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Stomata are micropores on the leaf epidermis that allow carbon dioxide (CO 2 ) uptake for photosynthesis at the expense of water loss through transpiration. Stomata coordinate the plant gas exchange of carbon and water with the atmosphere through their opening and closing dynamics. In the context of global climate change, it is essential to better understand the mechanism of stomatal movements under different environmental stimuli. Aquaporins (AQPs) are considered important regulators of stomatal movements by contributing to membrane diffusion of water, CO 2  and hydrogen peroxide. This review compiles the most recent findings and discusses future directions to update our knowledge of the role of AQPs in stomatal movements. After highlighting the role of subsidiary cells (SCs), which contribute to the high water use efficiency of grass stomata, we explore the expression of AQP genes in guard cells and SCs. We then focus on the cellular regulation of AQP activity at the protein level in stomata. After introducing their post-translational modifications, we detail their trafficking as well as their physical interaction with various partners that regulate AQP subcellular dynamics towards and within specific regions of the cell membranes, such as microdomains and membrane contact sites., (© 2024 John Wiley & Sons Ltd.)

Aquaporins (AQPs) are small, integral proteins facilitating water transport across plasma cell membranes in response to osmotic gradients. This family has 13 unique members (AQP0-12), which can also transport glycerol, urea, gases, and other salute small molecules. AQPs play a crucial role in the regulation of different cellular processes, including metabolism, migration, immunity, barrier function, and angiogenesis. These proteins are found to aberrantly overexpress in various cancers, including colorectal cancer (CRC). Growing evidence has explored AQPs as a potential diagnostic biomarker and therapeutic target in different cancers. However, there is no comprehensive review compiling the available information on the crucial role of AQPs in the context of colorectal cancer. This review highlights the significance of AQPs as the biomarker and regulator of tumor cells metabolism. In addition, the proliferation, angiogenesis, and metastasis of tumor cells related to AQPs expression as well as function are discussed. Understanding the AQPs prominent role in chemotherapy resistance is of great importance clinically., (© 2024. The Author(s) under exclusive licence to Japan Human Cell Society.)

Aquaporins-small, "unusual" proteins, whose discovery revolutionized the view of membrane transport of water and other small molecules, are essential for all living organisms. Aquaporins located in the male reproductive system seem to play a key role in the proper course of many processes occurring within it, thus maintaining a high reproductive potential., (© 2023 American Society of Andrology and European Academy of Andrology.)

The central nervous system is highly dependent on water, and disturbances in water homeostasis can have a significant impact on its normal functions. The regulation of water balance is, at least in part, carried out via specialized water channels called aquaporins. In the central nervous system, two major aquaporins (AQPs), AQP1 and AQP4, and their potential involvements have been long implicated in the pathophysiology of many brain disorders such as brain edema and Neuromyelitis optica. In addition to these diseases, there is growing attention to the involvement of AQPs in the removal of waste products in Alzheimer's disease (AD). This indicates that targeting fluid homeostasis is a novel and attractive approach for AD. This review article aims to summarize recent knowledge on the pathological implications of AQPs in AD, discussing unsolved questions and future prospects.

AQP0-12, a total of 13 aquaporins are expressed in the mammalian reproductive system. These aquaporins mediate the transport of water and small solutes across biofilms for maintaining reproductive tract water balance and germ cell water homeostasis. These aquaporins play important roles in the regulation of sperm and egg cell production, maturation, and fertilization processes. Impaired AQP function may lead to diminished male and female fertility. This review focuses on the distribution, function, and regulation of AQPs throughout the male and female reproductive organs and tracts. Their correlation with reproductive success, revealing recent advances in the physiological and pathophysiological roles of aquaporins in the reproductive system., (© 2023. The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.)

Exocrine and endocrine glands deliver their secretory product, respectively, at the surface of the target organs or within the bloodstream. The release of their products has been shown to rely on secretory mechanisms often involving aquaporins (AQPs). This chapter will provide insight into the role of AQPs in secretory glands located within the gastrointestinal tract, including salivary glands, gastric glands, duodenal Brunner's glands, liver, gallbladder, intestinal goblets cells, and pancreas, as well and in other parts of the body, including airway submucosal glands, lacrimal glands, mammary glands, and eccrine sweat glands. The involvement of AQPs in both physiological and pathophysiological conditions will also be highlighted., (© 2023. The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.)

Despite aquaporin water channels (AQPs) play a critical role in maintaining water homeostasis in female reproductive tract and prompt a gradual increase in water content in cervical edema as pregnancy progressed, their relationship with macrophage infiltration and collagen content in human cervical remodeling need to be further investigated. This is the first study to examine the expression and localization of AQP3, AQP4, AQP5, AQP8, and macrophages simultaneously in human cervical ripening. The immunoreactivity of these AQPs was 2.6 to 6-fold higher on gestational weeks 26 (GD26W) than that on GD6W and GD15W, but AQP4 expression on GD39W dropped a similar extent on GD15W, other AQPs continued to rise on GD39W. The AQP3, AQP4, and AQP5 intensity seemed more abundant in cervical stroma than in the perivascular area on GD26W; the distribution of AQP3, AQP5, and AQP8 in cervical stroma was equivalent to that in the perivascular area on GD39W. Macrophage numbers were 1.7-fold higher in subepithelium region and 3.0-fold higher in center area on GD26W than that on GD15W; such numbers remained elevated on GD39W. The electron micrographs showed that cervical extensibility increased significantly on GD26W and GD39W accompanied with increased macrophage infiltration, cervical water content, and much more space among collagen fibers. These findings suggest that the upregulation of AQPs expression in human cervix is closely related to enhanced macrophage infiltration during pregnancy; there may be a positive feedback mechanism between them to lead the increase of water content and the degradation of collagen., (© The Author(s) 2021. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.)

The canonical function of aquaporin (AQP) water channels is to facilitate passive transport of water across cellular membranes making them essential in the regulation of body water homeostasis. Moreover, AQPs, including AQP1, have been found to be overexpressed in multiple cancer types, including breast cancer, where AQP1 overexpression is associated with poor prognosis. AQPs have been shown to affect cellular processes associated with cancer progression and spread including cell migration, angiogenesis, and proliferation. Moreover, AQPs can regulate levels of adhesion proteins at cell-cell junctions, a regulatory role, which is still largely unexplored in cancer. Understanding the molecular mechanisms of how AQP1 contributes to breast cancer progression and metastatic processes is essential to establish AQP1 as a biomarker and to develop targeted anticancer treatments for breast cancer patients. This mini-review focuses on the role of AQP1 in breast cancer., (© 2021 Scandinavian Societies for Medical Microbiology and Pathology.)

Aquaporins are water channel proteins facilitating passive transport of water across cellular membranes. Aquaporins are over- or ectopically expressed in a multitude of cancers, including pancreatic ductal adenocarcinoma, which is a highly aggressive cancer with low survival rate. Evidence suggests that aquaporins can affect multiple cellular processes involved in cancer development and progression including epithelial-mesenchymal transition, cellular migration, cell proliferation, invasion, and cellular adhesions. In pancreatic ductal adenocarcinoma, aquaporin-1, aquaporin-3, and aquaporin-5 are overexpressed and have been associated with metastatic processes and poor survival. Thus, aquaporin expression has been suggested as diagnostic markers and therapeutic targets in pancreatic ductal adenocarcinoma., (© 2021 Scandinavian Societies for Medical Microbiology and Pathology.)

Water conservation is one of the most challenging processes for terrestrial vertebrates and is necessary for their survival. Birds are the only vertebrate animals other than mammals that have the ability to concentrate their urine. Previously, we identified and characterized aquaporins (AQP)1-4 responsible for urine concentration in Japanese quail kidneys. Today, a total of 13 orthologs for these genes have been reported in birds. Bird AQPs can be classified into four subfamilies: 1) Classical AQPs (AQP0-5 and novel member, AQP4-like) that conserve the selectivity filter; 2) aquaglyceroporins (AQP3, 7, 9 and 10) that retain an aspartic acid residue in the second NPA box and expand the pore to accept larger molecules; 3) unorthodox AQPs (AQP11-12) which structurally resemble their mammalian counterparts; 4) AQP8-type, a subfamily that differs from mammalian AQP8. Interestingly, over the course of time, birds lost their mammalian counterpart AQP6 but obtained a novel AQP4-like aquaporin member. In quail and/or chicken kidneys, at least six AQPs are expressed. Quail AQP1 (qAQP1) is expressed in both cortical and medullary proximal tubules but is absent in the descending limb (DL) and the thick ascending limb (TAL), supporting our previous finding that the DL and TAL are water impermeable. AQP2, an arginine vasotocin (AVT)-sensitive water channel, is exclusively expressed in the principal cells of the collecting duct (CD). AQP4 is unlikely to participate in free water resorption from the collecting duct (CD), and only AQP3 may represent an exit pathway for water reabsorbed apically via AQP2. While AQP9 is not expressed in mammalian kidneys, AQP9 was recently found in chicken kidneys. This review summarizes the current knowledge of the structure, function and expression of bird AQPs., (Copyright © 2021 Elsevier B.V. All rights reserved.)

Aquaporins (AQPs) are proteins that selectively transport water across the cell membrane. Although AQPs play important roles in secretion in the lacrimal gland, the expression and localization of AQPs have not been clarified yet. In the current study, we investigated the expression pattern of AQP family members in the murine lacrimal gland during development. Lacrimal gland tissues were harvested from E13.5 and E17.5 murine embryos and from mice 8 weeks of age (adults). Corneal and conjunctival tissues from the latter served as controls. Total RNA was isolated and analyzed for the expression of AQP family members using qPCR. The localization of AQPs in the adult lacrimal gland in adult murine lacrimal glands was also analyzed. Expression of Aqp 8 and Aqp 9 mRNAs was detected in the adult lacrimal gland but not in the cornea, conjunctiva, or fetal lacrimal gland. AQP8 and AQP9 and α -SMA partially colocalized around the basal regions of the acinar unit. The levels of Aqp 3 mRNAs and protein were much lower in the adult lacrimal gland but were readily detected in the adult cornea and conjunctiva. Our study suggests that AQP8 and AQP9 may serve as markers for adult murine lacrimal gland, ductal, and myoepithelial cells., Competing Interests: The authors declare that they have no conflict of interests or other interests that might be perceived to influence the results and/or discussion reported in this article., (Copyright © 2021 Naoko Okada et al.)

Aquaporins (AQPs) are transmembrane water channels and some of them are permeable in addition to water to other small solutes including hydrogen peroxide. The sperm cells of mammals and fishes express different AQPs, although there is no agreement in the literature on their localization. In humans, AQP3 and AQP11 are expressed mainly in the tail, AQP7 in the head and AQP8 in the midpiece. Thanks to the results of experiments with KO mice and to data obtained by comparing sub-fertile patients with normospermic subjects, the importance of AQPs for the normal functioning of sperms to ensure normal fertility emerged. AQP3, AQP7 and AQP11 appeared involved in the sperm volume regulation, a key role for fertility because osmoadaptation protect the sperm against a swelling and tail bending that could affect sperm motility. AQP8 seems to have a fundamental role in regulating the elimination of hydrogen peroxide, the most abundant reactive oxygen species (ROS), and therefore in the response to oxidative stress. In this review, the human AQPs expression, their localization and functions, as well as their relevance in normal fertility are discussed. To understand better the AQPs role in human sperm functionality, the results of studies obtained in other animal species were also considered., Competing Interests: Declaration competing interest None., (Copyright © 2021 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)

Skin is the most vulnerable organ of the human body since it is the first line of defense, covering the entire external body surface. Additionally, skin has a critical role in thermoregulation, sensation, immunological surveillance, and biochemical processes such as Vitamin D 3 production by ultraviolet irradiation. The ability of the skin layers and resident cells to maintain skin physiology, such as hydration, regulation of keratinocytes proliferation and differentiation and wound healing, is supported by key proteins such as aquaporins (AQPs) that facilitate the movements of water and small neutral solutes across membranes. Various AQP isoforms have been detected in different skin-resident cells where they perform specific roles, and their dysregulation has been associated with several skin pathologies. This review summarizes the current knowledge of AQPs involvement in skin physiology and pathology, highlighting their potential as druggable targets for the treatment of skin disorders., Competing Interests: Declaration of competing interest The authors declare no conflict of interest., (Copyright © 2021 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)

Aquaporins (AQPs) are water channel proteins facilitating passive transport of water and other small molecules across biomembranes. Regulation of osmotic homeostasis via AQPs is accompanied by dynamic participation of various cellular signaling pathways. Recently emerging evidence reveals that functional roles of AQPs are further extended from the osmotic regulation via water permeation into the cell proliferation and differentiation. In particular, anomalous expression of AQPs has been demonstrated in various types of cancer cells and cancer stem-like cells and it has been proposed as markers for proliferation and progression of cancer cells. Thus, a more comprehensive view on AQPs could bring a great interest in the cell stemness accompanied by the expression of AQPs. AQPs are broadly expressed across tissues and cells in a cell type- and lineage-specific manner during development via spatiotemporal transcriptional regulation. Moreover, AQPs are expressed in various adult stem cells and cells associated with a stem cell niche as well as cancer stem-like cells. However, the expression and regulatory mechanisms of AQP expression in stem cells have not been well understood. This review highlighted the AQPs expression in stem cell niches/stem cells and the involvement of AQPs in the cell proliferation and signaling pathways associated with cell stemness., Competing Interests: Declaration of competing interest The authors have no conflict of interest to declare., (Copyright © 2021 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)

High-scored premium wines are typically produced under moderate drought stress, suggesting that the water status of grapevine is crucial for wine quality. Aquaporins greatly influence the plant water status by facilitating water diffusion across the plasma membrane in a tightly regulated manner. They adjust the hydraulic conductance of the plasma membrane rapidly and reversibly, which is essential in specific physiological events, including adaptation to soil water scarcity. The comprehension of the sophisticated plant-water relations at the molecular level are thus important to optimize agricultural practices or to assist plant breeding programs. This review explores the recent progresses in understanding the water transport in grapevine at the cellular level through aquaporins and its regulation. Important aspects, including aquaporin structure, diversity, cellular localization, transport properties, and regulation at the cellular and whole plant level are addressed. An ecophysiological perspective about the roles of grapevine aquaporins in plant response to drought stress is also provided., (Copyright © 2021 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)

Background: Canavalia rosea (Sw.) DC. (bay bean) is an extremophile halophyte that is widely distributed in coastal areas of the tropics and subtropics. Seawater and drought tolerance in this species may be facilitated by aquaporins (AQPs), channel proteins that transport water and small molecules across cell membranes and thereby maintain cellular water homeostasis in the face of abiotic stress. In C. rosea, AQP diversity, protein features, and their biological functions are still largely unknown., Results: We describe the action of AQPs in C. rosea using evolutionary analyses coupled with promoter and expression analyses. A total of 37 AQPs were identified in the C. rosea genome and classified into five subgroups: 11 plasma membrane intrinsic proteins, 10 tonoplast intrinsic proteins, 11 Nod26-like intrinsic proteins, 4 small and basic intrinsic proteins, and 1 X-intrinsic protein. Analysis of RNA-Seq data and targeted qPCR revealed organ-specific expression of aquaporin genes and the involvement of some AQP members in adaptation of C. rosea to extreme coral reef environments. We also analyzed C. rosea sequences for phylogeny reconstruction, protein modeling, cellular localizations, and promoter analysis. Furthermore, one of PIP1 gene, CrPIP1;5, was identified as functional using a yeast expression system and transgenic overexpression in Arabidopsis., Conclusions: Our results indicate that AQPs play an important role in C. rosea responses to saline-alkaline soils and drought stress. These findings not only increase our understanding of the role AQPs play in mediating C. rosea adaptation to extreme environments, but also improve our knowledge of plant aquaporin evolution more generally., (© 2021. The Author(s).)

Background: Root hydraulic conductance is primarily determined by the conductance of living tissues to radial water flow. Plasma membrane intrinsic proteins (PIPs) in root cortical cells are important for plants to take up water and are believed to be directly involved in cell growth., Results: In this study, we found that constitutive overexpression of the poplar root-specific gene PtoPIP1;1 in Arabidopsis accelerated bolting and flowering. At the early stage of the developmental process, PtoPIP1;1 OE Arabidopsis exhibited faster cell growth in both leaves and roots. The turgor pressure of plants was correspondingly increased in PtoPIP1;1 OE Arabidopsis, and the water status was changed. At the same time, the expression levels of flowering-related genes (CRY1, CRY2 and FCA) and hub genes in the regulatory networks underlying floral timing (FT and SOC1) were significantly upregulated in OE plants, while the floral repressor FLC gene was significantly downregulated., Conclusions: Taken together, the results of our study indicate that constitutive overexpression of PtoPIP1;1 in Arabidopsis accelerates bolting and flowering through faster cell growth in both the leaf and root at an early stage of the developmental process. The autonomous pathway of flowering regulation may be executed by monitoring developmental age. The increase in turgor and changes in water status with PtoPIP1;1 overexpression play a role in promoting cell growth.

In most fish exhibiting external fertilization, spermatozoa become motile after release into water, triggered by differences between intracellular and extracellular conditions such as osmotic pressure, ion composition, and pH. The rapid change in osmolarity initiating spermatozoon motility induces osmotic pressure, resulting in active water movement across the cell membrane. Mechanisms of ion and water transport across the plasma membrane and cell volume regulation are important in maintaining structure and functional integrity of the cell. The capacity of the fish spermatozoon plasma membrane to adapt to dramatic environmental changes is an essential prerequisite for motility and successful fertilization. Adaptation to change in external osmolality may be the basis of spermatozoon function and an indicator of sperm quality. The involvement of specific water channels (aquaporins) in cell volume regulation and motility is highly likely. The goal of this review is to describe basic mechanisms of water transport and their role in fish spermatozoon physiology, focusing on osmoresistance, cell volume regulation, motility, and survival.

Soil salinity reduces root hydraulic conductivity (L pr ) of several plant species. However, how cellular signaling and root hydraulic properties are linked in plants that can cope with water restriction remains unclear. In this work, we exposed the halotolerant species red beet (Beta vulgaris) to increasing concentrations of NaCl to determine the components that might be critical to sustaining the capacity to adjust root hydraulics. Our strategy was to use both hydraulic and cellular approaches in hydroponically grown seedlings during the first osmotic phase of salt stress. Interestingly, L pr presented a bimodal profile response apart from the magnitude of the imposed salt stress. As well as L pr , the PIP2-aquaporin profile follows an unphosphorylated/phosphorylated pattern when increasing NaCl concentration while PIP1 aquaporins remain constant. L pr also shows high sensitivity to cycloheximide. In low NaCl concentrations, L pr was high and 70 % of its capacity could be attributed to the CHX-inhibited cell-to-cell pathway. More interestingly, roots can maintain a constant spontaneous exudated flow that is independent of the applied NaCl concentration. In conclusion, Beta vulgaris root hydraulic adjustment completely lies in a dominant cell-to-cell pathway that contributes to satisfying plant water demands., (Copyright © 2021 Elsevier B.V. All rights reserved.)

Plant plasma membrane-type plasma membrane intrinsic protein (PIP) aquaporins are classified into two groups, PIP1s and PIP2s. In this study, we focused on HvPIP1;2, a PIP1 in barley (Hordeum vulgare), to dissect the molecular mechanisms that evoke HvPIP1-mediated water transport. No HvPIP1;2 protein was localized to the plasma membrane when expressed alone in Xenopus laevis oocytes. By contrast, a chimeric HvPIP1;2 protein (HvPIP1;2_24NC), in which the N- and C-terminal regions were replaced with the corresponding regions from HvPIP2;4, was found to localize to the plasma membrane of oocytes. However, HvPIP1;2_24NC showed no water transport activity in swelling assays. These results suggested that the terminal regions of PIP2 proteins direct PIP proteins to the plasma membrane, but the relocalization of PIP1 proteins was not sufficient to PIP1s functionality as a water channel in a membrane. A single amino acid replacement of threonine by methionine in HvPIP2;4 (HvPIP2;4T229M) abolished water transport activity. Co-expression of HvPIP1;2_24NC either with HvPIP2;4_12NC or with HvPIP2;4TM_12NC, in which the N- and C-terminal regions were replaced with the corresponding regions of HvPIP1;2, increased the water transport activity in oocytes. These data provided evidence that the HvPIP1;2 molecule has own water transport activity and an interaction with the middle part of the HvPIP2;4 protein (except for the N- and C-termini) is required for HvPIP1;2 functionality as a water channel. This molecular mechanism could be applied to other PIP1s and PIP2s in addition to the known mechanism that the terminal regions of some PIP2s lead some PIP1s to the plasma membrane., (� The Author(s) 2020. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oup.com.)

Purpose: In the eye lens, cytosolic protein concentrations increase progressively from the periphery to the center, contributing to the gradient of refractive index (GRIN). Aquaporins are membrane proteins of lens fiber cells that regulate water transport and adhesion and interact with cytoskeletal proteins. This study investigates how these membrane proteins contribute to proper development of the lens GRIN., Methods: Loss-of-function deletions of aqp0a and/or aqp0b in zebrafish were generated using CRISPR/Cas9 gene editing. Lenses of single aqp0a-/- mutants, single aqp0b-/- mutants, and double aqp0a-/-/aqp0b-/- mutants from larval to elderly adult stages were measured using x-ray Talbot interferometry at SPring8 in Japan. The three-dimensional GRIN profiles in two orthogonal cross-sectional planes of each lens were analyzed and compared with in vivo images and previous results obtained from wild-type lenses., Results: Single aqp0a-/- mutants tended to show asymmetric GRIN profiles, with the central plateau regions shifted anteriorly. Single aqp0b-/- mutants had smooth, symmetric GRIN profiles throughout development until spoke opacities appeared in several extremely old samples. Double aqp0a-/-/aqp0b-/- mutants showed lower magnitude GRIN profiles, as well as dips in the central plateau region., Conclusions: These findings suggest that Aqp0a and Aqp0b have region-specific functions in the lens: Aqp0a is active peripherally, regulating centralization of the plateau region, and this function cannot be compensated for by Aqp0b. In the lens center, either Aqp0a or Aqp0b is required for formation of the plateau region, as well as for the GRIN to reach its maximum magnitude in mature lenses.

The major intrinsic protein (MIP) superfamily is a key part of the fungal transmembrane transport network. It facilitates the transport of water and low molecular weight solutes across biomembranes. The fungal uncharacterized X-Intrinsic Protein (XIP) subfamily includes the full protein diversity of MIP. Their biological functions still remain fully hypothetical. The aim of this study is still to deepen the diversity and the structure of the XIP subfamily in light of the MIP counterparts-the aquaporins (AQPs) and aquaglyceroporins (AQGPs)-and to describe for the first time their function in the development, biomass accumulation, and mycoparasitic aptitudes of the fungal bioagent Trichoderma atroviride . The fungus-XIP clade, with one member ( Triat XIP), is one of the three clades of MIPs that make up the diversity of T. atroviride MIPs, along with the AQPs (three members) and the AQGPs (three members). Triat XIP resembles those of strict aquaporins, predicting water diffusion and possibly other small polar solutes due to particularly wider ar/R constriction with a Lysine substitution at the LE2 position. The XIP loss of function in ∆ Triat XIP mutants slightly delays biomass accumulation but does not impact mycoparasitic activities. ∆ Triat MIP forms colonies similar to wild type; however, the hyphae are slightly thinner and colonies produce rare chlamydospores in PDA and specific media, most of which are relatively small and exhibit abnormal morphologies. To better understand the molecular causes of these deviant phenotypes, a wide-metabolic survey of the ∆ Triat XIPs demonstrates that the delayed growth kinetic, correlated to a decrease in respiration rate, is caused by perturbations in the pentose phosphate pathway. Furthermore, the null expression of the XIP gene strongly impacts the expression of four expressed MIP -encoding genes of T. atroviride , a plausible compensating effect which safeguards the physiological integrity and life cycle of the fungus. This paper offers an overview of the fungal XIP family in the biocontrol agent T. atroviride which will be useful for further functional analysis of this particular MIP subfamily in vegetative growth and the environmental stress response in fungi. Ultimately, these findings have implications for the ecophysiology of Trichoderma spp. in natural, agronomic, and industrial systems.

Research Question: Fat accumulation is present in most post-menopausal women, but the underlying mechanism remains unclear. Aquaporin 7 (AQP7) is the most important glycerol channel facilitating glycerol efflux in adipocytes. High circulating FSH in post-menopausal women may play an independent role in regulation of the lipogenic effect of AQP7 in adipocytes. This study explored the role of AQP7 in the pathophysiology of post-menopausal lipogenesis mediated by high concentrations of circulating FSH., Design: Primary adipocytes from post-menopausal and childbearing women were analysed. An in-vivo post-menopausal animal model was established. AQP7 expression, lipid accumulation and glycerol concentration in adipocytes were measured. Luciferase reporter assay and chromatin immunoprecipitation were performed to identify transcriptional crosstalk in AQP7 promoter., Results: It was found that FSH down-regulated AQP7 expression and glycerol efflux function in mature adipocytes of post-menopausal women and ovariectomized (OVX) mice. In vitro, FSH inhibited lipid accumulation in primary cultured mature adipocytes in a dose-dependent manner and the mechanism was down-regulating AQP7 expression via a FSH receptor pathway. The effect of FSH on AQP7 in adipocytes was through activation of cAMP response element-binding (CREB) protein, which could bind to activator protein-1 (AP-1) sites in the AQP7 promoter, and therefore inhibited the transcriptional activation elicited by c-Jun., Conclusions: Down-regulation of AQP7 by FSH mediated post-menopausal lipogenesis, and the role of FSH was based on binding competition for AP-1 sites between CREB and c-Jun., (Copyright © 2020 Reproductive Healthcare Ltd. Published by Elsevier Ltd. All rights reserved.)

Aquaporins (AQPs) aka water channels are a family of conserved transmembrane proteins (~30 kDa monomers) expressed in various organ systems. Of the 13 AQPs (AQP0 through AQP12) in the human body, four (AQPs 1, 3, 4, and 5) are expressed in the respiratory system. These channels are conventionally known for mediating transcellular fluid movements. Certain AQPs (aquaglyceroporins) have the capability to transport glycerol and potentially other solutes. There is an emerging body of literature unveiling the non-conventional roles of AQPs such as in cell proliferation and migration, gas permeation, signal potentiation, etc. Initial gene knock-out studies established a physiological role for lung AQPs, particularly AQP5, in maintaining homeostasis, by mediating fluid secretion from submucosal glands onto the airway surface liquid (ASL) lining. Subsequent studies have highlighted the functional significance of AQPs, particularly AQP1 and AQP5 in lung pathophysiology and diseases, including but not limited to chronic and acute lung injury, chronic obstructive pulmonary disease (COPD), other inflammatory lung conditions, and lung cancer. AQP1 has been suggested as a potential prognostic marker for malignant mesothelioma. Recent efforts are directed toward exploiting AQPs as targets for diagnosis, prevention, intervention, and/or treatment of various lung conditions. Emerging information on regulatory pathways and directed mechanistic research are posited to unravel novel strategies for these clinical implications. Future considerations should focus on development of AQP inhibitors, blockers, and modulators for therapeutic needs, and better understanding the role of lung-specific AQPs in inter-individual susceptibility to chronic lung diseases such as COPD and cancer., (Copyright © 2020 Elsevier Ltd. All rights reserved.)

Background and Aim: Intratumor hypoxia is a hallmark of hepatocellular carcinoma (HCC) and is associated with an aggressive tumor phenotype. Although it has been shown that AQP9 plays an important role in HCC, the relevance between hypoxia and AQP9 is still unknown., Methods: We established in vitro normoxic or hypoxic models to investigate the role of AQP9 in the regulation of hypoxia-inducible factor 1α (HIF-1α) and hypoxia-enhanced invasion of hepatoma cells. Molecular expression was detected using western blot or quantitative polymerase chain reaction. Cell invasion ability was determined using Transwell invasion assay. In vivo xenograft experiment was used to detect the role of AQP9 on tumor growth., Results: Our present study revealed a decrease in the expression levels of AQP9 in hypoxic microenvironments. Overexpression of AQP9 led to a decreased expression of HIF-1α; conversely, suppression of AQP9 in HCC cells had an opposite effect. Furthermore, up-regulated AQP9 blocked the hypoxic-enhanced invasion of HCC cells. The overexpression of AQP9 inhibited the growth of tumors and HIF-1α expression in vivo., Conclusions: These data suggest that AQP9 acts as a tumor suppressor in HCC invasion via the regulation of HIF-1α expression in the tumor hypoxic microenvironment., (© 2020 Journal of Gastroenterology and Hepatology Foundation and John Wiley & Sons Australia, Ltd.)

Detergent-resistant membranes (DRMs) microdomains, or "raft lipids", are key components of the plasma membrane (PM), being involved in membrane trafficking, signal transduction, cell wall metabolism or endocytosis. Proteins imbibed in these domains play important roles in these cellular functions, but there are few studies concerning DRMs under abiotic stress. In this work, we determine DRMs from the PM of broccoli roots, the lipid and protein content, the vesicles structure, their water osmotic permeability and a proteomic characterization focused mainly in aquaporin isoforms under salinity (80 mM NaCl). Based on biochemical lipid composition, higher fatty acid saturation and enriched sterol content under stress resulted in membranes, which decreased osmotic water permeability with regard to other PM vesicles, but this permeability was maintained under control and saline conditions; this maintenance may be related to a lower amount of total PIP1 and PIP2. Selective aquaporin isoforms related to the stress response such as PIP1;2 and PIP2;7 were found in DRMs and this protein partitioning may act as a mechanism to regulate aquaporins involved in the response to salt stress. Other proteins related to protein synthesis, metabolism and energy were identified in DRMs independently of the treatment, indicating their preference to organize in DMRs.

The phosphorylation state of two serine residues within the C-terminal domain of AtPIP2;1 (S280, S283) regulates its plasma membrane localization in response to salt and osmotic stress. Here, we investigated whether the phosphorylation state of S280 and S283 also influence AtPIP2;1 facilitated water and cation transport. A series of single and double S280 and S283 phosphomimic and phosphonull AtPIP2;1 mutants were tested in heterologous systems. In Xenopus laevis oocytes, phosphomimic mutants AtPIP2;1 S280D, S283D, and S280D/S283D had significantly greater ion conductance for Na + and K + , whereas the S280A single phosphonull mutant had greater water permeability. We observed a phosphorylation-dependent inverse relationship between AtPIP2;1 water and ion transport with a 10-fold change in both. The results revealed that phosphorylation of S280 and S283 influences the preferential facilitation of ion or water transport by AtPIP2;1. The results also hint that other regulatory sites play roles that are yet to be elucidated. Expression of the AtPIP2;1 phosphorylation mutants in Saccharomyces cerevisiae confirmed that phosphorylation influences plasma membrane localization, and revealed higher Na + accumulation for S280A and S283D mutants. Collectively, the results show that phosphorylation in the C-terminal domain of AtPIP2;1 influences its subcellular localization and cation transport capacity., (© 2020 John Wiley & Sons Ltd.)

Water deficit limits plant growth and development by interfering with several physiological and molecular processes both in root and shoot tissues. Through their ability to scavenge nitric oxide (NO), phytoglobins (Pgbs) exercise a protective role during several conditions of stress. While their action has been mainly documented in roots, it is unclear whether Pgb exercises a specific and direct role in shoot tissue. We used a Zea mays root-less system to assess how over-expression or down-regulation of ZmPgb1.1 influences the behavior of shoots exposed to polyethylene glycol (PEG)-simulated water deficit. Relative to their WT and ZmPgb1.1 down-regulating counterparts, PEG-treated shoots over-expressing ZmPgb1.1 exhibited a reduced accumulation of ROS and lipid peroxidation. These effects were ascribed to lower transcript levels of Respiratory Burst Oxidase Homolog (RBOH) genes encoding the ROS generating enzyme complex NADPH oxidase, and a more active antioxidant system. Furthermore, over-expression of ZmPgb1.1 attenuated the reduction in osmotic potential and relative water content experienced during water stress, an observation also demonstrated at a whole plant level, possibly through the retention of the expression of three aquaporins involved in water transfer and implicated in drought tolerance. Pharmacological treatments modulating NO and ethylene levels revealed that the ZmPgb1.1 action was mediated by ethylene synthesis and response, with NO acting as an upstream intermediate. Collectively we provide substantial evidence that ZmPgb1.1 exercises a direct role in shoot tissue, independent from that previously reported in roots, which confers tolerance to water stress., (Copyright © 2020 Elsevier Masson SAS. All rights reserved.)

Aquaporins (AQPs) are a class of integral membrane proteins that facilitate the membrane diffusion of water and other small solutes. Nicotiana tabacum is an important model plant, and its allotetraploid genome has recently been released, providing us with the opportunity to analyze the AQP gene family and its evolution. A total of 88 full-length AQP genes were identified in the N. tabacum genome, and the encoding proteins were assigned into five subfamilies: 34 plasma membrane intrinsic proteins (PIPs); 27 tonoplast intrinsic proteins (TIPs); 20 nodulin26-like intrinsic proteins (NIPs); 3 small basic intrinsic proteins (SIPs); 4 uncharacterized X intrinsic proteins (XIPs), including two splice variants. We also analyzed the genomes of two N. tabacum ancestors, Nicotiana tomentosiformis and Nicotiana sylvestris, and identified 49 AQP genes in each species. Functional prediction, based on the substrate specificity-determining positions (SDPs), revealed significant differences in substrate specificity among the AQP subfamilies. Analysis of the organ-specific AQP expression levels in the N. tabacum plant and RNA-seq data of N. tabacum bright yellow-2 suspension cells indicated that many AQPs are simultaneously expressed, but differentially, according to the organs or the cells. Altogether, these data constitute an important resource for future investigations of the molecular, evolutionary, and physiological functions of AQPs in N. tabacum .

The main role of salivary glands (SG) is the production and secretion of saliva, in which aquaporins (AQPs) play a key role by ensuring water flow. The AQPs are transmembrane channel proteins permeable to water to allow water transport across cell membranes according to osmotic gradient. This review gives an insight into SG AQPs. Indeed, it gives a summary of the expression and localization of AQPs in adult human, rat and mouse SG, as well as of their physiological role in SG function. Furthermore, the review provides a comprehensive view of the involvement of AQPs in pathological conditions affecting SG, including Sjögren's syndrome, diabetes, agedness, head and neck cancer radiotherapy and SG cancer. These conditions are characterized by salivary hypofunction resulting in xerostomia. A specific focus is given on current and future therapeutic strategies aiming at AQPs to treat xerostomia. A deeper understanding of the AQPs involvement in molecular mechanisms of saliva secretion and diseases offered new avenues for therapeutic approaches, including drugs, gene therapy and tissue engineering. As such, AQP5 represents a potential therapeutic target in different strategies for the treatment of xerostomia.

The inner ear is responsible for hearing and balance and consists of a membranous labyrinth within a bony labyrinth. The balance structure is divided into the otolith organ that recognizes linear acceleration and the semicircular canal that is responsible for rotational movement. The cochlea is the hearing organ. The external and middle ear are covered with skin and mucosa, respectively, and the space is filled with air, whereas the inner ear is composed of endolymph and perilymph. The inner ear is a fluid-filled sensory organ composed of hair cells with cilia on the upper part of the cells that convert changes in sound energy and balance into electric energy through the hair cells to transmit signals to the auditory nerve through synapses. Aquaporins (AQPs) are a family of transmembrane proteins present in all species that can be roughly divided into three subfamilies according to structure and function: 1) classical AQP, 2) aquaglyceroporin, and 3) superaquaporin. Currently, the subfamily of mammalian species is known to include 13 AQP members (AQP0-AQP12). AQPs have a variety of functions depending on their structure and are related to inner ear diseases such as Meniere's disease, sensorineural hearing loss, and presbycusis. Additional studies on the relationship between the inner ear and AQPs may be helpful in the diagnosis and treatment of inner ear disease. Laryngoscope, 130:1532-1539, 2020., (© 2019 The American Laryngological, Rhinological and Otological Society, Inc.)

Background: As the glomerular filtrate passes through the nephron and into the renal medulla, electrolytes, water, and urea are reabsorbed through the concerted actions of solute carrier channels and aquaporins at various positions along the nephron and in the outer and inner medulla. Proliferating stem cells expressing the nuclear transcription factor Pax2 give rise to renal epithelial cells. Pax2 expression ends once the epithelial cells differentiate into mature proximal and distal tubules, whereas expression of the related Pax8 protein continues. The collecting tubules and renal medulla are derived from Pax2-positive ureteric bud epithelia that continue to express Pax2 and Pax8 in adult kidneys. Despite the crucial role of Pax2 in renal development, functions for Pax2 or Pax8 in adult renal epithelia have not been established., Methods: To examine the roles of Pax2 and Pax8 in the adult mouse kidney, we deleted either Pax2 , Pax8 , or both genes in adult mice and examined the resulting phenotypes and changes in gene expression patterns. We also explored the mechanism of Pax8-mediated activation of potential target genes in inner medullary collecting duct cells., Results: Mice with induced deletions of both Pax2 and Pax8 exhibit severe polyuria that can be attributed to significant changes in the expression of solute carriers, such as the urea transporters encoded by Slc14a2 , as well as aquaporins within the inner and outer medulla. Furthermore, Pax8 expression is induced by high-salt levels in collecting duct cells and activates the Slc14a2 gene by recruiting a histone methyltransferase complex to the promoter., Conclusions: These data reveal novel functions for Pax proteins in adult renal epithelia that are essential for retaining water and concentrating urine., (Copyright © 2020 by the American Society of Nephrology.)

The study investigated the effect of normal and supraphysiological (resulting from gonadotropin-dependent ovarian stimulation) levels of estradiol (E2) and progesterone (P4) on mouse uterine aquaporin gene/protein (Aqp/AQP) expression on Day 1 (D1) and D4 of pregnancy. The study also examined the effect of ovarian stimulation on uterine luminal closure and uterine receptivity on D4 of pregnancy and embryo implantation on D5 and D7 of pregnancy. These analyses revealed that the expression of Aqp3, Aqp4, Aqp5 and Aqp8 is induced by E2 while the expression of Aqp1 and Aqp11 is induced by P4. Additionally, P4 inhibits E2 induction of Aqp3 and Aqp4 expression while E2 inhibits Aqp1 and Aqp11 expression. Aqp9, however, is constitutively expressed. Ovarian stimulation disrupts Aqp3, Aqp5 and Aqp8 expression on D4 and AQP1, AQP3 and AQP5 spatial expression on both D1 and D4, strikingly so in the myometrium. Interestingly, while ovarian stimulation has no overt effect on luminal closure and uterine receptivity, it reduces implantation events, likely through a disruption in myometrial activity and embryo development. The wider implication of this study is that ovarian stimulation, which results in supraphysiological levels of E2 and P4 and changes (depending on the degree of stimulation) in the E2:P4 ratio, triggers abnormal expression of uterine AQP during pregnancy, and this is associated with implantation failure. These findings lead us to recognize that abnormal expression would also occur under any pathological state (such as endometriosis) that is associated with changes in the normal E2:P4 ratio. Thus, infertility among these patients might in part be linked to abnormal uterine AQP expression., (© The Author(s) 2020. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For permissions, please e-mail: journals.permission@oup.com.)

The lens of the eye is an avascular and anuclear tissue that serves to focus objects on the retina. Cataract is opacity within the clear lens that changes the transparency and refractive index of the lens causing significant visual impairments. These impairments can severely restrict the ability to carry out daily activities. Cataracts is common among elderly person occurring in more than 80% of patients aged 80 or older. Notably, we have recently identified key compounds that are effective against cataract formation. Presbyopia is also an ocular disease that typically develops in people over the age of 45 while affecting almost 100% of people over the age of 65. Recent research suggests that age-related changes in hydrostatic pressure of the lens controlled by Na/K ATPase contribute to the development of presbyopia. In the lens, Na/K ATPase has been shown to be regulated by transient receptor potential cation channels, vanilloid 1 (TRPV1) and 4, thus suggesting the potential role of TRPV1 and TRPV4 in the development of presbyopia. This review article summarizes data obtained from our laboratory with my colleagues highlighting the critical role of aquaporin 0 (AQP0) in maintaining a healthy lens redox environment, key molecules that delay the onset of cataract in vivo, as well as potential mechanisms of lens hydrostatic pressure control that may be associated with presbyopia.

The purpose of this minireview is to show that a new paradigm is developing regarding hepatic bile flow. The focus thus far has been on carrier-mediated transport of bile acids and other solutes, such as glutathione, which create an osmotic gradient for the transcellular and paracellular flow of water into canaliculi. In addition to the physicochemical properties of bile acids, which govern the osmotic gradient, data now exist showing that the tight junctions governing paracellular water flow and Aquaporin-8 water channels governing transcellular water flow are regulated independently. Thus, the rate of water flow into the canaliculus in response to bile acid transport is variable and determines canalicular bile acid concentration, which affects the production and solubilization of cholesterol-lecithin vesicles. These new considerations modify thinking regarding the occurrence of cholestasis and its progression and reorient the design of experimental studies that can distinguish the different determinants of bile flow. SIGNIFICANCE STATEMENT: The paradigm that water flow into the canaliculus is determined only by the rate of carrier-mediated transport has been challenged recently by the changes that occur in hepatic bile composition in the Claudin-2 knockout mouse and with the cholestatic effect of estradiol 17 β -d-glucuronide. Thus, a respective reduction in paracellular or transcellular canalicular water flow, probably via Aquaporin 8, has no significant effect on bile acid excretion., (Copyright © 2019 by The American Society for Pharmacology and Experimental Therapeutics.)

Aquaporins are integral membrane proteins that facilitate the diffusion of water and other small, uncharged solutes across the cellular membrane and are widely distributed in organisms from humans to bacteria. However, the characteristics of prokaryotic aquaporins remain largely unknown. We investigated the distribution and sequence characterization of aquaporins in prokaryotic organisms and summarized the transport characteristics, physiological functions, and regulatory mechanisms of prokaryotic aquaporins. Aquaporin homologues were identified in 3315 prokaryotic genomes retrieved from the Kyoto Encyclopedia of Genes and Genomes (KEGG) database, but the protein clustering pattern is not completely congruent with the phylogeny of the species that carry them. Moreover, prokaryotic aquaporins display diversified aromatic/arginine constriction region (ar/R) amino acid compositions, implying multiple functions. The typical water and glycerol transport characterization, physiological functions, and regulations have been extensively studied in Escherichia coli AqpZ and GlpF. A Streptococcus aquaporin has recently been verified to facilitate the efflux of endogenous H 2 O 2 , which not only contributes to detoxification but also to species competitiveness, improving our understanding of prokaryotic aquaporins. Furthermore, recent studies revealed novel regulatory mechanisms of prokaryotic aquaporins at post-translational level. Thus, we propose that intensive investigation on prokaryotic aquaporins would extend the functional categories and working mechanisms of these ubiquitous, intrinsic membrane proteins., Competing Interests: The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript; or in the decision to publish the results.

Objective: We previously reported that tissue-specific effects of estrogen on Aquaporin-7 (AQP7) expression are associated with the development of menopausal obesity. The current study was designed to identify the estrogen response elements (EREs) in the promoter of Aqp7 and investigate the role of AQP7 in the regulation of estrogen-induced anti-adipogenesis. Methods: We measured AQP7 expression and intracellular fat accumulation in 3T3-L1 adipocytes either silenced with shRNA or treated with estrogen receptor (ER)-specific antagonists or agonists before exposure to estrogen. EREs were predicted by Bioinformatics, assessed by chromatin immunoprecipitation, and verified by luciferase reporter assay. Results: We found that regulation of AQP7 expression was mainly via ERα, as confirmed by the use of ER selective antagonists and agonists. In addition, the induction of AQP7 expression by estrogen was linked to ER binding with two EREs in the promoter region of Aqp7 . Furthermore, we found that the regulation of adipogenesis by 17β-estradiol was AQP7 dependent, as evidenced by the increase in fat accumulation after silencing AQP7. Conclusions: Estrogen induces AQP7 expression by binding EREs in the promoter of the Aqp7 gene, resulting in fat catabolism of adipocyte. These results provide new insights into the molecular mechanisms underpinning the anti-adipogenic effect of estrogen.

Purpose: Connexins and aquaporins play essential roles in maintaining lens homeostasis and transparency and there is a close physical and functional relationship between these two proteins. Aquaporin 0 (AQP0), in addition to its role in water transport in the lens, acts as a cell-cell adhesion molecule. Recently, we showed a new role of connexin (Cx) 50 in mediating cell-cell adhesion. However, the cooperative roles of these two proteins in the lens in vivo have not been reported., Methods: We generated an AQP0/Cx50 double knockout (dKO) mouse model. Light, fluorescence, transmission thin section, and freeze-fracture electron microscopy, as well as wheat germ agglutinin and phalloidin labeling were used to evaluate lens structure. Mechanical properties of lenses were determined by mechanical compression testing., Results: DKO mice exhibited small eyes and lenses with severe cataracts, along with lens posterior defects, including posterior capsule rupture. The dKO mouse lenses had severe structural disruption associated with increased spaces between lens fiber cells when compared with wild-type lenses or lenses deficient in either Cx50 or AQP0. DKO mice also exhibited greater reduction in lens size compared with Cx50 KO mice. Gap-junction plaque size was greatly decreased in cortical fiber cells in dKO mice. Moreover, lens stiffness and elasticity were completely diminished, exhibiting a gelatinous texture in adult dKO mice., Conclusions: This novel mouse model reveals that Cx50 and AQP0 play an important role in mediating cell-cell adhesion function in the lens fiber cells and their deficiency impairs lens fiber organization, integrity, mechanical properties, and lens development.

Background: Inflammatory cytokines enhanced the progress of the pathogenesis of osteoarthritis, however the mechanisms remain unclear. The objective is to determine aquaporins (AQPs) in the pathogenesis of osteoarthritis., Methods and Findings: Primary rat articular chondrocytes were treated with IL-1β to mimic the early stage of osteoarthritis in vitro. Early osteoarthritis animal model was established by intra-articular injection of 4% papain. Micro- or ultra-structure histopathologic changes, cell viability, apoptosis cells and cell membrane permeability, locations and expressions of AQP1 and AQP3 and matrix were detected in the cartilage or in the chondrocytes of knee. IL-1β could reduce the chondrocytes viability, increase the apoptosis cells, and also impair the cell membrane and organelles. IL-1β significantly induced the up-regulation of AQP1 and AQP3 in the chondrocytes. In the chondrocytes, AQPs were mainly clustered in both membrane and perinuclear region of cytoplasm, while higher AQPs were detected in the superficial and middle layers of the cartilage. With the up-regulation of AQPs, the cartilage matrix was considerably decreased in both the chondrocytes and in the osteoarthritis cartilage. In the early osteoarthritis rat model, serum and synovial fluid confirmed that higher IL-1β could increase the expressions of AQPs, and decrease the cartilage matrix in both the chondrocytes and the cartilage., Conclusions: Inflammatory cytokine IL-1β via up-regulation of AQPs caused the abnormal metabolism of water transport and loss of the cartilage matrix in the chondrocytes, and ultimately exacerbated the pathogenesis of early osteoarthritis. Therefore, AQPs may be a candidate therapeutic target for prevention and treatment of osteoarthritis., Competing Interests: The authors have declared that no competing interests exist.

Background: Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.)., Results: In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Froger's positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of cucumber AQP genes (CsAQPs). Three aquaporins (CsTIP1;1, CsPIP2;4, and CsPIP1;2) were the most transcript abundance genes, with CsTIP1;1 showing the highest expression levels among all aquaporins. Subcellular localization analysis in Nicotiana benthamiana epidermal cells revealed the diverse and broad array of sub-cellular localizations of CsAQPs. We then performed RNA-seq to identify the expression pattern of CsAQPs under salt stress and found a general decreased expression level of root CsAQPs. Moreover, qRT-PCR revealed rapid changes in the expression levels of CsAQPs in response to diverse abiotic stresses including salt, polyethylene glycol (PEG)-6000, heat, and chilling stresses. Additionally, transient expression of AQPs in N. benthamiana increased leaf water loss rate, suggesting their potential roles in the regulation of plant water status under stress conditions., Conclusions: Our results indicated that CsAQPs play important roles in response to salt stress. The genome-wide identification and primary function characterization of cucumber aquaporins provides insight to elucidate the complexity of the AQP gene family and their biological functions in cucumber.

Aquaporins influence water flow in plants, yet little is known of their involvement in the water-driven process of seed germination. We therefore investigated their role in seeds in the laboratory and under field and global warming conditions. We mapped the expression of tonoplast intrinsic proteins (TIPs) during dormancy cycling and during germination under normal and water stress conditions. We found that the two key tonoplast aquaporins, TIP3;1 and TIP3;2, which have previously been implicated in water or solute transport, respectively, act antagonistically to modulate the response to abscisic acid, with TIP3;1 being a positive and TIP3;2 a negative regulator. A third isoform, TIP4;1, which is normally expressed upon completion of germination, was found to play an earlier role during water stress. Seed TIPs also contribute to the regulation of depth of primary dormancy and differences in the induction of secondary dormancy during dormancy cycling. Protein and gene expression during annual cycling under field conditions and a global warming scenario further illustrate this role. We propose that the different responses of the seed TIP contribute to mechanisms that influence dormancy status and the timing of germination under variable soil conditions., (© 2019 The Authors Plant, Cell & Environment Published by John Wiley & Sons Ltd.)

Purpose: We reported previously that aquaporin 0 (AQP0) modulates lens fiber cell gap junction (GJ) channel function. The present study was conducted to find out whether the C-terminal end of AQP0 is involved in this regulation., Methods: A mouse model, AQP0ΔC/ΔC, was genetically engineered to express AQP0 with 1-246 amino acids, without the normal intact AQP0 (1-263 amino acids) in the lens. Transparency and focusing of the lens were assessed. Intracellular impedance was measured to determine GJ coupling resistance. Intracellular hydrostatic pressure (HP) was also determined. Western blotting was performed to determine connexin (Cx46 and Cx50) expression levels., Results: At postnatal day 10, AQP0ΔC/ΔC mouse lenses relative to age-matched wild-type lenses showed loss of transparency and abnormal optical distortion; GJ coupling resistance increased in the differentiating (1.6-fold) and mature (8-fold) fiber cells; lens HP increased approximately 1.5-fold at the junction between the differentiating and mature fiber cells and approximately 2.0-fold in the center; there was no significant change (P > 0.05) in expression levels of Cx46 or Cx50., Conclusions: The increase in GJ coupling resistance was not associated with reduced connexin expression, suggesting either a reduction in the open probability or some physical change in plaque location. The increase in resistance was significantly greater than the increase in HP, suggesting less pressure-driven water flow through each open GJ channel. These changes may lead to a loss of transparency and abnormal optical distortion. Overall, our data demonstrate the C-terminal end of AQP0 is involved in modulating GJ coupling to maintain lens transparency and homeostasis.

Aquaporins are key proteins in regulating water transport, plant growth and development. In this study, we investigated the function of plasma membrane intrinsic proteins (PIPs) in both yeast (Saccharomyces cerevisiae) and rice (Oryza sativa cv. Nipponbare). Three OsPIP1s (OsPIP1;1, OsPIP1;2 and OsPIP1;3) and four OsPIP2s (OsPIP2;1, OsPIP2;3, OsPIP2;4 and OsPIP2;5) were successfully amplified and expressed in yeast. Overexpression of OsPIP2s, especially OsPIP2;1, increased yeast membrane water permeability (P f ). Root hydraulic conductivity (Lpr) was decreased by approximately four-fold in OsPIP2; 1 RNAi knock-down plants, resulting in a decrease in OsPIP2;1 expression levels of 70% and 50% in line 3 and line 4, respectively, compared to the wild type (WT) plants. No significant differences in the photosynthetic rate, transpiration rate, mesophyll conductance and chloroplast CO 2 concentration were observed between WT and OsPIP2; 1 RNAi plants. Higher stomatal conductance and intercellular CO 2 concentrations were observed in line 3 plants than in WT plants. In addition, lower root total length, surface area, root volume and fewer root tips were found in the RNAi plants than in the WT plants. Finally, the RNAi plants were more sensitive to drought stress. The results indicate that PIP2; 1 plays an important role in the regulation of water transport and plant growth., (Copyright © 2019 Elsevier Masson SAS. All rights reserved.)

Aquaporins are water channel proteins that regulate plant development, growth, and response to environmental stresses. Populus trichocarpa is one of the plants with the highest number of aquaporins in its genome, but only few of them have been characterized at the whole plant functional level. Here we analyzed a putative aquaporin gene, aqua1, a gene that encodes for a protein of 257 amino acid with the typical NPA (Asp-Pro-Ala) signature motif of the aquaporin gene family. aqua1 was down-regulated of ∼10 fold under excess Zn in both leaves and roots, and conferred Zn tolerance when expressed in yeast Zn hypersensitive strain. In vivo localization of AQUA1-GFP in Arabidopsis protoplast showed a heterogeneous distribution of this protein on different membranes destined to form aggregates related to autophagic multivesicular bodies. Zn-dependent AQUA1-GFP re-localization was perturbed by phosphatases' and kinases' inhibitors that could affect both intracellular trafficking and aquaporins' activity. Exposed to high concentration of Zn, AQUA1 also co-localized with AtTIP1;1, a well-known Arabidopsis vacuolar marker, probably in pro-vacuolar multivesicular bodies. These findings suggest that high concentration of Zn down-regulates aqua1 and causes its re-localization in new forming pro-vacuoles. This Zn-dependent re-localization appears to be mediated by mechanisms regulating intracellular trafficking and aquaporins' post-translational modifications. This functional characterization of a poplar aquaporin in response to excess Zn will be a useful reference for understanding aquaporins' roles and regulation in response to high concentration of Zn in poplar., (Copyright © 2018 The Authors. Published by Elsevier Masson SAS.. All rights reserved.)

Stomatal regulation is crucial for forest species performance and survival on drought-prone sites. We investigated the regulation of root and shoot hydraulics in three Pinus radiata clones exposed to drought stress and its coordination with stomatal conductance (g s ) and leaf water potential (Ψ leaf ). All clones experienced a substantial decrease in root-specific root hydraulic conductance (K root-r ) in response to the water stress, but leaf-specific shoot hydraulic conductance (K shoot-l ) did not change in any of the clones. The reduction in K root-r caused a decrease in leaf-specific whole-plant hydraulic conductance (K plant-l ). Among clones, the larger the decrease in K plant-l , the more stomata closed in response to drought. Rewatering resulted in a quick recovery of K root-r and g s . Our results demonstrated that the reduction in K plant-l , attributed to a down regulation of aquaporin activity in roots, was linked to the isohydric stomatal behaviour, resulting in a nearly constant Ψ leaf as water stress started. We concluded that higher K plant-l is associated with water stress resistance by sustaining a less negative Ψ leaf and delaying stomatal closure., (© 2018 John Wiley & Sons Ltd.)

The function of kidney is maintaining water balance of our body through regulation of urine concentration and dilution. The aquaporins are molecular basis of renal urine production and water transport, and their expression and membrane translocation are regulated delicately. Nuclear receptors are a superfamily of ligand-activated transcription factors consisting of 48 members in human. They widely participate in a variety of physiological and pathophysiological regulation including growth and development, glucose and lipid metabolism, inflammation, immunology by regulating target gene transcription and expression. Increasing evidence demonstrates that these receptors are involved in the regulation of aquaporins expression and membrane translocation in kidney, thereby playing a major role in water homeostasis. Here we review the role of nuclear receptors in regulating renal water transport.

Beta vulgaris (sugar beet) is one of the most important industrial crops. Screening of a cDNA library for sugar beet genes able to confer cold tolerance upon overexpression in yeast identified a novel aquaporin, which we named BvCOLD1. The amino acid sequence of BvCOLD1 indicated that an acidic protein (pI 5.18) is similar to tonoplast intrinsic protein aquaporins. RNA expression analysis indicated that BvCOLD1 is expressed in all sugar beet organs. Confocal microscopy of a green fluorescent protein-tagged version localized BvCOLD1 in the endoplasmic reticulum in yeast and in plant cells. Experiments in yeast showed that BvCOLD1 has an important role in transporting several molecules, among them is boron, one of the most limiting micronutrients for sugar beet cultivation. Transgenic Arabidopsis thaliana plants overexpressing BvCOLD1 showed enhanced tolerance to cold, to different abiotic stresses, and to boron deficiency at different developmental stages. Searches in databases only retrieved BvCOLD1 orthologues in genomes from the Chenopodioideae, a subfamily of the Amaranthaceae family that includes the closely related crop Spinacea oleracea and halotolerant plants such as Salicornia herbacea or Suaeda glauca. Orthologues share a conserved sequence in the carboxy terminus, not present in other aquaporins, which is required for the functionality of the protein., (© 2018 John Wiley & Sons Ltd.)

Current theory and supporting research suggests that radial transport is the most limiting factor to root water uptake, raising the question whether only absorbing root length and radial conductivity matter to water uptake. Here, we extended the porous pipe analytical model of root water uptake to entire root networks in 3D and analysed the relative importance of axial and radial characteristics to total uptake over parameter ranges reported in the literature. We found that network conductance can be more sensitive to axial than radial conductance of absorbing roots. When axial transport limits uptake, more dichotomous topology, especially towards the base of the network, increases water uptake efficiency, while the effect of root length is reduced. Whole root system conductance was sensitive to radial transport and length in model lupin (Lupinus angustifolius L.), but to axial transport and topology in wheat (Triticum aestivum L.), suggesting the root habit niche space of monocots may be constrained by their loss of secondary growth. A deep tap root calibrated to oak (Quercus fusiformis J. Buchholz) hydraulic parameters required 15 times more xylem volume to transport comparable amounts of water once recalibrated to parameters from juniper (Juniperus ashei Small 1901), showing that anatomical constraints on axial conductance can lead to significant trade-offs in woody roots as well. Root system water uptake responds to axial transport and can be limited by it in a biologically meaningful way., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

The recent discoveries of the glymphatic and lymphatic systems of the brain have helped advance our understanding of CSF physiology and may allow new insights in the understanding of idiopathic intracranial hypertension (IIH). The clinical and radiologic presentations of IIH appear to be related to congestion of the glymphatic system associated with an overflow of the lymphatic CSF outflow pathway. By revisiting the role of "vascular arachnoid granulations" in the brain, we hypothesize that an initial impairment of the transport of interstitial fluid from the glymphatic system to the venous blood of the dural sinuses may trigger the hydrodynamic cascade of IIH. Furthermore, we speculate that, similar to other water-exchange systems in the brain, a specific subtype of aquaporin is involved in this transport. This theory may eventually help to provide an underlying explanation for IIH and its associated conditions, since in most of them, the expression of several aquaporins is altered., (© 2018 American Academy of Neurology.)