| Literature DB >> 26769242 |
Viviana Dalamon1, Mariana C Fiori2, Vania A Figueroa3, Carolina A Oliva3, Rodrigo Del Rio4, Wendy Gonzalez5, Jonathan Canan5, Ana B Elgoyhen1,6, Guillermo A Altenberg2, Mauricio A Retamal7,8.
Abstract
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 Ca(2+) 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.Entities:
Keywords: Connexins; Deafness; Gap-junction channels; Hemichannels; Ion channel; Mutation
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Year: 2016 PMID： 26769242 DOI： 10.1007/s00424-016-1788-7
Source DB: PubMed Journal: Pflugers Arch ISSN： 0031-6768 Impact factor: 3.657