ArticleFEBS open bio2021
Aquaporin 1 mediates early responses to osmotic stimuli in endothelial cells via the calmodulin pathway.
Article in FEBS open bio, 2021. 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, 12 citations in OpenAlex.
- Single-cell and spatial transcriptomic analyses reveal the dynamic transcript profiles of myocardial lymphangiogenesis post-myocardial infarction.Chinese medical journal · 2026Article
- Article
- Mechanical shear flow regulates the malignancy of colorectal cancer cells.The Kaohsiung journal of medical sciences · 2024Article
- Establishment of the deuterium oxide dilution method as a new possibility for determining the transendothelial water permeability.Pflugers Archiv : European journal of physiology · 2024Article
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Molecular mechanisms governing aquaporin relocalisation.Biochimica et biophysica acta. Biomembranes · 2022Review
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aquaporins (AQPs) are a family of integral membrane proteins which play critical roles in controlling transcellular water movement in various tissues throughout the body. AQP1 helps mediate the cellular response to osmotic stress and tissue water permeability. However, the mechanism by which AQP1 mediates changes in cell volume is not completely clear. Here, we investigated how AQP1 responds to and controls cell volume upon osmotic stimuli during the early phase after the immediate response. Cells overexpressing AQP1 were exposed to hypotonic or hypertonic medium in the presence or absence of staurosporine or W-7 hydrochloride, and fluorescence imaging was performed at 0, 5, 10, and 15 min later. Osmotic stimuli induced redistribution of AQP1 into the cell membrane, hypotonic stimuli caused cell enlargement, and hypertonic stimuli induced a reduction in cell size, which was blocked by T157A/T239A mutations. Changes in cell size induced by osmotic stimuli were blocked by an antagonist of calmodulin kinase, W-7 hydrochloride, but not by the PKC inhibitor staurosporine. These results suggest that calmodulin kinase regulates AQP1 activity during the early response to osmotic stimuli.
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