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To produce the recombinant human Aquaporin-1 (AQP1), the gene coding for the AQP1 protein (2-269aa) is first isolated and inserted into a plasmid vector along with the N-terminal 6xHis-SUMO-tag gene. This vector is cultured in the in vitro E.coli expression system to induce the expression of the AQP1 protein. After sufficient growth, the culture supernatant is collected and purified to obtain the recombinant AQP1 protein. The purified AQP1 protein undergoes an SDS-PAGE test to measure its purity, greater than 90%.
AQP1 is a fundamental member of the aquaporin superfamily, serving as a prototype for understanding the rapid regulation of aquaporin function and cellular water transport mechanisms [1]. AQP1, the first identified aquaporin, is crucial for regulating membrane water permeability and is involved in various physiological processes such as water reabsorption in the kidney, vascular function, cell migration, and angiogenesis [2][3][4]. Studies have demonstrated that AQP1 translocates rapidly in response to stimuli, thereby regulating water flow across membranes [2]. Moreover, AQP1 has been associated with water balance disorders and is considered a potential target for conditions like glaucoma and cancer [3][4]. The tetrameric organization of AQP1 contributes to its functionality in facilitating water transport across membranes [4].
AQP1's expression in tissues like the gastrointestinal system and vascular smooth muscle cells highlights its significance in maintaining water balance and cellular function [5][6]. Structural studies utilizing techniques such as electron crystallography and solid-state NMR have provided insights into the extracellular loops and dynamics of AQP1 [7].
References:
[1] B. Jap, H. Li, & S. Lee, 3-d structure of a water channel at ˜6å resolution as determined by electron crystallography, Microscopy and Microanalysis, vol. 3, no. S2, p. 1031-1032, 1997. https://doi.org/10.1017/s1431927600012046
[2] M. Conner, A. Conner, C. Bland, L. Taylor, J. Brown, H. Parriet al., Rapid aquaporin translocation regulates cellular water flow, Journal of Biological Chemistry, vol. 287, no. 14, p. 11516-11525, 2012. https://doi.org/10.1074/jbc.m111.329219
[3] M. Knepper and S. Nielsen, Peter agre, 2003 nobel prize winner in chemistry, Journal of the American Society of Nephrology, vol. 15, no. 4, p. 1093-1095, 2004. https://doi.org/10.1097/01.asn.0000118814.47663.7d
[4] 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
[5] C. Shanahan, D. Connolly, K. Tyson, N. Cary, J. Osbourn, P. Agreet al., Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across vascular cell membranes, Journal of Vascular Research, vol. 36, no. 5, p. 353-362, 1999. https://doi.org/10.1159/000025674
[6] 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
[7] D. Fu, A. Libson, L. Miercke, C. Weitzman, P. Nollert, J. Krucinskiet al., Structure of a glycerol-conducting channel and the basis for its selectivity, Science, vol. 290, no. 5491, p. 481-486, 2000. https://doi.org/10.1126/science.290.5491.481
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