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Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload
Aquaporin-4 (AQP4) is a selective water channel that is located on the plasma membrane of myofibers in skeletal muscle and is bound to α1-syntrophin. It is considered that AQP4 is involved in the modulation of homeostasis in myofibers through the regulation of water transport and osmotic pressure. H...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4939316/ https://www.ncbi.nlm.nih.gov/pubmed/27462134 http://dx.doi.org/10.1267/ahc.16005 |
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author | Ishido, Minenori Nakamura, Tomohiro |
author_facet | Ishido, Minenori Nakamura, Tomohiro |
author_sort | Ishido, Minenori |
collection | PubMed |
description | Aquaporin-4 (AQP4) is a selective water channel that is located on the plasma membrane of myofibers in skeletal muscle and is bound to α1-syntrophin. It is considered that AQP4 is involved in the modulation of homeostasis in myofibers through the regulation of water transport and osmotic pressure. However, it remains unclear whether AQP4 expression is altered by skeletal muscle hypertrophy to modulate water homeostasis in myofibers. The present study investigated the effect of muscle hypertrophy on the changes in AQP4 and α1-syntrophin expression patterns in myofibers. Novel findings indicated in the present study were as follows: 1) Expression levels of AQP4 and α1-syntrophin were stably maintained in hypertrophied muscles, and 2) AQP4 was not expressed in the myofibers containing the slow-type myosin heavy chain isoform (MHC) with or without the presence of fast-type MHC. The present study suggests that AQP4 may regulate the efficiency of water transport in hypertrophied myofibers through its interaction with α1-syntrophin. In addition, this study suggests that AQP4 expression may be inhibited by a regulatory mechanism activated under physiological conditions that induces the expression of slow-type MHC in skeletal muscles. |
format | Online Article Text |
id | pubmed-4939316 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY |
record_format | MEDLINE/PubMed |
spelling | pubmed-49393162016-07-26 Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload Ishido, Minenori Nakamura, Tomohiro Acta Histochem Cytochem Regular Article Aquaporin-4 (AQP4) is a selective water channel that is located on the plasma membrane of myofibers in skeletal muscle and is bound to α1-syntrophin. It is considered that AQP4 is involved in the modulation of homeostasis in myofibers through the regulation of water transport and osmotic pressure. However, it remains unclear whether AQP4 expression is altered by skeletal muscle hypertrophy to modulate water homeostasis in myofibers. The present study investigated the effect of muscle hypertrophy on the changes in AQP4 and α1-syntrophin expression patterns in myofibers. Novel findings indicated in the present study were as follows: 1) Expression levels of AQP4 and α1-syntrophin were stably maintained in hypertrophied muscles, and 2) AQP4 was not expressed in the myofibers containing the slow-type myosin heavy chain isoform (MHC) with or without the presence of fast-type MHC. The present study suggests that AQP4 may regulate the efficiency of water transport in hypertrophied myofibers through its interaction with α1-syntrophin. In addition, this study suggests that AQP4 expression may be inhibited by a regulatory mechanism activated under physiological conditions that induces the expression of slow-type MHC in skeletal muscles. JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY 2016-06-28 2016-06-16 /pmc/articles/PMC4939316/ /pubmed/27462134 http://dx.doi.org/10.1267/ahc.16005 Text en 2016 The Japan Society of Histochemistry and Cytochemistry 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 work is properly cited. |
spellingShingle | Regular Article Ishido, Minenori Nakamura, Tomohiro Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload |
title | Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload |
title_full | Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload |
title_fullStr | Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload |
title_full_unstemmed | Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload |
title_short | Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload |
title_sort | aquaporin-4 protein is stably maintained in the hypertrophied muscles by functional overload |
topic | Regular Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4939316/ https://www.ncbi.nlm.nih.gov/pubmed/27462134 http://dx.doi.org/10.1267/ahc.16005 |
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