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Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties
In mammals, a single pannexin1 gene (Panx1) is widely expressed in the CNS including the inner and outer retinae, forming large-pore voltage-gated membrane channels, which are involved in calcium and ATP signaling. Previously, we discovered that zebrafish lack Panx1 expression in the inner retina, w...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3808535/ https://www.ncbi.nlm.nih.gov/pubmed/24194896 http://dx.doi.org/10.1371/journal.pone.0077722 |
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author | Kurtenbach, Sarah Prochnow, Nora Kurtenbach, Stefan Klooster, Jan Zoidl, Christiane Dermietzel, Rolf Kamermans, Maarten Zoidl, Georg |
author_facet | Kurtenbach, Sarah Prochnow, Nora Kurtenbach, Stefan Klooster, Jan Zoidl, Christiane Dermietzel, Rolf Kamermans, Maarten Zoidl, Georg |
author_sort | Kurtenbach, Sarah |
collection | PubMed |
description | In mammals, a single pannexin1 gene (Panx1) is widely expressed in the CNS including the inner and outer retinae, forming large-pore voltage-gated membrane channels, which are involved in calcium and ATP signaling. Previously, we discovered that zebrafish lack Panx1 expression in the inner retina, with drPanx1a exclusively expressed in horizontal cells of the outer retina. Here, we characterize a second drPanx1 protein, drPanx1b, generated by whole-genome duplications during teleost evolution. Homology searches strongly support the presence of pannexin sequences in cartilaginous fish and provide evidence that pannexins evolved when urochordata and chordata evolution split. Further, we confirm Panx1 ohnologs being solely present in teleosts. A hallmark of differential expression of drPanx1a and drPanx1b in various zebrafish brain areas is the non-overlapping protein localization of drPanx1a in the outer and drPanx1b in the inner fish retina. A functional comparison of the evolutionary distant fish and mouse Panx1s revealed both, preserved and unique properties. Preserved functions are the capability to form channels opening at resting potential, which are sensitive to known gap junction and hemichannel blockers, intracellular calcium, extracellular ATP and pH changes. However, drPanx1b is unique due to its highly complex glycosylation pattern and distinct electrophysiological gating kinetics. The existence of two Panx1 proteins in zebrafish displaying distinct tissue distribution, protein modification and electrophysiological properties, suggests that both proteins fulfill different functions in vivo. |
format | Online Article Text |
id | pubmed-3808535 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38085352013-11-05 Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties Kurtenbach, Sarah Prochnow, Nora Kurtenbach, Stefan Klooster, Jan Zoidl, Christiane Dermietzel, Rolf Kamermans, Maarten Zoidl, Georg PLoS One Research Article In mammals, a single pannexin1 gene (Panx1) is widely expressed in the CNS including the inner and outer retinae, forming large-pore voltage-gated membrane channels, which are involved in calcium and ATP signaling. Previously, we discovered that zebrafish lack Panx1 expression in the inner retina, with drPanx1a exclusively expressed in horizontal cells of the outer retina. Here, we characterize a second drPanx1 protein, drPanx1b, generated by whole-genome duplications during teleost evolution. Homology searches strongly support the presence of pannexin sequences in cartilaginous fish and provide evidence that pannexins evolved when urochordata and chordata evolution split. Further, we confirm Panx1 ohnologs being solely present in teleosts. A hallmark of differential expression of drPanx1a and drPanx1b in various zebrafish brain areas is the non-overlapping protein localization of drPanx1a in the outer and drPanx1b in the inner fish retina. A functional comparison of the evolutionary distant fish and mouse Panx1s revealed both, preserved and unique properties. Preserved functions are the capability to form channels opening at resting potential, which are sensitive to known gap junction and hemichannel blockers, intracellular calcium, extracellular ATP and pH changes. However, drPanx1b is unique due to its highly complex glycosylation pattern and distinct electrophysiological gating kinetics. The existence of two Panx1 proteins in zebrafish displaying distinct tissue distribution, protein modification and electrophysiological properties, suggests that both proteins fulfill different functions in vivo. Public Library of Science 2013-10-23 /pmc/articles/PMC3808535/ /pubmed/24194896 http://dx.doi.org/10.1371/journal.pone.0077722 Text en © 2013 Kurtenbach et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Kurtenbach, Sarah Prochnow, Nora Kurtenbach, Stefan Klooster, Jan Zoidl, Christiane Dermietzel, Rolf Kamermans, Maarten Zoidl, Georg Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties |
title | Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties |
title_full | Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties |
title_fullStr | Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties |
title_full_unstemmed | Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties |
title_short | Pannexin1 Channel Proteins in the Zebrafish Retina Have Shared and Unique Properties |
title_sort | pannexin1 channel proteins in the zebrafish retina have shared and unique properties |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3808535/ https://www.ncbi.nlm.nih.gov/pubmed/24194896 http://dx.doi.org/10.1371/journal.pone.0077722 |
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