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Advances in Aquaporins II
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Advances in Aquaporins II

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

Deadline for manuscript submissions: closed (30 June 2023) | Viewed by 9443

Special Issue Editor

Prof. Dr. Giuseppe Calamita

E-Mail Website
Guest Editor
Department of Biosciences, Biotechnologies and Environment, University of Bari “Aldo Moro”, 70125 Bari, Italy
Interests: cell physiology and pathophysiology; cellular and molecular biology; biophysics of the molecular transport properties of aquaporin membrane channels; aquaporins in health and disease; aquaporins as biomarkers and drug targets
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Aquaporins are a family of transmembrane channel proteins that are widespread throughout nature, where they facilitate the transport of water and small solutes into and out of cells. They are widely studied in prokaryotic and eukaryotic biology, playing different roles. Aquaporins are also implicated in several clinical disorders, and their interest in the field of medicine is strong.

 This Special Issue, in its second edition, with the first having been proven to be a success judging by the high number of contributions received, welcomes original research and review papers addressing every aspect of aquaporins, including their biophysics, function, and regulation in biology and medicine, as well as their translational value in pharmacology, biotechnologies (water purification), and agriculture. Interdisciplinary applications of the knowledge shared will hopefully stimulate future research.

Prof. Dr. Giuseppe Calamita
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 submissions that pass pre-check are 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 semimonthly 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 2700 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

  • membrane water and solute transport
  • fluid homeostasis
  • channel proteins in health and disease
  • biomarkers
  • novel drug targets

Published Papers (7 papers)

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Research

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12 pages, 1894 KiB  
Article
Aquaglyceroporins in Human Breast Cancer
by Teresa Kirkegaard, Andreas Riishede, Trine Tramm and Lene N. Nejsum
Cells 2023, 12(17), 2185; https://doi.org/10.3390/cells12172185 - 31 Aug 2023
Cited by 2 | Viewed by 1132
Abstract
Aquaporins are water channels that facilitate passive water transport across cellular membranes following an osmotic gradient and are essential in the regulation of body water homeostasis. Several aquaporins are overexpressed in breast cancer, and AQP1, AQP3 and AQP5 have been linked to spread [...] Read more.
Aquaporins are water channels that facilitate passive water transport across cellular membranes following an osmotic gradient and are essential in the regulation of body water homeostasis. Several aquaporins are overexpressed in breast cancer, and AQP1, AQP3 and AQP5 have been linked to spread to lymph nodes and poor prognosis. The subgroup aquaglyceroporins also facilitate the transport of glycerol and are thus involved in cellular metabolism. Transcriptomic analysis revealed that the three aquaglyceroporins, AQP3, AQP7 and AQP9, but not AQP10, are overexpressed in human breast cancer. It is, however, unknown if they are all expressed in the same cells or have a heterogeneous expression pattern. To investigate this, we employed immunohistochemical analysis of serial sections from human invasive ductal and lobular breast cancers. We found that AQP3, AQP7 and AQP9 are homogeneously expressed in almost all cells in both premalignant in situ lesions and invasive lesions. Thus, potential intervention strategies targeting cellular metabolism via the aquaglyceroporins should consider all three expressed aquaglyceroporins, namely AQP3, AQP7 and AQP9. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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14 pages, 2387 KiB  
Article
Aquaporin-7-Mediated Glycerol Permeability Is Linked to Human Sperm Motility in Asthenozoospermia and during Sperm Capacitation
by João C. Ribeiro, Raquel L. Bernardino, Ana Gonçalves, Alberto Barros, Giuseppe Calamita, Marco G. Alves and Pedro F. Oliveira
Cells 2023, 12(15), 2003; https://doi.org/10.3390/cells12152003 - 05 Aug 2023
Viewed by 1185
Abstract
Osmoregulation plays a vital role in sperm function, encompassing spermatogenesis, maturation, and fertilization. Aquaglyceroporins, a subclass of aquaporins (AQPs), facilitate the transport of water and glycerol across the sperm membrane, with glycerol serving as an important substrate for sperm bioenergetics. This study aimed [...] Read more.
Osmoregulation plays a vital role in sperm function, encompassing spermatogenesis, maturation, and fertilization. Aquaglyceroporins, a subclass of aquaporins (AQPs), facilitate the transport of water and glycerol across the sperm membrane, with glycerol serving as an important substrate for sperm bioenergetics. This study aimed to elucidate the significance of AQP-mediated glycerol permeability in sperm motility. The presence and localization of AQP3 and AQP7 in human sperm were assessed using immunofluorescence. Subsequently, the glycerol permeability of spermatozoa obtained from normozoospermic individuals (n = 30) was measured, using stopped-flow light scattering, after incubation with specific aquaporin inhibitors targeting AQP3 (DFP00173), AQP7 (Z433927330), or general aquaglyceroporin (phloretin). Sperm from asthenozoospermic men (n = 30) were utilized to evaluate the AQP7-mediated glycerol permeability, and to compare it with that of normozoospermic men. Furthermore, hypermotile capacitated sperm cells were examined, to determine the AQP7 expression and membrane glycerol permeability. AQP3 was predominantly observed in the tail region, while AQP7 was present in the head, midpiece, and tail of human sperm. Our findings indicate that AQP7 plays a key role in glycerol permeability, as the inhibition of AQP7 resulted in a 55% decrease in glycerol diffusion across the sperm membrane. Importantly, this glycerol permeability impairment was evident in spermatozoa from asthenozoospermic individuals, suggesting the dysregulation of AQP7-mediated glycerol transport, despite similar AQP7 levels. Conversely, the AQP7 expression increased in capacitated sperm, compared to non-capacitated sperm. Hence, AQP7-mediated permeability may serve as a valuable indicator of sperm motility, and be crucial in sperm function. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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12 pages, 3375 KiB  
Article
Methylthiosulfonate-Based Cysteine Modifiers as Alternative Inhibitors of Mercurial-Sensitive Aquaporins
by Katrin Jeuken, Emmi Jaeger, Emily Matthews and Eric Beitz
Cells 2023, 12(13), 1742; https://doi.org/10.3390/cells12131742 - 28 Jun 2023
Viewed by 942
Abstract
(1) Background: Several members of the ubiquitous aquaporin family, AQP, of water and neutral solute channels carry a cysteine residue in the selectivity filter region. Traditionally, toxic mercury-containing compounds are used to bind to the cysteine as covalent AQP inhibitors for physiological studies [...] Read more.
(1) Background: Several members of the ubiquitous aquaporin family, AQP, of water and neutral solute channels carry a cysteine residue in the selectivity filter region. Traditionally, toxic mercury-containing compounds are used to bind to the cysteine as covalent AQP inhibitors for physiological studies or analysis of structure–function relationships. (2) Methods: We tested thiol-reactive methylthiosulfonate reagents, MTS, as alternative Cys modifiers for AQP inhibition. Three MTS reagents transferring S-alkyl moieties of increasing size, i.e., S-methyl, S-n-propyl, and S-benzyl, were used with yeast-expressed water-selective AQP1 and the aquaglyceroporin AQP9. Respective Cys-to-Ala variants and mouse erythrocytes that naturally express AQP1 and AQP9 served as controls. (3) Results: Both wildtype AQP isoforms were inhibited by the Cys modifiers in a size-dependent manner, whereas the Cys-to-Ala-variants exhibited resistance. Sub-millimolar concentrations and incubation times in the minute range were sufficient. The modifications were reversible by treatment with the thiol reagents acetylcysteine, ACC, and dithiothreitol, DTT. (4) Conclusions: MTS reagents represent a valid alternative of low toxicity for the inhibition of mercurial-sensitive AQPs. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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9 pages, 2097 KiB  
Communication
Adenoviral Transfer of Human Aquaporin-8 Gene to Mouse Liver Improves Ammonia-Derived Ureagenesis
by Alejo M. Capiglioni, María C. Capitani, Julieta Marrone and Raúl A. Marinelli
Cells 2023, 12(11), 1535; https://doi.org/10.3390/cells12111535 - 02 Jun 2023
Cited by 1 | Viewed by 937
Abstract
We previously reported that, in cultured hepatocytes, mitochondrial aquaporin-8 (AQP8) channels facilitate the conversion of ammonia to urea and that the expression of human AQP8 (hAQP8) enhances ammonia-derived ureagenesis. In this study, we evaluated whether hepatic gene transfer of hAQP8 improves detoxification of [...] Read more.
We previously reported that, in cultured hepatocytes, mitochondrial aquaporin-8 (AQP8) channels facilitate the conversion of ammonia to urea and that the expression of human AQP8 (hAQP8) enhances ammonia-derived ureagenesis. In this study, we evaluated whether hepatic gene transfer of hAQP8 improves detoxification of ammonia to urea in normal mice as well as in mice with impaired hepatocyte ammonia metabolism. A recombinant adenoviral (Ad) vector encoding hAQP8, AdhAQP8, or a control Ad vector was administered via retrograde infusion into the bile duct of the mice. Hepatocyte mitochondrial expression of hAQP8 was confirmed using confocal immunofluorescence and immunoblotting. The normal hAQP8-transduced mice showed decreased plasma ammonia and increased liver urea. Enhanced ureagenesis was confirmed via the NMR studies assessing the synthesis of 15N-labeled urea from 15N-labeled ammonia. In separate experiments, we made use of the model hepatotoxic agent, thioacetamide, to induce defective hepatic metabolism of ammonia in mice. The adenovirus-mediated mitochondrial expression of hAQP8 was able to restore normal ammonemia and ureagenesis in the liver of the mice. Our data suggest that hAQP8 gene transfer to mouse liver improves detoxification of ammonia to urea. This finding could help better understand and treat disorders with defective hepatic ammonia metabolism. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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14 pages, 3793 KiB  
Article
Tamoxifen Affects Aquaporin-3 Expression and Subcellular Localization in Rat and Human Renal Collecting Ducts
by Stine Julie Tingskov, Mariagrazia D’Agostino, Frédéric H. Login, Grazia Tamma, Lene N. Nejsum and Rikke Nørregaard
Cells 2023, 12(8), 1140; https://doi.org/10.3390/cells12081140 - 12 Apr 2023
Cited by 2 | Viewed by 1255
Abstract
Sex hormones play an important role in the regulation of water homeostasis, and we have previously shown that tamoxifen (TAM), a selective estrogen receptor modulator (SERM), affects the regulation of aquaporin (AQP)-2. In this study, we investigated the effect of TAM on the [...] Read more.
Sex hormones play an important role in the regulation of water homeostasis, and we have previously shown that tamoxifen (TAM), a selective estrogen receptor modulator (SERM), affects the regulation of aquaporin (AQP)-2. In this study, we investigated the effect of TAM on the expression and localization of AQP3 in collecting ducts using various animal, tissue, and cell models. The impact of TAM on AQP3 regulation was studied in rats subjected to 7 days of unilateral ureteral obstruction (UUO), with the rats fed a lithium-containing diet to induce nephrogenic diabetes insipidus (NDI), as well as in human precision-cut kidney slices (PCKS). Moreover, intracellular trafficking of AQP3 after TAM treatment was investigated in Madin-Darby Canine Kidney (MDCK) cells stably expressing AQP3. In all models, the expression of AQP3 was evaluated by Western blotting, immunohistochemistry and qPCR. TAM administration attenuated UUO-induced downregulation of AQP3 and affected the localization of AQP3 in both the UUO model and the lithium-induced NDI model. In parallel, TAM also affected the expression profile of other basolateral proteins, including AQP4 and Na/K-ATPase. In addition, TGF-β and TGF-β+TAM treatment affected the localization of AQP3 in stably transfected MDCK cells, and TAM partly attenuated the reduced AQP3 expression in TGF-β exposed human tissue slices. These findings suggest that TAM attenuates the downregulation of AQP3 in a UUO model and a lithium-induced NDI model and affects the intracellular localization in the collecting ducts. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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Review

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31 pages, 3436 KiB  
Review
Insights into the Function of Aquaporins in Gastrointestinal Fluid Absorption and Secretion in Health and Disease
by Giuseppe Calamita and Christine Delporte
Cells 2023, 12(17), 2170; https://doi.org/10.3390/cells12172170 - 29 Aug 2023
Viewed by 1554
Abstract
Aquaporins (AQPs), transmembrane proteins permeable to water, are involved in gastrointestinal secretion. The secretory products of the glands are delivered either to some organ cavities for exocrine glands or to the bloodstream for endocrine glands. The main secretory glands being part of the [...] Read more.
Aquaporins (AQPs), transmembrane proteins permeable to water, are involved in gastrointestinal secretion. The secretory products of the glands are delivered either to some organ cavities for exocrine glands or to the bloodstream for endocrine glands. The main secretory glands being part of the gastrointestinal system are salivary glands, gastric glands, duodenal Brunner’s gland, liver, bile ducts, gallbladder, intestinal goblet cells, exocrine and endocrine pancreas. Due to their expression in gastrointestinal exocrine and endocrine glands, AQPs fulfill important roles in the secretion of various fluids involved in food handling. This review summarizes the contribution of AQPs in physiological and pathophysiological stages related to gastrointestinal secretion. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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12 pages, 1224 KiB  
Review
The Role of Aquaporin 5 (AQP5) in Lung Adenocarcinoma: A Review Article
by Lukasz Jaskiewicz, Anna Romaszko-Wojtowicz, Anna Doboszynska and Agnieszka Skowronska
Cells 2023, 12(3), 468; https://doi.org/10.3390/cells12030468 - 31 Jan 2023
Cited by 3 | Viewed by 1846
Abstract
Aquaporins (AQPs) are selective, transmembrane proteins, which are primarily responsible for the transport of water and small molecules. They have been demonstrated to play a key role in the development and progression of cancer. Lung adenocarcinoma is the most common primary lung cancer [...] Read more.
Aquaporins (AQPs) are selective, transmembrane proteins, which are primarily responsible for the transport of water and small molecules. They have been demonstrated to play a key role in the development and progression of cancer. Lung adenocarcinoma is the most common primary lung cancer diagnosed in patients in Europe and the USA. The research done so far has provided firm evidence that some AQPs can be biomarkers for various diseases. The objective of this review article is to present a potential role of AQP5 in the development of lung adenocarcinoma. Original papers discussing the involvement of AQP5 in carcinogenesis and containing relevant clinical data were identified. In order to analyze the research material in accordance with PRISMA guidelines, a systematic search of the ScienceDirect, Web of Science, and Pubmed databases was conducted. Out of the total number of 199 papers identified, 14 original articles were subject to analysis. This article presents the pathophysiological role of AQP5 in the biology of lung adenocarcinoma as well as its prognostic value. The analysis substantiates the conclusion that the prognostic value of AQP5 in lung cancer requires further research. Another aim of this paper is to disseminate knowledge about AQPs among clinicians. Full article
(This article belongs to the Special Issue Advances in Aquaporins II)
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