Molecular mechanisms governing aquaporin relocalisation |
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| Institution: | 1. College of Health and Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK;2. MRC Institute of Metabolic Science, University of Cambridge, Cambridge CB2 0QQ, UK;3. School of Sciences, Research Institute in Healthcare Science, University of Wolverhampton, Wolverhampton WV1 1LY, UK;4. Department of Biochemistry and Structural Biology, Lund University, PO Box 124, 221 00 Lund, Sweden;5. Institute of Clinical Sciences, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK;6. Department of Physiology Anatomy and Genetics, University of Oxford, Oxford OX1 3QX, UK;7. Oxford Parkinson''s Disease Centre, University of Oxford, South Parks Road, Oxford OX1 3QX, UK |
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| Abstract: | The aquaporins (AQPs) form a family of integral membrane proteins that facilitate the movement of water across biological membrane by osmosis, as well as facilitating the diffusion of small polar solutes. AQPs have been recognised as drug targets for a variety of disorders associated with disrupted water or solute transport, including brain oedema following stroke or trauma, epilepsy, cancer cell migration and tumour angiogenesis, metabolic disorders, and inflammation. Despite this, drug discovery for AQPs has made little progress due to a lack of reproducible high-throughput assays and difficulties with the druggability of AQP proteins. However, recent studies have suggested that targetting the trafficking of AQP proteins to the plasma membrane is a viable alternative drug target to direct inhibition of the water-conducting pore. Here we review the literature on the trafficking of mammalian AQPs with a view to highlighting potential new drug targets for a variety of conditions associated with disrupted water and solute homeostasis. |
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