ArticleActa histochemica et cytochemica2012
Close association of aquaporin-2 internalization with caveolin-1.
Article in Acta histochemica et cytochemica, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Upregulation of aquaporin-2 and caveolins in rat bladder with outlet obstruction-induced detrusor overactivity.Investigative and clinical urology · 2026Article
- Orchestrating movement: the role of Caveolin-1 in migration and metastasis.Molecular cancer · 2025Review
- Mechanisms of aquaporin-4 vesicular trafficking in mammalian cells.Journal of neurochemistry · 2024Article
- Expression Regulation and Trafficking of Aquaporins.Advances in experimental medicine and biology · 2023Review
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022Review
- Review
- Caveolin-1 Regulates Perivascular Aquaporin-4 Expression After Cerebral Ischemia.Frontiers in cell and developmental biology · 2020Article
- Molecular mechanisms regulating aquaporin-2 in kidney collecting duct.American journal of physiology. Renal physiology · 2016Review
- The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases.Frontiers in pharmacology · 2016Review
- Vasopressin induces apical expression of caveolin in rat kidney collecting duct principal cells.American journal of physiology. Renal physiology · 2013Article
- Function of the membrane water channel aquaporin-5 in the salivary gland.Acta histochemica et cytochemica · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin 2 (AQP2) is a membrane water channel protein that traffics between the intracellular membrane compartment and the plasma membrane in a vasopressin-dependent manner in the renal collecting duct cell to control the amount of water reabsorption. We examined the relation between AQP2 internalization from the plasma membrane and caveolin-1, which is a major protein in membrane microdomain caveolae, in Mardin-Darby canine kidney cells expressing human AQP2 (MDCK-hAQP2 cells). Double-immunofluorescence microscopy showed that AQP2 is colocalized with caveolin-1 in the apical plasma membrane by stimulating the intracellular signaling cascade of vasopressin with forskolin. After washing forskolin, both AQP2 and caveolin-1 were internalized to early endosomes and then separately went back to their individual compartments, which are subapical compartments and the apical membrane, respectively.Double-immunogold electron microscopy in ultrathin cryosections confirmed the colocalization of AQP2 with caveolin-1 at caveolar structures on the apical plasma membrane of forskolin-treated cells and the colocalization within the same intracellular vesicles after washing forskolin. A co-immunoprecipitation experiment showed the close interaction between AQP2 and caveolin-1 in forskolin-treated cells and in cells after washing forskolin. These results suggest that a caveolin-1-dependent and possibly caveolar-dependent pathway is a candidate for AQP2 internalization in MDCK cells.
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