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Authors
Markou, AUnger, L
Abir-Awan, M
Saadallah, A
Halsey, A
Baklava, Z
Conner, Matthew T.
Törnroth-Horsefield, S
Greenhill, SD
Conner, A
Bill, RM
Salman, MM
Kitchen, P
Issue Date
2022-01-05
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Show full item recordAbstract
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.Citation
Markou, A., Unger, L., Abir-Awan, M. et al. (2022) Molecular mechanisms governing aquaporin relocalisation. Biochimica et Biophysica Acta - Biomembranes, 1864(4), 183853.Publisher
ElsevierJournal
Biochimica et Biophysica Acta - BiomembranesPubMed ID
34973181 (pubmed)Type
Journal articleLanguage
enDescription
© 2022 The Authors. Published by Elsevier. This is an open access article available under a Creative Commons licence. The published version can be accessed at the following link on the publisher’s website: https://doi.org/10.1016/j.bbamem.2021.183853ISSN
0005-2736EISSN
1879-2642Sponsors
This work was supported by Aston University through a 50th Anniversary Prize fellowship to PK and a PhD studentship to AM. RMB, ACC and PK were supported by the Biotechnology & Biosciences Research Council (BB/P025927/1). LU is supported by the European Union‘s Horizon 2020 research and innovation programme under Marie Skłodowska Curie grant agreement No. 847,419 (MemTrain). MA is supported by a studentship co-funded by Aston University and the UK Engineering and Physical Sciences Research Council (EP/R512889/1) to RMB. AS is supported by a studentship from the Iraqi Ministry of Higher Education and Scientific Research and the University of Mosul. AH was supported by a studentship from Spinal Research. STH is supported by the Swedish Research Council (2013-05945), the Crafoord Foundation (20140811 and 20180916) and the Magnus Bergvall Foundation (2015- 01534).ae974a485f413a2113503eed53cd6c53
10.1016/j.bbamem.2021.183853
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Except where otherwise noted, this item's license is described as https://creativecommons.org/licenses/by/4.0/
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