Special Issue "Aquaporins"

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (31 December 2018).

Special Issue Editor

Prof. Kenichi Ishibashi
E-Mail Website
Guest Editor
Department of Medical Physiology, School of Pharmacy, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo, 204–8588, Japan
Tel. +81-42-495-8502; Fax: +81-42-495-8502
Interests: transporter; channel; electrolyte homeostasis; nephrology
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

Aquaporins are ancient channels with a highly conserved internal-repeat structure, which primarily transport water as well as other small solutes such as glycerol and superoxide, or even gases. They are widely studied in biology and mostly function to adapt to the environment, especially water stress. They also play important roles in the field of agriculture and medicine.

This Special Issue welcomes original research and review papers addressing every aspect of aquaporins, including function and regulation in biology and medicine. Hopefully, interdisciplinary applications of the knowledge will stimulate future research.

Prof. Dr. Kenichi Ishibashi
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • aquaporin
  • water metabolism and urine concentration
  • dehydration and osmotic stress
  • free radical and inflammation
  • glycerol (fat) metabolism and energy balance
  • cell movement and metastasis
  • evolution and coevolution
  • prokaryotic and eukaryotic cells
  • structure–function relationship

Published Papers (19 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle
Aquaporins Respond to Chilling in the Phloem by Altering Protein and mRNA Expression
Cells 2019, 8(3), 202; https://doi.org/10.3390/cells8030202 - 27 Feb 2019
Abstract
Previous experiments using heat exchangers (liquid cooled blocks) to chill a portion of plant stem have shown a transient stoppage in phloem translocation and an increase in measured phloem pressure. Although a chilled-induced stoppage of phloem transport has been known for over 100 [...] Read more.
Previous experiments using heat exchangers (liquid cooled blocks) to chill a portion of plant stem have shown a transient stoppage in phloem translocation and an increase in measured phloem pressure. Although a chilled-induced stoppage of phloem transport has been known for over 100 years, the mechanism of this phenomenon is still poorly understood. Recently, work has highlighted that aquaporins occur within the plasma membrane of the sieve tubes along the entire source-to-sink pathway, and that isoforms of these water channel proteins may change dynamically. Aquaporins show regulatory roles in controlling tissue and cellular water status in response to environmental hardships. Thus, we tested if protein localization and mRNA transcript abundance changes occur in response to chilling in balsam poplar (Populus balsamifera) using immunohistochemistry and qrtPCR. The results of the immunolocalization experiments show that the labeling intensity of the sieve elements treated for only 2 min of chill time significantly increased for PIP2. After 10 min of chilling, this signal declined significantly to lower than that of the pre-chilled sieve elements. Overall, the abundance of mRNA transcript increased for the tested PIP2s following cold application. We discuss the implication that aquaporins are responsible for the alleviation of sieve tube pressure and the resumption of flow following a cold-induced blockage event. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Open AccessArticle
AQP1 and AQP4 Contribution to Cerebrospinal Fluid Homeostasis
Cells 2019, 8(2), 197; https://doi.org/10.3390/cells8020197 - 24 Feb 2019
Cited by 1
Abstract
Aquaporin 1 (AQP1), expressed in epithelial cells of the choroid plexus, and aquaporin 4 (AQP4) present in ependymal cells and glia limitants have been proposed to play a significant role in cerebrospinal fluid (CSF) production and homeostasis. However, the specific contribution of each [...] Read more.
Aquaporin 1 (AQP1), expressed in epithelial cells of the choroid plexus, and aquaporin 4 (AQP4) present in ependymal cells and glia limitants have been proposed to play a significant role in cerebrospinal fluid (CSF) production and homeostasis. However, the specific contribution of each water channel to these functions remains unknown, being a subject of debate during the last years. Here, we analyzed in detail how AQP1 and AQP4 participate in different aspects of the CSF homeostasis such as the load and drainage of ventricles, and further explored if these proteins play a role in the ventricular compliance. To do that, we carried out records of intraventricular pressure and CSF outflow, and evaluated ventricular volume by magnetic resonance imaging in AQP1−/−, AQP4−/−, double AQP1−/−-AQP4−/− knock out and wild type mice controls. The analysis performed clearly showed that both AQPs have a significant participation in the CSF production, and additionally revealed that the double AQP1-AQP4 mutation alters the CSF drainage and the ventricular compliance. The data reported here indicate a significant extra-choroidal CSF formation mediated by AQP4, supporting the idea of an important and constant CSF production/absorption process, sustained by efflux/influx of water between brain capillaries and interstitial fluid. Moreover, our results suggest the participation of AQPs in structural functions also related with CSF homeostasis such as the distensibility capacity of the ventricular system. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessArticle
An Early Decrease in Release of Aquaporin-2 in Urinary Extracellular Vesicles After Cisplatin Treatment in Rats
Cells 2019, 8(2), 139; https://doi.org/10.3390/cells8020139 - 10 Feb 2019
Cited by 3
Abstract
Aquaporin-1 (AQP1) and AQP2 are important proteins involved in the regulation of renal water handling. Both AQPs have been found in urinary extracellular vesicles (uEVs) (uEV-AQP1 and -AQP2). Cisplatin, an antineoplastic agent, is known to down-regulate renal AQP1 and AQP2. However, the effect [...] Read more.
Aquaporin-1 (AQP1) and AQP2 are important proteins involved in the regulation of renal water handling. Both AQPs have been found in urinary extracellular vesicles (uEVs) (uEV-AQP1 and -AQP2). Cisplatin, an antineoplastic agent, is known to down-regulate renal AQP1 and AQP2. However, the effect of cisplatin on the release of uEV-AQP1 and -AQP2 is largely unknown. In this study, we examined whether treatment of rats with cisplatin affected the release of uEV-AQP1 and -AQP2. Blood tests indicated that renal function was little altered at 24 h after cisplatin treatment but thereafter decreased dramatically at all of the other time points examined. Release of uEV-AQP1 was slightly increased at 24 h and decreased at 168 h. On the other hand, release of uEV-AQP2 was decreased dramatically at 24 h, and the decrease was maintained during the experimental period. These data suggest that uEV-AQP2 can be used to detect early renal impairment due to cisplatin. Furthermore, a combination of uEV-AQP2 and -AQP1 may be useful for estimation of cisplatin-induced renal injury in a stage-dependent manner. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessArticle
Host-Cell Type Dependent Features of Recombinant Human Aquaporin-4 Orthogonal Arrays of Particles—New Insights for Structural and Functional Studies
Cells 2019, 8(2), 119; https://doi.org/10.3390/cells8020119 - 02 Feb 2019
Abstract
The CNS plasma-membrane water channel aquaporin-4 (AQP4) is expressed as two major isoforms able to aggregate into supramolecular assemblies known as ‘orthogonal arrays of particles’ (OAPs). OAP subnanometric features are largely unknown mainly because a method for the expression, isolation, and crystallization of [...] Read more.
The CNS plasma-membrane water channel aquaporin-4 (AQP4) is expressed as two major isoforms able to aggregate into supramolecular assemblies known as ‘orthogonal arrays of particles’ (OAPs). OAP subnanometric features are largely unknown mainly because a method for the expression, isolation, and crystallization of integral human OAPs has not been developed. Here, the human OAP-forming isoform M23-AQP4 was expressed in insect and mammalian cell lines and AQP4 and OAP features evaluated. Native size exclusion chromatography was employed to isolate and analyze authentically folded OAPs, and neuromyelitis optica (NMO)-specific sandwich ELISA was developed to test OAP-integrity. The results demonstrate that in insect cells most AQP4 remains intracellular and unfolded and that OAPs are largely disassembled after the detergent extraction step. In mammalian cells, AQP4 showed regular plasma membrane targeting and OAPs exhibited strong post-extraction stability. Starting from the mammalian cell expression system, we isolated authentically folded OAPs. Together these data suggest a new strategy for expressing and isolating integral recombinant human OAPs and providing new insights into the cell-type dependent OAP-assembly and post-extraction stability, potentially useful to design new approaches for structural and functional studies of OAP and for other plasma membrane proteins organized into supramolecular structures. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Open AccessArticle
Gi Protein Modulation of the Potassium Channel TASK-2 Mediates Vesicle Osmotic Swelling to Facilitate the Fusion of Aquaporin-2 Water Channel Containing Vesicles
Cells 2018, 7(12), 276; https://doi.org/10.3390/cells7120276 - 19 Dec 2018
Abstract
Vesicle fusion is a fundamental cell biological process similar from yeasts to humans. For secretory vesicles, swelling is considered a step required for the expulsion of intravesicular content. Here this concept is revisited providing evidence that it may instead represent a general mechanism. [...] Read more.
Vesicle fusion is a fundamental cell biological process similar from yeasts to humans. For secretory vesicles, swelling is considered a step required for the expulsion of intravesicular content. Here this concept is revisited providing evidence that it may instead represent a general mechanism. We report the first example that non-secretory vesicles, committed to insert the Aquaporin-2 water channel into the plasma membrane, swell and this phenomenon is required for fusion to plasma membrane. Through an interdisciplinary approach, using atomic force microscope (AFM), a fluorescence-based assay of vesicle volume changes and NMR spectroscopy to measure water self-diffusion coefficient, we provide evidence that Gi protein modulation of potassium channel TASK-2 localized in AQP2 vesicles, is required for vesicle swelling. Estimated intravesicular K+ concentration in AQP2 vesicles, as measured by inductively coupled plasma mass spectrometry, was 5.3 mM, demonstrating the existence of an inwardly K+ chemical gradient likely generating an osmotic gradient causing vesicle swelling upon TASK-2 gating. Of note, abrogation of K+ gradient significantly impaired fusion between vesicles and plasma membrane. We conclude that vesicle swelling is a potentially important prerequisite for vesicle fusion to the plasma membrane and may be required also for other non-secretory vesicles, depicting a general mechanism for vesicle fusion. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessArticle
Systemic Hypertension Effects on the Ciliary Body and Iris. An Immunofluorescence Study with Aquaporin 1, Aquaporin 4, and Na+, K+ ATPase in Hypertensive Rats
Cells 2018, 7(11), 210; https://doi.org/10.3390/cells7110210 - 13 Nov 2018
Cited by 2
Abstract
Aquaporin 1 (AQP1) and aquaporin 4 (AQP4) have been identified in the eye as playing an essential role in the formation of the aqueous humor along with the Na+/K+ ATPase pump. Different authors have described the relationship between blood pressure, [...] Read more.
Aquaporin 1 (AQP1) and aquaporin 4 (AQP4) have been identified in the eye as playing an essential role in the formation of the aqueous humor along with the Na+/K+ ATPase pump. Different authors have described the relationship between blood pressure, aqueous humor production, and intraocular pressure with different conclusions, with some authors supporting a positive correlation between blood pressure and intraocular pressure while others disagree. The aim of this work was to study the effect of high blood pressure on the proteins involved in the production of aqueous humor in the ciliary body (CB) and iris. For this purpose, we used the eyes of spontaneously hypertensive rats (SHR) and their control Wistar-Kyoto rats (WKY). Immunofluorescence was performed in different eye structures to analyze the effects of hypertension in the expression of AQP1, AQP4, and the Na+/K+ ATPase α1 and α2 subunits. The results showed an increase in AQP1 and Na+/K+ ATPase α1 and a decrease in AQP4 and Na+/K+ ATPase α2 in the CB of SHR, while an increase in AQP4 and no significant differences in AQP1 were found in the iris. Therefore, systemic hypertension produced changes in the proteins implicated in the movement of water in the CB and iris that could influence the production rate of aqueous humor, which would be affected depending on the duration of systemic hypertension. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessArticle
Molecular Basis of Aquaporin-7 Permeability Regulation by pH
Cells 2018, 7(11), 207; https://doi.org/10.3390/cells7110207 - 10 Nov 2018
Cited by 6
Abstract
The aquaglyceroporin AQP7, a family member of aquaporin membrane channels, facilitates the permeation of water and glycerol through cell membranes and is crucial for body lipid and energy homeostasis. Regulation of glycerol permeability via AQP7 is considered a promising therapeutic strategy towards fat-related [...] Read more.
The aquaglyceroporin AQP7, a family member of aquaporin membrane channels, facilitates the permeation of water and glycerol through cell membranes and is crucial for body lipid and energy homeostasis. Regulation of glycerol permeability via AQP7 is considered a promising therapeutic strategy towards fat-related metabolic complications. Here, we used a yeast aqy-null strain for heterologous expression and functional analysis of human AQP7 and investigated its regulation by pH. Using a combination of in vitro and in silico approaches, we found that AQP7 changes from fully permeable to virtually closed at acidic pH, and that Tyr135 and His165 facing the extracellular environment are crucial residues for channel permeability. Moreover, instead of reducing the pore size, the protonation of key residues changes AQP7’s protein surface electrostatic charges, which, in turn, may decrease glycerol’s binding affinity to the pore, resulting in decreased permeability. In addition, since some pH-sensitive residues are located at the monomer-monomer interface, decreased permeability may result from cooperativity between AQP7’s monomers. Considering the importance of glycerol permeation via AQP7 in multiple pathophysiological conditions, this mechanism of hAQP7 pH-regulation may help the design of selective modulators targeting aquaglyceroporin-related disorders. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Open AccessArticle
Blue Light Induces Down-Regulation of Aquaporin 1, 3, and 9 in Human Keratinocytes
Cells 2018, 7(11), 197; https://doi.org/10.3390/cells7110197 - 03 Nov 2018
Cited by 2Retraction
Abstract
The development in digital screen technology has exponentially increased in the last decades, and many of today’s electronic devices use light-emitting diode (LED) technology producing very strong blue light (BL) waves. Long-term exposure at LED-BL seems to have an implication in the dehydration [...] Read more.
The development in digital screen technology has exponentially increased in the last decades, and many of today’s electronic devices use light-emitting diode (LED) technology producing very strong blue light (BL) waves. Long-term exposure at LED-BL seems to have an implication in the dehydration of the epidermis, in the alterations of shape and number of the keratinocytes, and in the aging of the skin. Aquaporins (AQPs) are water membrane channels that permeate both water and glycerol and play an important role in the hydration of epidermis, as well as in proliferation and differentiation of keratinocytes. Thus, we have hypothesized that AQPs could be involved in the aging of the skin exposed to LED-BL. Therefore, we have examined the expression of AQPs in human keratinocytes exposed to LED-BL at dose of 45 J/cm2, used as an in vitro model to produce the general features of photo aging of the skin. The aim was to verify if LED-BL induces changes of the basal levels of AQPs. The keratinocytes exposure to LED-BL produced an increase of reactive oxygen species (ROS), an activation of 8-hydroxy-2’-deoxyguanosine (8-OHdG), an alteration of proliferating cell nuclear antigen (PCNA), and a down-regulation of AQP1, 3 and 9. These findings are preliminary evidences that may be used as starting points for further investigations about the mechanistic involvement of AQP1, 3, and 9 in LED-BL-induced skin aging. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Open AccessArticle
Whole-Genome and Expression Analyses of Bamboo Aquaporin Genes Reveal Their Functions Involved in Maintaining Diurnal Water Balance in Bamboo Shoots
Cells 2018, 7(11), 195; https://doi.org/10.3390/cells7110195 - 02 Nov 2018
Cited by 4
Abstract
Water supply is essential for maintaining normal physiological function during the rapid growth of bamboo. Aquaporins (AQPs) play crucial roles in water transport for plant growth and development. Although 26 PeAQPs in bamboo have been reported, the aquaporin-led mechanism of maintaining diurnal [...] Read more.
Water supply is essential for maintaining normal physiological function during the rapid growth of bamboo. Aquaporins (AQPs) play crucial roles in water transport for plant growth and development. Although 26 PeAQPs in bamboo have been reported, the aquaporin-led mechanism of maintaining diurnal water balance in bamboo shoots remains unclear. In this study, a total of 63 PeAQPs were identified, based on the updated genome of moso bamboo (Phyllostachys edulis), including 22 PePIPs, 20 PeTIPs, 17 PeNIPs, and 4 PeSIPs. All of the PeAQPs were differently expressed in 26 different tissues of moso bamboo, based on RNA sequencing (RNA-seq) data. The root pressure in shoots showed circadian rhythm changes, with positive values at night and negative values in the daytime. The quantitative real-time PCR (qRT-PCR) result showed that 25 PeAQPs were detected in the base part of the shoots, and most of them demonstrated diurnal rhythm changes. The expression levels of some PeAQPs were significantly correlated with the root pressure. Of the 86 sugar transport genes, 33 had positive co-expression relationships with 27 PeAQPs. Two root pressure-correlated PeAQPs, PeTIP4;1 and PeTIP4;2, were confirmed to be highly expressed in the parenchyma and epidermal cells of bamboo culm, and in the epidermis, pith, and primary xylem of bamboo roots by in situ hybridization. The authors’ findings provide new insights and a possible aquaporin-led mechanism for bamboo fast growth. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Open AccessArticle
The Relationship between Turgor Pressure Change and Cell Hydraulics of Midrib Parenchyma Cells in the Leaves of Zea mays
Cells 2018, 7(10), 180; https://doi.org/10.3390/cells7100180 - 22 Oct 2018
Cited by 1
Abstract
Leaf dehydration decreases water potential and cell turgor pressure. Therefore, changes in cell turgor pressure may regulate water transport across plant cell membranes. Using a cell pressure probe, the hydraulic properties of parenchyma cells in the midrib of maize (Zea mays L.) [...] Read more.
Leaf dehydration decreases water potential and cell turgor pressure. Therefore, changes in cell turgor pressure may regulate water transport across plant cell membranes. Using a cell pressure probe, the hydraulic properties of parenchyma cells in the midrib of maize (Zea mays L.) leaves were measured (half time T 1 / 2 of water exchange in cells as a measure of hydraulic conductivity Lp). Using intact plants with root systems encased in a pressure chamber, the root systems were pressurized and the turgor pressure in leaf cells increased by increments up to 0.3 MPa. However, the increase in the cell turgor did not increase but stabilized T 1 / 2 values. Increased water potential in leaf cells seemed to have stabilizing effects on the T 1 / 2 probably due to enhanced water availability. When the cell turgor decreased by 0.1 MPa to 0.3 MPa with releasing the pressure in the pressure chamber, T 1 / 2 was temporarily increased to a large degree, a factor of up to 13 within 30 min. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessArticle
Estrogen Modulates Glycerol Permeability in Sertoli Cells through Downregulation of Aquaporin-9
Cells 2018, 7(10), 153; https://doi.org/10.3390/cells7100153 - 28 Sep 2018
Cited by 5
Abstract
High 17β-Estradiol (E2) levels are known to cause alterations of spermatogenesis and environments throughout the male reproductive tract. Sertoli cells (SCs) ensure an adequate environment inside the seminiferous tubule. Glycerol stands as essential for the maintenance of blood–testis barrier created by SCs, however, [...] Read more.
High 17β-Estradiol (E2) levels are known to cause alterations of spermatogenesis and environments throughout the male reproductive tract. Sertoli cells (SCs) ensure an adequate environment inside the seminiferous tubule. Glycerol stands as essential for the maintenance of blood–testis barrier created by SCs, however, the role of E2 in this process is not known. Herein, we hypothesized that the effect of E2 on glycerol permeability in mouse SCs (mSCs) could be mediated by aquaglyceroporins. The expression of aquaglyceroporins was assessed by RT-PCR and qRT-PCR. Glycerol permeability was evaluated by stopped-flow light scattering. We were able to identify the expression of AQP3 and AQP9 in mSCs where AQP9 is more abundant than AQP3. Our results show that high E2 levels decrease AQP9 mRNA abundance with no influence on AQP3 in mSCs. Interestingly, high E2 levels decreased mSCs’ permeability to glycerol, while downregulating AQP9 expression, thus suggesting a novel mechanism by which E2 modulates fluid secretion in the testis. In conclusion, E2 is an important regulator of mSCs physiology and secretion through changes in AQP9 expression and function. Thus, alterations in glycerol permeability induced by E2 may be the cause for male infertility in cases associated with the presence of high E2 levels. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessArticle
The Purified Extract from the Medicinal Plant Bacopa monnieri, Bacopaside II, Inhibits Growth of Colon Cancer Cells In Vitro by Inducing Cell Cycle Arrest and Apoptosis
Cells 2018, 7(7), 81; https://doi.org/10.3390/cells7070081 - 21 Jul 2018
Cited by 11
Abstract
Aquaporin-1 (AQP1), a transmembrane pore-forming molecule, facilitates the rapid movement of water and small solutes across cell membranes. We have previously shown that bacopaside II, an extract from the medicinal herb Bacopa monnieri, blocks the AQP1 water channel and impairs migration of [...] Read more.
Aquaporin-1 (AQP1), a transmembrane pore-forming molecule, facilitates the rapid movement of water and small solutes across cell membranes. We have previously shown that bacopaside II, an extract from the medicinal herb Bacopa monnieri, blocks the AQP1 water channel and impairs migration of cells that express AQP1. The aim of this study was to further elucidate the anti-tumour potential of bacopaside II in colon cancer cells. Expression of AQP1 in HT-29, SW480, SW620 and HCT116 was determined by quantitative PCR and western immunoblot. Cells were treated with bacopaside II, and morphology, growth, autophagy, cell cycle and apoptosis assessed by time-lapse microscopy, crystal violet, acridine orange, propidium iodide (PI) and annexin V/PI staining respectively. AQP1 expression was significantly higher in HT-29 than SW480, SW620 and HCT116. Bacopaside II significantly reduced growth at ≥20 µM for HT-29 and ≥15 µM for SW480, SW620 and HCT116. Inhibition of HT-29 at 20 µM was primarily mediated by G0/G1 cell cycle arrest, and at 30 µM by G2/M arrest and apoptosis. Inhibition of SW480, SW620 and HCT116 at ≥15 µM was mediated by G2/M arrest and apoptosis. These results are the first to show that bacopaside II inhibits colon cancer cell growth by inducing cell cycle arrest and apoptosis. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Review

Jump to: Research

Open AccessReview
Aquaporin-4 Water Channel in the Brain and Its Implication for Health and Disease
Cells 2019, 8(2), 90; https://doi.org/10.3390/cells8020090 - 27 Jan 2019
Cited by 5
Abstract
Aquaporin-4 (AQP4) is a water channel expressed on astrocytic endfeet in the brain. The role of AQP4 has been studied in health and in a range of pathological conditions. Interest in AQP4 has increased since it was discovered to be the target antigen [...] Read more.
Aquaporin-4 (AQP4) is a water channel expressed on astrocytic endfeet in the brain. The role of AQP4 has been studied in health and in a range of pathological conditions. Interest in AQP4 has increased since it was discovered to be the target antigen in the inflammatory autoimmune disease neuromyelitis optica spectrum disorder (NMOSD). Emerging data suggest that AQP4 may also be implicated in the glymphatic system and may be involved in the clearance of beta-amyloid in Alzheimer’s disease (AD). In this review, we will describe the role of AQP4 in the adult and developing brain as well as its implication for disease. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessReview
Phosphorylation-Dependent Regulation of Mammalian Aquaporins
Cells 2019, 8(2), 82; https://doi.org/10.3390/cells8020082 - 23 Jan 2019
Cited by 4
Abstract
Water homeostasis is fundamental for cell survival. Transport of water across cellular membranes is governed by aquaporins—tetrameric integral membrane channels that are highly conserved throughout the prokaryotic and eukaryotic kingdoms. In eukaryotes, specific regulation of these channels is required and is most commonly [...] Read more.
Water homeostasis is fundamental for cell survival. Transport of water across cellular membranes is governed by aquaporins—tetrameric integral membrane channels that are highly conserved throughout the prokaryotic and eukaryotic kingdoms. In eukaryotes, specific regulation of these channels is required and is most commonly carried out by shuttling the protein between cellular compartments (trafficking) or by opening and closing the channel (gating). Structural and functional studies have revealed phosphorylation as a ubiquitous mechanism in aquaporin regulation by both regulatory processes. In this review we summarize what is currently known about the phosphorylation-dependent regulation of mammalian aquaporins. Focusing on the water-specific aquaporins (AQP0–AQP5), we discuss how gating and trafficking are controlled by phosphorylation and how phosphorylation affects the binding of aquaporins to regulatory proteins, thereby highlighting structural details and dissecting the contribution of individual phosphorylated residues when possible. Our aim is to provide an overview of the mechanisms behind how aquaporin phosphorylation controls cellular water balance and to identify key areas where further studies are needed. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Open AccessReview
Exploring the Roles of Aquaporins in Plant–Microbe Interactions
Cells 2018, 7(12), 267; https://doi.org/10.3390/cells7120267 - 11 Dec 2018
Cited by 3
Abstract
Aquaporins (AQPs) are membrane channel proteins regulating the flux of water and other various small solutes across membranes. Significant progress has been made in understanding the roles of AQPs in plants’ physiological processes, and now their activities in various plant–microbe interactions are receiving [...] Read more.
Aquaporins (AQPs) are membrane channel proteins regulating the flux of water and other various small solutes across membranes. Significant progress has been made in understanding the roles of AQPs in plants’ physiological processes, and now their activities in various plant–microbe interactions are receiving more attention. This review summarizes the various roles of different AQPs during interactions with microbes which have positive and negative consequences on the host plants. In positive plant–microbe interactions involving rhizobia, arbuscular mycorrhizae (AM), and plant growth-promoting rhizobacteria (PGPR), AQPs play important roles in nitrogen fixation, nutrient transport, improving water status, and increasing abiotic stress tolerance. For negative interactions resulting in pathogenesis, AQPs help plants resist infections by preventing pathogen ingress by influencing stomata opening and influencing defensive signaling pathways, especially through regulating systemic acquired resistance. Interactions with bacterial or viral pathogens can be directly perturbed through direct interaction of AQPs with harpins or replicase. However, whilst these observations indicate the importance of AQPs, further work is needed to develop a fuller mechanistic understanding of their functions. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessReview
Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement
Cells 2018, 7(11), 209; https://doi.org/10.3390/cells7110209 - 11 Nov 2018
Cited by 5
Abstract
Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly [...] Read more.
Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly altering the membrane permeability. This review is focused on evidence that highlights the functional relationship between the monomers and the tetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanisms that affect the monomer, the tetramer, or tetramers combined in complex structures. We therefore explore: (i) water permeation and recent evidence on ion permeation, including the permeation pathway controversy—each monomer versus the central pore of the tetramer—and (ii) regulatory mechanisms that cannot be attributed to independent monomers. In particular, we discuss channel gating and AQPs that sense membrane tension. For the latter we propose a possible mechanism that includes the monomer (slight changes of pore shape, the number of possible H-bonds between water molecules and pore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect). Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessReview
The Expanding Role of Vesicles Containing Aquaporins
Cells 2018, 7(10), 179; https://doi.org/10.3390/cells7100179 - 22 Oct 2018
Cited by 2
Abstract
In animals and plants, membrane vesicles containing proteins have been defined as key for biological systems involving different processes such as trafficking or intercellular communication. Docking and fusion of vesicles to the plasma membrane occur in living cells in response to different stimuli, [...] Read more.
In animals and plants, membrane vesicles containing proteins have been defined as key for biological systems involving different processes such as trafficking or intercellular communication. Docking and fusion of vesicles to the plasma membrane occur in living cells in response to different stimuli, such as environmental changes or hormones, and therefore play an important role in cell homeostasis as vehicles for certain proteins or other substances. Because aquaporins enhance the water permeability of membranes, their role as proteins immersed in vesicles formed of natural membranes is a recent topic of study. They regulate numerous physiological processes and could hence serve new biotechnological purposes. Thus, in this review, we have explored the physiological implications of the trafficking of aquaporins, the mechanisms that control their transit, and the proteins that coregulate the migration. In addition, the importance of exosomes containing aquaporins in the cell-to-cell communication processes in animals and plants have been analyzed, together with their potential uses in biomedicine or biotechnology. The properties of aquaporins make them suitable for use as biomarkers of different aquaporin-related diseases when they are included in exosomes. Finally, the fact that these proteins could be immersed in biomimetic membranes opens future perspectives for new biotechnological applications. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessReview
Aquaporins and Their Regulation after Spinal Cord Injury
Cells 2018, 7(10), 174; https://doi.org/10.3390/cells7100174 - 18 Oct 2018
Cited by 2
Abstract
After injury to the spinal cord, edema contributes to the underlying detrimental pathophysiological outcomes that lead to worsening of function. Several related membrane proteins called aquaporins (AQPs) regulate water movement in fluid transporting tissues including the spinal cord. Within the cord, AQP1, 4 [...] Read more.
After injury to the spinal cord, edema contributes to the underlying detrimental pathophysiological outcomes that lead to worsening of function. Several related membrane proteins called aquaporins (AQPs) regulate water movement in fluid transporting tissues including the spinal cord. Within the cord, AQP1, 4 and 9 contribute to spinal cord injury (SCI)-induced edema. AQP1, 4 and 9 are expressed in a variety of cells including astrocytes, neurons, ependymal cells, and endothelial cells. This review discusses some of the recent findings of the involvement of AQP in SCI and highlights the need for further study of these proteins to develop effective therapies to counteract the negative effects of SCI-induced edema. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Figure 1

Open AccessReview
Aquaporin Activity to Improve Crop Drought Tolerance
Cells 2018, 7(9), 123; https://doi.org/10.3390/cells7090123 - 29 Aug 2018
Cited by 8
Abstract
In plants, aquaporins (AQP) occur in multiple isoforms in both plasmalemma and tonoplast membranes resulting in regulation of water flow in and out of cells, and ultimately, water transfer through a series of cells in leaves and roots. Consequently, it is not surprising [...] Read more.
In plants, aquaporins (AQP) occur in multiple isoforms in both plasmalemma and tonoplast membranes resulting in regulation of water flow in and out of cells, and ultimately, water transfer through a series of cells in leaves and roots. Consequently, it is not surprising that physiological and molecular studies have identified AQPs as playing key roles in regulating hydraulic conductance in roots and leaves. As a result, the activity of AQPs influences a range of physiological processes including phloem loading, xylem water exit, stomatal aperture and gas exchange. The influence of AQPs on hydraulic conductance in plants is particularly important in regulating plant transpiration rate, particularly under conditions of developing soil water-deficit stress and elevated atmospheric vapor pressure deficit (VPD). In this review, we examine the impact of AQP activity and hydraulic conductance on crop water use and the identification of genotypes that express soil water conservation as a result of these traits. An important outcome of this research has been the identification and commercialization of cultivars of peanut (Arachis hypogaea L.), maize (Zea mays L.), and soybean (Glycine max (Merr) L.) for dry land production systems. Full article
(This article belongs to the Special Issue Aquaporins)
Show Figures

Graphical abstract

Back to TopTop