Abstract
The aquaporins constitute a family of homologous intrinsic membrane proteins that function as highly selective water channels and are highly expressed in tissues where rapid water movement across the cell membrane is required. Molecular mechanism of water transport through the plasma membrane of skeletal muscle is still not clear. This study was designed to identify aquaporin subtypes and their expression regulation in C2C12 cells, a mouse myoblastic cell line. RT-PCR, immunohistochemistry and Western blot analysis revealed that C2C12 cells express AQP5. AQP5 expression was increased by induction of C2C12 differentiation. Exposure of C2C12 cells to hypertonic solutions induced an increase in AQP5 expression and p38 kinase activation. However, a p38 kinase inhibitor failed to inhibit hyperosmolar induction of AQP5 expression in C2C12 cells. These data indicate that skeletal muscle cells express AQP5 protein and its expression is regulated by differentiation and hypertonic stress.
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This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Hwang, S., Lee, R., Song, J. et al. Expression of aquaporin-5 and its regulation in skeletal muscle cells. Exp Mol Med 34, 69–74 (2002). https://doi.org/10.1038/emm.2002.10
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DOI: https://doi.org/10.1038/emm.2002.10
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