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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...

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Autores principales: Ishido, Minenori, Nakamura, Tomohiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY 2016
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.
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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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