Concatenation of human connexin26 (hCx26) and human connexin46 (hCx46) for the analysis of heteromeric gap junction hemichannels and heterotypic gap junction channels

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dc.identifier.uri http://dx.doi.org/10.15488/4250
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/4284
dc.contributor.author Schadzek, Patrick
dc.contributor.author Hermes, Doris
dc.contributor.author Stahl, Yannick
dc.contributor.author Dilger, Nadine
dc.contributor.author Ngezahayo, Anaclet
dc.date.accessioned 2018-12-20T14:20:26Z
dc.date.available 2018-12-20T14:20:26Z
dc.date.issued 2018
dc.identifier.citation Schadzek, P.; Hermes, D.; Stahl, Y.; Dilger, N.; Ngezahayo, A.: Concatenation of human connexin26 (hCx26) and human connexin46 (hCx46) for the analysis of heteromeric gap junction hemichannels and heterotypic gap junction channels. In: International Journal of Molecular Sciences 19 (2018), Nr. 9, 2742. DOI: https://doi.org/10.3390/ijms19092742
dc.description.abstract Gap junction channels and hemichannels formed by concatenated connexins were analyzed. Monomeric (hCx26, hCx46), homodimeric (hCx46-hCx46, hCx26-hCx26), and heterodimeric (hCx26-hCx46, hCx46-hCx26) constructs, coupled to GFP, were expressed in HeLa cells. Confocal microscopy showed that the tandems formed gap junction plaques with a reduced plaque area compared to monomeric hCx26 or hCx46. Dye transfer experiments showed that concatenation allows metabolic transfer. Expressed in Xenopus oocytes, the inside-out patch-clamp configuration showed single channels with a conductance of about 46 pS and 39 pS for hemichannels composed of hCx46 and hCx26 monomers, respectively, when chloride was replaced by gluconate on both membrane sides. The conductance was reduced for hCx46-hCx46 and hCx26-hCx26 homodimers, probably due to the concatenation. Heteromerized hemichannels, depending on the connexin-order, were characterized by substates at 26 pS and 16 pS for hCx46-hCx26 and 31 pS and 20 pS for hCx26-hCx46. Because of the linker between the connexins, the properties of the formed hemichannels and gap junction channels (e.g., single channel conductance) may not represent the properties of hetero-oligomerized channels. However, should the removal of the linker be successful, this method could be used to analyze the electrical and metabolic selectivity of such channels and the physiological consequences for a tissue. eng
dc.language.iso eng
dc.publisher Basel : MDPI AG
dc.relation.ispartofseries International Journal of Molecular Sciences 19 (2018), Nr. 9
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Channel stoichiometry eng
dc.subject Concatenated connexins eng
dc.subject Dual whole-cell patch-clamp eng
dc.subject Dye transfer eng
dc.subject Gap junction eng
dc.subject Heteromeric connexons eng
dc.subject Human connexin26 eng
dc.subject Human connexin46 eng
dc.subject Inside-out patch-clamp configuration eng
dc.subject Oligomerization eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Concatenation of human connexin26 (hCx26) and human connexin46 (hCx46) for the analysis of heteromeric gap junction hemichannels and heterotypic gap junction channels eng
dc.type article
dc.type Text
dc.relation.issn 16616596
dc.relation.doi https://doi.org/10.3390/ijms19092742
dc.bibliographicCitation.issue 9
dc.bibliographicCitation.volume 19
dc.bibliographicCitation.firstPage 2742
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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