File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Mouse Cx50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70

TitleMouse Cx50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70
Authors
KeywordsSpecies Index: Rodentia
Issue Date1992
PublisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/
Citation
Molecular Biology Of The Cell, 1992, v. 3 n. 7, p. 711-720 How to Cite?
AbstractThe crystalline lens is an attractive system to study the biology of intercellular communication; however, the identity of the structural components of gap junctions in the lens has been controversial. We have cloned a novel member of the connexin family of gap junction proteins, Cx50, and have shown that it is likely to correspond to the previously described lens fiber protein MP70. The N-terminal amino acid sequence of MP70 closely matches the sequence predicted by the clone. Cx50 mRNA is detected only in the lens, among the 12 organs tested, and this distribution is indistinguishable from that of MP70 protein. A monoclonal antibody directed against MP70 and an anti-Cx50 antibody produced against a synthetic peptide identify the same proteins on western blots and produce identical patterns of immunofluorescence on frozen sections of rodent lens. We also show that expression of Cx50 in paired Xenopus oocytes induces high levels of voltage- dependent conductance. This indicates that Cx50 is a functional member of the connexin family with unique physiological properties. With the cloning of Cx50, all known participants in gap junction formation between various cell types in the lens are available for study and reconstitution in experimental systems.
Persistent Identifierhttp://hdl.handle.net/10722/132768
ISSN
2015 Impact Factor: 4.037
2015 SCImago Journal Rankings: 3.665
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWhite, TWen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.contributor.authorGoodenough, DAen_HK
dc.contributor.authorPaul, DLen_HK
dc.date.accessioned2011-03-28T09:28:51Z-
dc.date.available2011-03-28T09:28:51Z-
dc.date.issued1992en_HK
dc.identifier.citationMolecular Biology Of The Cell, 1992, v. 3 n. 7, p. 711-720en_HK
dc.identifier.issn1059-1524en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132768-
dc.description.abstractThe crystalline lens is an attractive system to study the biology of intercellular communication; however, the identity of the structural components of gap junctions in the lens has been controversial. We have cloned a novel member of the connexin family of gap junction proteins, Cx50, and have shown that it is likely to correspond to the previously described lens fiber protein MP70. The N-terminal amino acid sequence of MP70 closely matches the sequence predicted by the clone. Cx50 mRNA is detected only in the lens, among the 12 organs tested, and this distribution is indistinguishable from that of MP70 protein. A monoclonal antibody directed against MP70 and an anti-Cx50 antibody produced against a synthetic peptide identify the same proteins on western blots and produce identical patterns of immunofluorescence on frozen sections of rodent lens. We also show that expression of Cx50 in paired Xenopus oocytes induces high levels of voltage- dependent conductance. This indicates that Cx50 is a functional member of the connexin family with unique physiological properties. With the cloning of Cx50, all known participants in gap junction formation between various cell types in the lens are available for study and reconstitution in experimental systems.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/en_HK
dc.relation.ispartofMolecular Biology of the Cellen_HK
dc.subjectSpecies Index: Rodentiaen_US
dc.titleMouse Cx50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70en_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.pmid1325220-
dc.identifier.scopuseid_2-s2.0-0027070644en_HK
dc.identifier.volume3en_HK
dc.identifier.issue7en_HK
dc.identifier.spage711en_HK
dc.identifier.epage720en_HK
dc.identifier.isiWOS:A1992JJ39800001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWhite, TW=35499703300en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK
dc.identifier.scopusauthoridGoodenough, DA=7102378382en_HK
dc.identifier.scopusauthoridPaul, DL=7401667165en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats