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Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness
dc.contributor.author | Dalamon V. | |
dc.contributor.author | Fiori M.C. | |
dc.contributor.author | Figueroa V.A. | |
dc.contributor.author | Oliva C.A. | |
dc.contributor.author | del Rio R. | |
dc.contributor.author | Gonzalez W. | |
dc.contributor.author | Canan J. | |
dc.contributor.author | Elgoyhen A.B. | |
dc.contributor.author | Altenberg G.A. | |
dc.contributor.author | Retamal M.A. | |
dc.date.accessioned | 2020-09-02T22:16:09Z | |
dc.date.available | 2020-09-02T22:16:09Z | |
dc.date.issued | 2016 | |
dc.identifier | 10.1007/s00424-016-1788-7 | |
dc.identifier.citation | 468, 5, 909-918 | |
dc.identifier.issn | 00316768 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12728/4216 | |
dc.description | Gap-junction channels (GJCs) are formed by head-to-head association of two hemichannels (HCs, connexin hexamers). HCs and GJCs are permeable to ions and hydrophilic molecules of up to Mr ~1 kDa. Hearing impairment of genetic origin is common, and mutations of connexin 26 (Cx26) are its major cause. We recently identified two novel Cx26 mutations in hearing-impaired subjects, L10P and G109V. L10P forms functional GJCs with slightly altered voltage dependence and HCs with decrease ATP/cationic dye selectivity. G109V does not form functional GJCs, but forms functional HCs with enhanced extracellular Ca2+ sensitivity and subtle alterations in voltage dependence and ATP/cationic dye selectivity. Deafness associated with G109V could result from decreased GJCs activity, whereas deafness associated to L10P may have a more complex mechanism that involves changes in HC permeability. © 2016, Springer-Verlag Berlin Heidelberg. | |
dc.language.iso | en | |
dc.publisher | Springer Verlag | |
dc.subject | Connexins | |
dc.subject | Deafness | |
dc.subject | Gap-junction channels | |
dc.subject | Hemichannels | |
dc.subject | Ion channel | |
dc.subject | Mutation | |
dc.subject | adenosine triphosphate | |
dc.subject | connexin 26 | |
dc.subject | dye | |
dc.subject | gap junction channel | |
dc.subject | gap junction protein | |
dc.subject | hemichannel | |
dc.subject | mutant protein | |
dc.subject | unclassified drug | |
dc.subject | adenosine triphosphate | |
dc.subject | calcium | |
dc.subject | DFNA3 protein, human | |
dc.subject | gap junction protein | |
dc.subject | animal cell | |
dc.subject | Article | |
dc.subject | channel gating | |
dc.subject | controlled study | |
dc.subject | electric potential | |
dc.subject | extracellular calcium | |
dc.subject | fluorescence analysis | |
dc.subject | gap junction | |
dc.subject | gene mutation | |
dc.subject | hearing impairment | |
dc.subject | human | |
dc.subject | human cell | |
dc.subject | ion current | |
dc.subject | ion permeability | |
dc.subject | membrane electrophysiology | |
dc.subject | missense mutation | |
dc.subject | molecular dynamics | |
dc.subject | nonhuman | |
dc.subject | priority journal | |
dc.subject | voltage dependence | |
dc.subject | Western blotting | |
dc.subject | wild type | |
dc.subject | Xenopus laevis | |
dc.subject | action potential | |
dc.subject | animal | |
dc.subject | channel gating | |
dc.subject | chemistry | |
dc.subject | genetics | |
dc.subject | hearing impairment | |
dc.subject | HeLa cell line | |
dc.subject | metabolism | |
dc.subject | mutation | |
dc.subject | Xenopus | |
dc.subject | Action Potentials | |
dc.subject | Adenosine Triphosphate | |
dc.subject | Animals | |
dc.subject | Calcium | |
dc.subject | Connexins | |
dc.subject | Deafness | |
dc.subject | HeLa Cells | |
dc.subject | Humans | |
dc.subject | Ion Channel Gating | |
dc.subject | Mutation | |
dc.subject | Xenopus | |
dc.title | Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness | |
dc.type | Article |