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Article: Multiple connexin proteins in single intercellular channels: Connexin compatibility and functional consequences

TitleMultiple connexin proteins in single intercellular channels: Connexin compatibility and functional consequences
Authors
Keywordscompatibility
connexin
connexon
Gap junction
gating
intercellular channel
voltage
Issue Date1996
PublisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0145-479X
Citation
Journal Of Bioenergetics And Biomembranes, 1996, v. 28 n. 4, p. 339-350 How to Cite?
AbstractIn vertebrates, the protein subunits of intercellular channels found in gap junctions are encoded by a family of genes called connexins. These channels span two plasma membranes and result from the association of two half channels, or connexons, which are hexameric assemblies of connexins. Physiological analysis of channel formation and gating has revealed unique patterns of connexin-connexin interaction, and uncovered novel functional characteristics of channels containing more than one type of connexin protein. Structure-function studies have further demonstrated that unique domains within connexins participate in the regulation of different functional properties of intercellular channels. Thus, gap junctional channels can contain more than one connexin, and this structural heterogeneity has functional consequences in vitro. Moreover, emerging evidence for the existence of intercellular channels containing multiple connexins in native tissues suggests that the functional diversity generated by connexin-connexin interaction could contribute to complex communication patterns that have been observed in vivo.
Persistent Identifierhttp://hdl.handle.net/10722/132746
ISSN
2015 Impact Factor: 2.08
2015 SCImago Journal Rankings: 1.092
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWhite, TWen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.date.accessioned2011-03-28T09:28:42Z-
dc.date.available2011-03-28T09:28:42Z-
dc.date.issued1996en_HK
dc.identifier.citationJournal Of Bioenergetics And Biomembranes, 1996, v. 28 n. 4, p. 339-350en_HK
dc.identifier.issn0145-479Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/132746-
dc.description.abstractIn vertebrates, the protein subunits of intercellular channels found in gap junctions are encoded by a family of genes called connexins. These channels span two plasma membranes and result from the association of two half channels, or connexons, which are hexameric assemblies of connexins. Physiological analysis of channel formation and gating has revealed unique patterns of connexin-connexin interaction, and uncovered novel functional characteristics of channels containing more than one type of connexin protein. Structure-function studies have further demonstrated that unique domains within connexins participate in the regulation of different functional properties of intercellular channels. Thus, gap junctional channels can contain more than one connexin, and this structural heterogeneity has functional consequences in vitro. Moreover, emerging evidence for the existence of intercellular channels containing multiple connexins in native tissues suggests that the functional diversity generated by connexin-connexin interaction could contribute to complex communication patterns that have been observed in vivo.en_HK
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0145-479Xen_HK
dc.relation.ispartofJournal of Bioenergetics and Biomembranesen_HK
dc.subjectcompatibilityen_HK
dc.subjectconnexinen_HK
dc.subjectconnexonen_HK
dc.subjectGap junctionen_HK
dc.subjectgatingen_HK
dc.subjectintercellular channelen_HK
dc.subjectvoltageen_HK
dc.titleMultiple connexin proteins in single intercellular channels: Connexin compatibility and functional consequencesen_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.doi10.1007/BF02110110-
dc.identifier.pmid8844331-
dc.identifier.scopuseid_2-s2.0-0029743057en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029743057&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume28en_HK
dc.identifier.issue4en_HK
dc.identifier.spage339en_HK
dc.identifier.epage350en_HK
dc.identifier.isiWOS:A1996VA32200006-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWhite, TW=35499703300en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK

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