ArticleActa histochemica et cytochemica2016
Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload.
Article in Acta histochemica et cytochemica, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Cyclin D3 Colocalizes with Myogenin and p21 in Skeletal Muscle Satellite Cells during Early-Stage Functional Overload.Acta histochemica et cytochemica · 2023Article
- Assessing the Role of Aquaporin 4 in Skeletal Muscle Function.International journal of molecular sciences · 2023Review
- Decrease in AQP4 expression level in atrophied skeletal muscles with innervation.Physiological reports · 2021Article
- Atrogin1-induced loss of aquaporin 4 in myocytes leads to skeletal muscle atrophy.Scientific reports · 2020Article
- Time course changes in AQP4 expression patterns in progressive skeletal muscle atrophy during the early stage of denervation.Journal of musculoskeletal & neuronal interactions · 2020Article
- The expression of aquaporin-4 is regulated based on innervation in skeletal muscles.Journal of muscle research and cell motility · 2018Article
- Marked decrease of aquaporin-4 protein is independent of the changes in α1-syntrophin and TRPV4 levels in response to denervation-induced muscle atrophy in vivo.Journal of muscle research and cell motility · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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