Abstract
Aquaporins are unique water channel proteins located at cell membranes that possess high water permeability and high solute rejection. Their primary function is to maintain the osmotic balance of the cells via regulating the water transport. However, their discovery had also provided the scientists to understand the pathophysiology of some diseases. In fact, aquaporins are shown to be strongly related to cancer by taking part in several tumor-related processes such as cell migration, cell proliferation and cell adhesion. Other than their functions in human body, recently, aquaporins have started to be used in engineering biomimetic membranes, for different applications such as desalination. This review investigates the properties and functions of the aquaporins in a multidisciplinary point of view and demonstrates the recent developments in aquaporin-based research.
Highlights
Water is essential for all molecular interactions required for anabolic and catabolic reactions vital to sustain life
In 1988, Agre et al from United States of America, Acta Medica 2020; 51(2): 30 - 42 first originally named this protein as CHIP 28 [3] with regard to its function in the linkage of the membrane skeleton to the lipid bilayer in RBC, later in 1992 they reported CHIP as the water channel protein in erythrocytes [4]
This study has shown that Epo may induce the expression of aquaporin 1 (AQP1) at mRNA and protein levels, and inhibition of AQP1 can lead to an impairment in the migration of EA.hy926 endothelial cells exposed to Epo, suggesting a potential use of aquaporin-targeting in angiogenesis-related diseases [32]
Summary
Water is essential for all molecular interactions required for anabolic and catabolic reactions vital to sustain life. The pioneering studies of the Georghe Benga and Peter Agre groups have revealed a protein, later named as aquaporin 1 (AQP1) in erythrocytes. Three-amino-acid sequence (Asn-Pro-Ala) NPA motifs are present: one in the half helices located at the amino-terminal (M3) and one in the other half located at the carboxy-terminal (M7) [5] These motifs contribute to the hydrophilic part of the amphiphilic pore and by acting as H-bond donors/acceptors, they take part in coordinating water/glycerol transport through the aquaporin [13]. Its deletion in mice causes dysfunctions in several processes such as wound healing or skin hydration as a result of inadequate amount of glycerol Another aquaglyceroporin AQP7 is expressed in adipocytes which regulates glycerol transportation through the cell [14].
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