Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness

Viviana Dalamon; Mariana C. Fiori; Vania A. Figueroa; Carolina A. Oliva; Rodrigo Del Rio; Wendy Gonzalez; Jonathan Canan; Ana B. Elgoyhen; Guillermo A. Altenberg; Mauricio A. Retamal

doi:10.1007/s00424-016-1788-7

Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness

Viviana Dalamon, Mariana C. Fiori, Vania A. Figueroa, Carolina A. Oliva, Rodrigo Del Rio, Wendy Gonzalez, Jonathan Canan, Ana B. Elgoyhen, Guillermo A. Altenberg, Mauricio A. Retamal

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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 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.

Original language	English (US)
Pages (from-to)	1-10
Number of pages	10
Journal	Pflugers Archiv European Journal of Physiology
DOIs	https://doi.org/10.1007/s00424-016-1788-7
State	Accepted/In press - Jan 14 2016
Externally published	Yes

Keywords

Connexins
Deafness
Gap-junction channels
Hemichannels
Ion channel
Mutation

ASJC Scopus subject areas

Physiology
Clinical Biochemistry
Physiology (medical)

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10.1007/s00424-016-1788-7

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Dalamon, V., Fiori, M. C., Figueroa, V. A., Oliva, C. A., Del Rio, R., Gonzalez, W., Canan, J., Elgoyhen, A. B., Altenberg, G. A., & Retamal, M. A. (Accepted/In press). Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness. Pflugers Archiv European Journal of Physiology, 1-10. https://doi.org/10.1007/s00424-016-1788-7

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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 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.",

keywords = "Connexins, Deafness, Gap-junction channels, Hemichannels, Ion channel, Mutation",

author = "Viviana Dalamon and Fiori, {Mariana C.} and Figueroa, {Vania A.} and Oliva, {Carolina A.} and {Del Rio}, Rodrigo and Wendy Gonzalez and Jonathan Canan and Elgoyhen, {Ana B.} and Altenberg, {Guillermo A.} and Retamal, {Mauricio A.}",

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doi = "10.1007/s00424-016-1788-7",

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AU - Dalamon, Viviana

AU - Fiori, Mariana C.

AU - Figueroa, Vania A.

AU - Oliva, Carolina A.

AU - Del Rio, Rodrigo

AU - Gonzalez, Wendy

AU - Canan, Jonathan

AU - Elgoyhen, Ana B.

AU - Altenberg, Guillermo A.

AU - Retamal, Mauricio A.

PY - 2016/1/14

Y1 - 2016/1/14

N2 - 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.

AB - 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.

KW - Connexins

KW - Deafness

KW - Gap-junction channels

KW - Hemichannels

KW - Ion channel

KW - Mutation

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Gap-junctional channel and hemichannel activity of two recently identified connexin 26 mutants associated with deafness

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