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Lens Connexin Channels Show Differential Permeability to Signaling Molecules
Gap junction channels mediate the direct intercellular passage of small ions as well as larger solutes such as second messengers. A family of proteins called connexins make up the subunits of gap junction channels in chordate animals. Each individual connexin forms channels that exhibit distinct per...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555617/ https://www.ncbi.nlm.nih.gov/pubmed/32971763 http://dx.doi.org/10.3390/ijms21186943 |
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author | Brink, Peter R. Valiunas, Virginijus White, Thomas W. |
author_facet | Brink, Peter R. Valiunas, Virginijus White, Thomas W. |
author_sort | Brink, Peter R. |
collection | PubMed |
description | Gap junction channels mediate the direct intercellular passage of small ions as well as larger solutes such as second messengers. A family of proteins called connexins make up the subunits of gap junction channels in chordate animals. Each individual connexin forms channels that exhibit distinct permeability to molecules that influence cellular signaling, such as calcium ions, cyclic nucleotides, or inositol phosphates. In this review, we examine the permeability of connexin channels containing Cx43, Cx46, and Cx50 to signaling molecules and attempt to relate the observed differences in permeability to possible in vivo consequences that were revealed by studies of transgenic animals where these connexin genes have been manipulated. Taken together, these data suggest that differences in the permeability of individual connexin channels to larger solutes like 3′,5′-cyclic adenosine monophosphate (cAMP) and inositol 1,4,5-trisphosphate (IP(3)) could play a role in regulating epithelial cell division, differentiation, and homeostasis in organs like the ocular lens. |
format | Online Article Text |
id | pubmed-7555617 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-75556172020-10-19 Lens Connexin Channels Show Differential Permeability to Signaling Molecules Brink, Peter R. Valiunas, Virginijus White, Thomas W. Int J Mol Sci Review Gap junction channels mediate the direct intercellular passage of small ions as well as larger solutes such as second messengers. A family of proteins called connexins make up the subunits of gap junction channels in chordate animals. Each individual connexin forms channels that exhibit distinct permeability to molecules that influence cellular signaling, such as calcium ions, cyclic nucleotides, or inositol phosphates. In this review, we examine the permeability of connexin channels containing Cx43, Cx46, and Cx50 to signaling molecules and attempt to relate the observed differences in permeability to possible in vivo consequences that were revealed by studies of transgenic animals where these connexin genes have been manipulated. Taken together, these data suggest that differences in the permeability of individual connexin channels to larger solutes like 3′,5′-cyclic adenosine monophosphate (cAMP) and inositol 1,4,5-trisphosphate (IP(3)) could play a role in regulating epithelial cell division, differentiation, and homeostasis in organs like the ocular lens. MDPI 2020-09-22 /pmc/articles/PMC7555617/ /pubmed/32971763 http://dx.doi.org/10.3390/ijms21186943 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Brink, Peter R. Valiunas, Virginijus White, Thomas W. Lens Connexin Channels Show Differential Permeability to Signaling Molecules |
title | Lens Connexin Channels Show Differential Permeability to Signaling Molecules |
title_full | Lens Connexin Channels Show Differential Permeability to Signaling Molecules |
title_fullStr | Lens Connexin Channels Show Differential Permeability to Signaling Molecules |
title_full_unstemmed | Lens Connexin Channels Show Differential Permeability to Signaling Molecules |
title_short | Lens Connexin Channels Show Differential Permeability to Signaling Molecules |
title_sort | lens connexin channels show differential permeability to signaling molecules |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7555617/ https://www.ncbi.nlm.nih.gov/pubmed/32971763 http://dx.doi.org/10.3390/ijms21186943 |
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