AQP10
- Known as:
- AQP10
- Catalog number:
- 001818A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AQP10
Related genes to: AQP10
- Gene:
- AQP10 NIH gene
- Name:
- aquaporin 10
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-04
- Date modifiied:
- 2014-11-18
Related products to: AQP10
Related articles to: AQP10
- Chronic exposure to inorganic arsenic affects more than 200 million people, and disease outcome varies widely among individuals with comparable intake. Explanations have centered on arsenic metabolism, which acts on arsenite that is already inside the cell. Uptake sits upstream of metabolism and sets how much arsenite reaches the genome, yet whether it acts as a gene-by-environment modifier of genotoxicity has been asserted far more often than it has been measured. We expressed human aquaporin-3 (AQP3), its point mutants and the paralogues AQP7, AQP9 and AQP10 in three human cell lines, and measured DNA damage as γH2AX by flow cytometry against a damage threshold re-derived from mock-transfected cells in every experiment. In lung fibroblasts, AQP3 raised the γH2AX-high fraction 2.36-fold at 5 μM arsenite. Because a gene-by-environment interaction widens the genotype gap with dose while an independent genotoxin would not, the combination exceeds what the two factors would produce if they simply added by 6.36 percentage points, which is an interaction. The response required the AQP3 sequence, was suppressed by N-acetylcysteine in proportion to arsenite dose, was absent in RKO cells, and was shared with AQP9 and AQP10, which created an arsenite dose-response in a cell line that had none of its own. Low-input RNA sequencing of 135 ten-cell pools located the effect inside the cell: at an identical 1 μM applied dose and within a single batch, AQP3 raised (induced when trivalent arsenic modifies KEAP1 thiols, and so a report of intracellular rather than applied exposure) 3.3-fold, a shift equivalent to 40% of the 1-to-10 μM interval on the measured dose-response, while AQP3 without arsenite was indistinguishable from untreated. Duplex sequencing detected no consistent change in somatic mutation frequency from arsenite alone at any dose to 10 μM, in an assay that resolved a 26-fold response to N-ethyl-N-nitrosourea; the arsenite-induced mutation frequency at the locus nonetheless differed 1.61-fold by AQP3 genotype. The interaction is therefore not unique to AQP3, and aquaglyceroporin complement belongs alongside metabolism among the host factors that set arsenic susceptibility. - Source: PubMed
Publication date: 2026/09/24
Yin ShiweiFeng BingruVaziripour MaryamSlewitzke Shannon EFernandes Gail FYun JihyeAmos Christopher IXia Jun - Human metabolism converts inorganic arsenic to the pentavalent methylated species MMA(V) and DMA(V), the forms most people excrete, and the forms long read as the end of a detoxification pathway. Whether a transporter sets how much of these metabolites reaches the genome has not been tested in a mammalian cell. We expressed human AQP3, AQP7, AQP9 or AQP10 in HEK293T and MRC5-SV40 cells and measured γH2AX by flow cytometry across dose series of As(V), MMA(V) and DMA(V), pairing every aquaporin with a GFP-Tubulin control and an untransfected mock acquired in the same run. As(V) was inactive in HEK293T cells and only weakly active in MRC5-SV40 cells to 20 µM, and both methylated species damaged DNA only in the millimolar range, DMA(V) being the more potent of the two in both cell lines. Against that weak baseline, AQP9 and AQP10 raised DMA(V)-induced γH2AX in HEK293T cells by roughly 17 percentage points over the matched control, more than doubling the damage the same exposure produced in control cells, whereas AQP3 and AQP7 changed it not at all. AQP9 alone remained active with MMA(V). The ranking held in MRC5-SV40 fibroblasts at one-sixth the size, and within single wells the damage rose with the amount of AQP9 a cell carried while the control was flat. Aquaglyceroporins therefore discriminate among arsenic species, and AQP9 and AQP10 turn a weakly genotoxic metabolite into a substantially more genotoxic one. - Source: PubMed
Publication date: 2026/09/25
Yin ShiweiFeng BingruVaziripour MaryamXia Jun - Human aquaporins are integral membrane proteins that facilitate transmembrane transport of small molecules. Among the 13 members of this family, pH-regulated human aquaporin-10 (hAQP10) plays a critical role in glycerol metabolism and lipid homeostasis. A molecular-level understanding of water and glycerol transport through hAQP10 nanopores is essential for enabling rational therapeutic interventions. We present an all-atom molecular dynamics (MD) simulation study characterizing the nanoscale structure, thermodynamic stability, and glycerol permeability of tetrameric hAQP10 channels embedded in lipid bilayer membranes. Using equilibrium and advanced sampling MD simulations, we investigate the cooperative diffusion of water and glycerol through the channel. Free energy (ΔG) landscape derived from replica-exchange umbrella sampling simulations reveals multiple binding sites and energy barriers of a few kT along the channel axis. Integrating the (ΔG) profile with the inhomogeneous solubility-diffusion model, we estimate a single channel diffusive permeability of glycerol through hAQP10 to be 4 × 10 cm/s at a concentration of 100 mM. Glycerol residence times in the channel during unbiased simulations range from nanoseconds to microseconds. Transport kinetics, characterized using a theoretical model derived by coarse-graining all-atom simulation trajectories, indicate a mean first-passage time of several microseconds. Steered molecular dynamics simulations comparing water and glycerol permeation energetics reveal similar barriers in the open conformation. Together, these findings provide a comprehensive quantitative picture of glycerol and water permeation through hAQP10, with potential implications in understanding physiological role of hAQP10 in human health. - Source: PubMed
Publication date: 2026/08/14
Rai KunalJoshi Himanshu - The aquaporin genes (aqps) are widely distributed among vertebrates. In cartilaginous fish, aqp3 and aqp10 are duplicated, whereas many species have lost aqp8. While the solute permeability of aquaglyceroporins and Aqp8 exhibits significant diversity, systematic evaluations of their activity within species are limited. Consequently, we conducted a comprehensive analysis of the aqps in various cartilaginous fish genome databases. Our analysis revealed that the sharpnose sevengill shark (Heptranchias perlo) and North Pacific spiny dogfish (Squalus suckleyi) possess all aqp genes found in cartilaginous fish, rendering them suitable for comparative analysis of Aqp activity. The activity of all aquaglyceroporins and Aqp8 in the sharpnose sevengill shark was analyzed using Xenopus oocyte swelling assays. The water permeability of Aqp3c2, Aqp8, Aqp9, Aqp10c1, and Aqp10c2; the glycerol permeability of Aqp3c2, Aqp9, and Aqp10c2; the urea permeability of Aqp3c2, Aqp8, Aqp9, and Aqp10c2; and the boric acid permeability of Aqp8 and Aqp9 were determined. The urea and boric acid permeabilities of Aqp9 were higher than those of other Aqps. Our results provide genomic evidence for the loss of aqp7 and further elucidate the diversification of aqp8 in cartilaginous fishes. Moreover, the urea permeability of Aqp9 suggests a functional role in their unique urea-based osmoregulation strategy. - Source: PubMed
Hidaka ShinichiroNagashima AyumiKato Akira - Aquaporins (AQPs) are transmembrane channel proteins that transport water and small solutes. Their dysregulation in cancer reveals functions beyond maintaining osmotic balance. This review summarizes that AQPs drive tumor progression through three core mechanisms: metabolic reprogramming, enhanced motility, and remodeling of the immune microenvironment. Specifically, AQP3, AQP7, and AQP9 serve as metabolic hubs for glycerol, while AQP3 and AQP8 help maintain redox homeostasis. AQP1 and AQP4 facilitate cell migration via hydrodynamic mechanisms, and AQP5 promotes invasion through signaling pathways such as Ras/NF-κB. In immune regulation, AQP9 and AQP3 modulate immune cell function by transporting metabolites, and AQP1 influences angiogenesis. Other isoforms, including AQP0, AQP2, AQP6, AQP10, and AQP11, also play roles in malignancy. Collectively, AQPs form a multifunctional network linking tumor metabolism, physical properties, and immunity, offering insights for novel diagnostic and therapeutic strategies. However, tissue-specific functions, complex regulatory mechanisms, and challenges in developing targeted therapies remain significant hurdles in translational medicine. - Source: PubMed
Publication date: 2026/03/26
Qu KexinWang RuiBi YingweiLiu YuxinYi BolinWang Jianbo