Show simple item record

dc.contributor.authorDalamon V.
dc.contributor.authorFiori M.C.
dc.contributor.authorFigueroa V.A.
dc.contributor.authorOliva C.A.
dc.contributor.authordel Rio R.
dc.contributor.authorGonzalez W.
dc.contributor.authorCanan J.
dc.contributor.authorElgoyhen A.B.
dc.contributor.authorAltenberg G.A.
dc.contributor.authorRetamal M.A.
dc.date.accessioned2020-09-02T22:16:09Z
dc.date.available2020-09-02T22:16:09Z
dc.date.issued2016
dc.identifier10.1007/s00424-016-1788-7
dc.identifier.citation468, 5, 909-918
dc.identifier.issn00316768
dc.identifier.urihttps://hdl.handle.net/20.500.12728/4216
dc.descriptionGap-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.isoen
dc.publisherSpringer Verlag
dc.subjectConnexins
dc.subjectDeafness
dc.subjectGap-junction channels
dc.subjectHemichannels
dc.subjectIon channel
dc.subjectMutation
dc.subjectadenosine triphosphate
dc.subjectconnexin 26
dc.subjectdye
dc.subjectgap junction channel
dc.subjectgap junction protein
dc.subjecthemichannel
dc.subjectmutant protein
dc.subjectunclassified drug
dc.subjectadenosine triphosphate
dc.subjectcalcium
dc.subjectDFNA3 protein, human
dc.subjectgap junction protein
dc.subjectanimal cell
dc.subjectArticle
dc.subjectchannel gating
dc.subjectcontrolled study
dc.subjectelectric potential
dc.subjectextracellular calcium
dc.subjectfluorescence analysis
dc.subjectgap junction
dc.subjectgene mutation
dc.subjecthearing impairment
dc.subjecthuman
dc.subjecthuman cell
dc.subjection current
dc.subjection permeability
dc.subjectmembrane electrophysiology
dc.subjectmissense mutation
dc.subjectmolecular dynamics
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectvoltage dependence
dc.subjectWestern blotting
dc.subjectwild type
dc.subjectXenopus laevis
dc.subjectaction potential
dc.subjectanimal
dc.subjectchannel gating
dc.subjectchemistry
dc.subjectgenetics
dc.subjecthearing impairment
dc.subjectHeLa cell line
dc.subjectmetabolism
dc.subjectmutation
dc.subjectXenopus
dc.subjectAction Potentials
dc.subjectAdenosine Triphosphate
dc.subjectAnimals
dc.subjectCalcium
dc.subjectConnexins
dc.subjectDeafness
dc.subjectHeLa Cells
dc.subjectHumans
dc.subjectIon Channel Gating
dc.subjectMutation
dc.subjectXenopus
dc.titleGap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness
dc.typeArticle


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record