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New Insights into Aquaporins: 2nd Edition
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New Insights into Aquaporins: 2nd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 July 2025 | Viewed by 6150

Special Issue Editors

Dr. Graça Soveral

E-Mail Website
Guest Editor
Research Institute for Medicines (iMed.ULisboa), Faculdade de Farmacia, Universidaded de Lisboa, Lisbon, Portugal
Interests: water and solute transport; membrane; pathophysiology; metabolism; cancer
Special Issues, Collections and Topics in MDPI journals
Dr. Inês Vieira Da Silva

E-Mail Website
Guest Editor
Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisboa, Portugal
Interests: aquaporin; inflammation; immunology; metabolic diseases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Aquaporins (AQPs) are involved in many biological functions, including transepithelial fluid transport, cell migration and proliferation, brain edema and neuroexcitation, adipocyte metabolism, and epidermal water retention. In the plant kingdom, aquaporins are key proteins providing strict regulation of water uptake and transport across cellular membranes and tissues at the whole-plant level, regulating plant growth and development. Over the last decade, aquaporins have become a hot area of research in molecular cell biology, biochemistry, and biophysics, with increasing physiological and medical implications. In addition, human diseases caused by aquaporin dysfunction have unveiled these proteins’ potential as drug targets and opened new perspectives with which to untangle mechanisms of disease.

This Special Issue aims to provide an updated scientific view of the aquaporin field, including structure–function relationships, physiological and chemical regulation, implications in disease, and potential as drug targets, creating opportunities for drug development and novel therapies. Authors are invited to submit original research and review papers addressing these topics for this Special Issue.

Dr. Graça Soveral
Dr. Inês Vieira Da Silva
Guest Editors

Manuscript Submission Information

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Keywords

  • aquaporin
  • membrane channel
  • regulation
  • pathophysiology
  • drug target

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Related Special Issue

Published Papers (5 papers)

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Research

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28 pages, 9411 KiB  
Article
Localization and Expression of Aquaporin 1 (AQP1) in the Tissues of the Spiny Dogfish (Squalus acanthias)
by Christopher P. Cutler and Bryce MacIver
Int. J. Mol. Sci. 2025, 26(12), 5593; https://doi.org/10.3390/ijms26125593 - 11 Jun 2025
Abstract
Aquaporin 1 is a membrane water channel protein, which was studied here in spiny dogfish (Squalus acanthias) osmoregulatory tissues using a variety of techniques. The cloning of aquaporin 1 (AQP1) in the spiny dogfish identified a splice variant version [...] Read more.
Aquaporin 1 is a membrane water channel protein, which was studied here in spiny dogfish (Squalus acanthias) osmoregulatory tissues using a variety of techniques. The cloning of aquaporin 1 (AQP1) in the spiny dogfish identified a splice variant version of the mRNA/protein (AQP1SV1/AQP1SV1). Polymerase chain reaction (PCR) in a range of tissues showed AQP1 to be expressed at very high levels in the rectal gland with ubiquitous mRNA expression at lower levels in other tissues. Northern blotting showed that AQP1 had a mRNA size of 5.3 kb in kidney total RNA. The level of AQP1 mRNA was significantly lower in the rectal glands of fish acclimated to 120% seawater (SW; vs. 75% SW (p = 0.0007) and 100% SW (p = 0.0025)) but was significantly higher in those fish in the kidney (vs. 100% SW (p = 0.0178)) and intestine (vs. 75% SW (p= 0.0355) and 100% SW (p = 0.0285)). Quantitative PCR determined that AQP1SV1 mRNA levels were also significantly lower in the rectal glands of both 120% (p = 0.0134) and 100% SW (p = 0.0343) fish in comparison to 75% SW-acclimated dogfish. Functional expression in Xenopus oocytes showed that AQP1 exhibited significant apparent membrane water permeability (p = 0.000008–0.0158) across a range of pH values, whereas AQP1SV1 showed no similar permeability. Polyclonal antibodies produced against AQP1 (AQP1 and AQP1/2 antibodies) and AQP1SV1 had bands at the expected sizes of 28 kDa and 24 kDa, respectively, as well as some other banding. The weak AQP1 antibody and the stronger AQP1/2 antibody exhibited staining in the apical membranes of rectal gland secretory tubules, particularly towards the periphery of the gland. In the gill, the AQP1/2 antibody in particular showed staining in secondary-lamellar pavement-cell basal membranes, and in blood vessels and connective tissue in the gill arch. In the spiral valve intestine side wall and valve flap, the AQP1/2 antibody stained muscle tissue and blood vessel walls and, after tyramide signal amplification, showed some staining in the apical membranes of epithelial cells at the ends of the luminal surface of epithelial folds. In the rectum/colon, there was also some muscle and blood vessel staining, but the AQP1 and AQP1/2 antibodies both stained a layer of cells at the base of the surface epithelium. In the kidney convoluted bundle zone, all three antibodies stained bundle sheath membranes to variable extents, and the AQP1/2 antibody also showed staining in the straight bundle zone bundle sheath. In the kidney sinus zone, the AQP1/2 antibody stained the apical membranes of late distal tubule (LDT) nephron loop cells most strongly, with the strongest staining in the middle of the LDT loop and in patches towards the start of the LDT loop. There was also a somewhat less strong staining of segments of the first sinus zone nephron loop, particularly in the intermediate I (IS-I) tubule segment. Some tubules appeared to show no or only low levels of staining. The results suggest that AQP1 plays a role in rectal gland fluid secretion, kidney fluid reabsorption and gill pavement-cell volume regulation and probably a minor role in intestinal/rectal/colon fluid absorption. Full article
(This article belongs to the Special Issue New Insights into Aquaporins: 2nd Edition)
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14 pages, 2123 KiB  
Article
Detection of Androgen Receptors in Spermatozoa of Small Ruminants: A Putative Modulation Pathway for Cryoresistance Through AQP3
by Esther Alba, Cristina Castaño, Adolfo Toledano-Díaz, Rosario Velázquez, Belén Martínez-Madrid, Alberto Gómez-Crespo, Manuel Álvarez-Rodríguez, Heriberto Rodriguez-Martinez and Julián Santiago-Moreno
Int. J. Mol. Sci. 2024, 25(22), 11972; https://doi.org/10.3390/ijms252211972 - 7 Nov 2024
Viewed by 1081
Abstract
This work was aimed to identify androgen receptors (AR) in the spermatozoa of wild and domestic ruminants and to assess the effect of testosterone on sperm localization of aquaporin-3 (AQP3) and cryopreservation process. Sperm samples from wild species were incubated with testosterone (T [...] Read more.
This work was aimed to identify androgen receptors (AR) in the spermatozoa of wild and domestic ruminants and to assess the effect of testosterone on sperm localization of aquaporin-3 (AQP3) and cryopreservation process. Sperm samples from wild species were incubated with testosterone (T group), 1,3-propanediol (PDO group), phloretin (PHL group), PDO+T group, PHL+T group. Western blot identified the presence of AR as a single band of about 48 KDa. Immunolabelling of AR was located in the equatorial segment of the sperm head. In mouflons, the cryoresistance ratio for acrosome integrity was lower (p < 0.05) in the PHL+T than in Control and T groups. In ibexes, the cryoresistance ratio for acrosome integrity was lower (p < 0.05) in the PHL+T, PHL, and T group than in the Control group; the cryoresistance ratios for sperm kinematic variables were lower (p < 0.05) in PDO+T than in Control. No changes were found among treatments in the proportion of spermatozoa showing AQP3 in the different membrane domains after incubation and thawing in both mouflon and ibex. In conclusion, testosterone negatively affected sperm cryoresistance expressed as acrosome integrity, enhancing the effects of the AQP blocker PHL. Our findings provide a sound knowledge of the molecular mechanisms that explain the seasonal variation in sperm freezability from ruminants. Full article
(This article belongs to the Special Issue New Insights into Aquaporins: 2nd Edition)
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15 pages, 2866 KiB  
Article
Glycerol Handling in Paired Visceral and Subcutaneous Adipose Tissues in Women with Normal Weight and Upper-Body Obesity
by Anne Nørholm, Ida Guldbrandt Kjær, Esben Søndergaard, Birgitte Nellemann, Søren Nielsen and Janne Lebeck
Int. J. Mol. Sci. 2024, 25(16), 9008; https://doi.org/10.3390/ijms25169008 - 19 Aug 2024
Viewed by 1156
Abstract
In adipose tissue, reduced expression of the glycerol channel aquaporin 7 (AQP7) has been associated with increased accumulation of triglyceride. The present study determines the relative protein abundances of lipolytic enzymes, AQP7, and cytosolic phosphoenolpyruvate carboxykinase (PEPCK-C) in paired mesenteric and omental visceral [...] Read more.
In adipose tissue, reduced expression of the glycerol channel aquaporin 7 (AQP7) has been associated with increased accumulation of triglyceride. The present study determines the relative protein abundances of lipolytic enzymes, AQP7, and cytosolic phosphoenolpyruvate carboxykinase (PEPCK-C) in paired mesenteric and omental visceral adipose tissue (VAT) and abdominal and femoral subcutaneous adipose tissue (SAT) in women with either normal weight or upper-body obesity. No differences in the expression of hormone-sensitive lipase (HSL) or AQP7 were found between the two groups in the four depots. The expression of adipocyte triglyceride lipase (ATGL) and HSL were higher in omental VAT and femoral SAT than in mesenteric VAT in both groups of women. Similarly, AQP7 expression was higher in omental VAT than in mesenteric VAT. The expression of PEPCK-C was lower in omental VAT than in femoral SAT. No correlation between the expression of AQP7 and the mean adipocyte size was observed; however, the expression of PEPCK-C positively correlated with the mean adipocyte size. In conclusion, a depot-specific protein expression pattern was found for ATGL, HSL, AQP7, and PEPCK-C. The expression pattern supports that the regulation of AQP7 protein expression is at least in part linked to the lipolytic rate. Furthermore, the results support that the synthesis of glycerol-3-phosphate via glyceroneogenesis contributes to regulating triglyceride accumulation in white adipose tissue in women. Full article
(This article belongs to the Special Issue New Insights into Aquaporins: 2nd Edition)
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Review

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21 pages, 1283 KiB  
Review
The Expanding Role of Aquaporin-1, Aquaporin-3 and Aquaporin-5 as Transceptors: Involvement in Cancer Development and Potential Druggability
by Catarina Pimpão, Inês V. da Silva and Graça Soveral
Int. J. Mol. Sci. 2025, 26(3), 1330; https://doi.org/10.3390/ijms26031330 - 4 Feb 2025
Cited by 2 | Viewed by 2012
Abstract
Aquaporins (AQPs) are transmembrane proteins that facilitate the transport of water and small solutes, including glycerol, hydrogen peroxide and ions, across cell membranes. Beyond their established physiological roles in water regulation and metabolic processes, AQPs also exhibit receptor-like signaling activities in cancer-associated signaling [...] Read more.
Aquaporins (AQPs) are transmembrane proteins that facilitate the transport of water and small solutes, including glycerol, hydrogen peroxide and ions, across cell membranes. Beyond their established physiological roles in water regulation and metabolic processes, AQPs also exhibit receptor-like signaling activities in cancer-associated signaling pathways, integrating the dual roles of transporters and receptors, hence functioning as transceptors. This dual functionality underpins their critical involvement in cancer biology, where AQPs play key roles in promoting cell proliferation, migration, and invasion, contributing significantly to carcinogenesis. Among the AQPs, AQP1, AQP3 and AQP5 have been consistently identified as being aberrantly expressed in various tumor types. Their overexpression is strongly associated with tumor progression, metastasis, and poor patient prognosis. This review explores the pivotal roles of AQP1, AQP3 and AQP5 as transceptors in cancer biology, underscoring their importance as pharmacological targets. It highlights the urgent need for the development of effective modulators to target these AQPs, offering a promising avenue to enhance current therapeutic approaches for cancer treatment. Full article
(This article belongs to the Special Issue New Insights into Aquaporins: 2nd Edition)
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20 pages, 2421 KiB  
Review
Aquaporins in Biliary Function: Pathophysiological Implications and Therapeutic Targeting
by Mohamad Khalil, Patrizia Gena, Agostino Di Ciaula, Piero Portincasa and Giuseppe Calamita
Int. J. Mol. Sci. 2024, 25(22), 12133; https://doi.org/10.3390/ijms252212133 - 12 Nov 2024
Cited by 2 | Viewed by 1430
Abstract
Aquaporins (AQPs) are transmembrane proteins permeable to water and a series of small solutes. AQPs play a key role in pathways of hepatobiliary secretion at the level of the liver, bile ducts, and gallbladder. AQP8 and -9 are pivotal in facilitating the osmotic [...] Read more.
Aquaporins (AQPs) are transmembrane proteins permeable to water and a series of small solutes. AQPs play a key role in pathways of hepatobiliary secretion at the level of the liver, bile ducts, and gallbladder. AQP8 and -9 are pivotal in facilitating the osmotic water movement of hepatic bile, which is composed of 95% water. In the biliary tract, AQP1 and -4 are involved in the rearrangement of bile composition by mechanisms of reabsorption/secretion of water. In the gallbladder, AQP1 and -8 are also involved in trans-epithelial bidirectional water flow with the ultimate goal of bile concentration. Pathophysiologically, AQPs have been indicated as players in several hepatobiliary disorders, including cholestatic diseases and cholesterol cholelithiasis. Research on AQP function and the modulation of AQP expression is in progress, with the identification of potent and homolog-specific compounds modulating the expression or inhibiting these membrane channels with promising pharmacological developments. This review summarizes the contribution of AQPs in physiological and pathophysiological stages related to hepatobiliary function. Full article
(This article belongs to the Special Issue New Insights into Aquaporins: 2nd Edition)
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