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Aquaporin-1 (AQP1) is a protein comprised of 269 amino acids, featuring six transmembrane segments [1]. It stands as the pioneering identified integral membrane protein channel within mammalian red blood cells, facilitating the rapid passive transport of water across biological membranes [2]. As a member of the aquaporin family, AQP1 joins a group of transmembrane proteins primarily dedicated to expediting water movement across cellular membranes [1]. Research reveals AQP1's involvement in a spectrum of physiological functions, including its role in maintaining water balance within the brain and post-traumatic injury and contributing to the kidney's countercurrent multiplier mechanism [3][4]. Moreover, AQP1 demonstrates to impede apoptosis and influence prognosis in esophageal squamous cell carcinoma [5].
The examination of AQP1's structure and dynamics has been extensive, employing crystallographic techniques, cryo-EM structures, and molecular dynamics, yielding profound insights into its operational characteristics [6][7]. Additionally, several studies have suggested that AQP1 may transport small polar non-electrolytes alongside water, further underlining its multifaceted functions and structural attributes. These revelations underscore the pivotal role of AQP1 in a myriad of physiological and pathological processes.
References:
[1] J. Bomholt, C. Hélix-Nielsen, P. Scharff-Poulsen, & P. Pedersen, "Recombinant production of human aquaporin-1 to an exceptional high membrane density in saccharomyces cerevisiae", Plos One, vol. 8, no. 2, p. e56431, 2013. https://doi.org/10.1371/journal.pone.0056431
[2] Y. Koyama, T. Yamamoto, D. Kondo, H. Funaki, E. Yaoita, K. Kawasakiet al., "Molecular cloning of a new aquaporin from rat pancreas and liver", Journal of Biological Chemistry, vol. 272, no. 48, p. 30329-30333, 1997. https://doi.org/10.1074/jbc.272.48.30329
[3] P. Fernández-Llama, P. Andrews, R. Turner, S. Saggi, J. Dimari, T. Kwonet al., "Decreased abundance of collecting duct aquaporins in post-ischemic renal failure in rats", Journal of the American Society of Nephrology, vol. 10, no. 8, p. 1658-1668, 1999. https://doi.org/10.1681/asn.v1081658
[4] S. Wang, C. Ing, S. Emami, Y. Jiang, H. Liang, R. Pomèset al., "Structure and dynamics of extracellular loops in human aquaporin-1 from solid-state nmr and molecular dynamics", The Journal of Physical Chemistry B, vol. 120, no. 37, p. 9887-9902, 2016. https://doi.org/10.1021/acs.jpcb.6b06731
[5] Y. Yamazato, A. Shiozaki, D. Ichikawa, T. Kosuga, K. Shoda, T. Aritaet al., "Aquaporin 1 suppresses apoptosis and affects prognosis in esophageal squamous cell carcinoma", Oncotarget, vol. 9, no. 52, p. 29957-29974, 2018. https://doi.org/10.18632/oncotarget.25722
[6] D. Ruiz‐Carrillo, J. Ying, D. Darwis, C. Soon, T. Cornvik, J. Torreset al., "Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 å", Acta Crystallographica Section F Structural Biology Communications, vol. 70, no. 12, p. 1657-1663, 2014. https://doi.org/10.1107/s2053230x14024558
[7] B. Yang and A. Verkman, "Water and glycerol permeabilities of aquaporins 1–5 and mip determined quantitatively by expression of epitope-tagged constructs inxenopus oocytes", Journal of Biological Chemistry, vol. 272, no. 26, p. 16140-16146, 1997. https://doi.org/10.1074/jbc.272.26.16140
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