, 1999, v. 11 n. 6, p. 1883-1890 How to Cite?
AbstractRetinal neurons are coupled by electrical synapses that have been studied extensively in situ and in isolated cell pairs. Although many unique gating properties have been identified, the connexin composition of retinal gap junctions is not well defined. We have functionally characterized connexin35 (Cx35), a recently cloned connexin belonging to the γ subgroup expressed in the skate retina, and compared its biophysical properties with those obtained from electrically coupled retinal cells. Injection of Cx35 RNA into pairs of Xenopus oocytes induced intercellular conductances that were voltage-gated at transjunctional potentials ≥ 60 mV, and that were also closed by intracellular acidification. In contrast, Cx35 was unable to functionally interact with rodent connexins from the α or β subfamilies. Voltage-activated hemichannel currents were also observed in single oocytes expressing Cx35, and superfusing these oocytes with medium containing 100 μM quinine resulted in a 1.8-fold increase in the magnitude of the outward currents, but did not change the threshold of voltage activation (membrane potential = +20 mV). Cx35 intercellular channels between paired oocytes were insensitive to quinine treatment. Both hemichannel activity and its modulation by quinine were seen previously in recordings from isolated skate horizontal cells. Voltage-activated currents of Cx46 hemichannels were also enhanced 1.6-fold following quinine treatment, whereas Cx43-injected oocytes showed no hemichannel activity in the presence, or absence, of quinine. Although the cellular localization of Cx35 is unknown, the functional characteristics of Cx35 in Xenopus oocytes are consistent with the hemichannel and intercellular channel properties of skate horizontal cells.
Persistent Identifierhttp://hdl.handle.net/10722/132731
ISSN
2015 Impact Factor: 2.975
2015 SCImago Journal Rankings: 2.130
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWhite, TWen_HK
dc.contributor.authorDeans, MRen_HK
dc.contributor.authorO'Brien, Jen_HK
dc.contributor.authorAlUbaidi, MRen_HK
dc.contributor.authorGoodenough, DAen_HK
dc.contributor.authorRipps, Hen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.date.accessioned2011-03-28T09:28:37Z-
dc.date.available2011-03-28T09:28:37Z-
dc.date.issued1999en_HK
dc.identifier.citationEuropean Journal Of Neuroscience, 1999, v. 11 n. 6, p. 1883-1890en_HK
dc.identifier.issn0953-816Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/132731-
dc.description.abstractRetinal neurons are coupled by electrical synapses that have been studied extensively in situ and in isolated cell pairs. Although many unique gating properties have been identified, the connexin composition of retinal gap junctions is not well defined. We have functionally characterized connexin35 (Cx35), a recently cloned connexin belonging to the γ subgroup expressed in the skate retina, and compared its biophysical properties with those obtained from electrically coupled retinal cells. Injection of Cx35 RNA into pairs of Xenopus oocytes induced intercellular conductances that were voltage-gated at transjunctional potentials ≥ 60 mV, and that were also closed by intracellular acidification. In contrast, Cx35 was unable to functionally interact with rodent connexins from the α or β subfamilies. Voltage-activated hemichannel currents were also observed in single oocytes expressing Cx35, and superfusing these oocytes with medium containing 100 μM quinine resulted in a 1.8-fold increase in the magnitude of the outward currents, but did not change the threshold of voltage activation (membrane potential = +20 mV). Cx35 intercellular channels between paired oocytes were insensitive to quinine treatment. Both hemichannel activity and its modulation by quinine were seen previously in recordings from isolated skate horizontal cells. Voltage-activated currents of Cx46 hemichannels were also enhanced 1.6-fold following quinine treatment, whereas Cx43-injected oocytes showed no hemichannel activity in the presence, or absence, of quinine. Although the cellular localization of Cx35 is unknown, the functional characteristics of Cx35 in Xenopus oocytes are consistent with the hemichannel and intercellular channel properties of skate horizontal cells.en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJNen_HK
dc.relation.ispartofEuropean Journal of Neuroscienceen_HK
dc.subjectGap junctionen_HK
dc.subjectNeuronen_HK
dc.subjectOocyteen_HK
dc.subjectQuinineen_HK
dc.subjectVoltageen_HK
dc.titleFunctional characteristics of skate connexin35, a member of the γ subfamily of connexins expressed in the vertebrate retinaen_HK
dc.typeArticleen_HK
dc.identifier.emailBruzzone, R: bruzzone@hkucc.hku.hken_HK
dc.identifier.authorityBruzzone, R=rp01442en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1046/j.1460-9568.1999.00607.xen_HK
dc.identifier.pmid10336656-
dc.identifier.scopuseid_2-s2.0-0033009274en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033009274&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume11en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1883en_HK
dc.identifier.epage1890en_HK
dc.identifier.isiWOS:000080720600005-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWhite, TW=35499703300en_HK
dc.identifier.scopusauthoridDeans, MR=6602714276en_HK
dc.identifier.scopusauthoridO'Brien, J=7403406771en_HK
dc.identifier.scopusauthoridAlUbaidi, MR=7004717462en_HK
dc.identifier.scopusauthoridGoodenough, DA=7102378382en_HK
dc.identifier.scopusauthoridRipps, H=7005410758en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK

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