Relevant bibliographies by topics / Aquaporin 1 inhibitors

Academic literature on the topic 'Aquaporin 1 inhibitors'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Aquaporin 1 inhibitors"

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Esteva-Font, Cristina, Byung-Ju Jin, Sujin Lee, Puay-Wah Phuan, Marc O. Anderson, and A. S. Verkman. "Experimental Evaluation of Proposed Small-Molecule Inhibitors of Water Channel Aquaporin-1." Molecular Pharmacology 89, no. 6 (March 18, 2016): 686–93. http://dx.doi.org/10.1124/mol.116.103929.

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Patil, Rajkumar V., Shouxi Xu, Alfred N. van Hoek, Andrew Rusinko, Zixia Feng, Jesse May, Mark Hellberg, et al. "Rapid Identification of Novel Inhibitors of the Human Aquaporin-1 Water Channel." Chemical Biology & Drug Design 87, no. 5 (January 17, 2016): 794–805. http://dx.doi.org/10.1111/cbdd.12713.

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Yamaguchi, Takeo, Yohei Iwata, Shingo Miura, Yukari Maehara, and Kazuyuki Nozawa. "Enhancement of Pressure-Induced Hemolysis by Aquaporin-1 Inhibitors in Human Erythrocytes." Bulletin of the Chemical Society of Japan 85, no. 4 (April 15, 2012): 497–503. http://dx.doi.org/10.1246/bcsj.20110285.

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Ruiz Carrillo, David, Janet To Yiu Ying, Dina Darwis, Cin Huang Soon, Tobias Cornvik, Jaume Torres, and Julien Lescar. "Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 Å." Acta Crystallographica Section F Structural Biology Communications 70, no. 12 (November 14, 2014): 1657–63. http://dx.doi.org/10.1107/s2053230x14024558.

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Aquaporin water channels (AQPs) are found in almost every organism from humans to bacteria. In humans, 13 classes of AQPs control water and glycerol homeostasis. Knockout studies have suggested that modulating the activity of AQPs could be beneficial for the treatment of several pathologies. In particular, aquaporin 1 is a key factor in cell migration and angiogenesis, and constitutes a possible target for anticancer compounds and also for the treatment of glaucoma. Here, a preliminary crystallographic analysis at 3.28 Å resolution of crystals of human aquaporin 1 (hAQP1) obtained from protein expressed in Sf9 insect cells is reported. The crystals belonged to the tetragonal space groupI422, with unit-cell parametersa=b= 89.28,c= 174.9 Å, and contained one monomer per asymmetric unit. The hAQP1 biological tetramer is generatedviathe crystallographic fourfold axis. This work extends previous electron crystallographic studies that used material extracted from human red blood cells, in which the resolution was limited to approximately 3.8 Å. It will inform efforts to improve lattice contacts and the diffraction limit for the future structure-based discovery of specific hAQP1 inhibitors.
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Bauer, Georg. "Inhibition of Membrane-Associated Catalase, Extracellular ROS/RNS Signaling and Aquaporin/H2O2-Mediated Intracellular Glutathione Depletion Cooperate during Apoptosis Induction in the Human Gastric Carcinoma Cell Line MKN-45." Antioxidants 10, no. 10 (October 9, 2021): 1585. http://dx.doi.org/10.3390/antiox10101585.

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The human gastric carcinoma cell line MKN-45 is a prototype of bona fide tumor cells, as it is protected from the NADPH oxidase-1 (NOX-1)-driven HOCl- and nitric oxide (NO)/peroxynitrite apoptosis-inducing signaling pathways by a membrane-associated catalase. The use of inhibitors/scavengers shows that inhibition of membrane-associated catalase is sufficient for the activation of NO/peroxynitrite or HOCl signaling. However, this signaling is not sufficient for apoptosis induction, as intracellular glutathione peroxidase/glutathione counteracts these signaling effects. Therefore, intrusion of extracellular tumor cell-derived H2O2 through aquaporins is required for the full apoptosis-inducing effect of extracellular reactive oxygen/nitrogen species. This secondary step in apoptosis induction can be prevented by inhibition of aquaporins, inhibition of NOX1 and decomposition of H2O2. Pretreatment with inhibitors of glutathione synthase or the cysteine-glutamine antiporter (xC transporter) abrogate the requirement for aquaporin/H2O2-mediated glutathione depletion, thus demonstrating that intracellular glutathione is the target of intruding H2O2. These data allow definition of mechanistic interactions between ROS/RNS signaling after inhibition of membrane-associated catalase, the sensitizing effects of aquaporins/H2O2 and the counteraction of the xC transporter/glutathione synthase system. Knowledge of these mechanistic interactions is required for the understanding of selective apoptosis induction in tumor cells through reestablishment of apoptosis-inducing ROS/RNS signaling.
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Schnitzer, J. E., and P. Oh. "Aquaporin-1 in plasma membrane and caveolae provides mercury-sensitive water channels across lung endothelium." American Journal of Physiology-Heart and Circulatory Physiology 270, no. 1 (January 1, 1996): H416—H422. http://dx.doi.org/10.1152/ajpheart.1996.270.1.h416.

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Classically, water transport across endothelium of the continuous type found in the microvessels of many organs such as lung was thought to occur almost completely via the paracellular pathway through intercellular junctions. Direct transmembrane and transcellular transport was considered to be minimal. In this study, we focused on the critical transport interface in direct contact with the circulating blood by purifying luminal endothelial cell plasma membranes directly from rat lungs and then isolating the noncoated plasmalemmal vesicles or caveolae from these membranes. Immunoblotting of these fractions showed that the transmembrane water channel protein aquaporin-1 was amply expressed on the endothelial cell surface at levels comparable to rat erythrocyte plasma membranes. It was found concentrated, but not exclusively, in caveolae. The functional role of these water channels in transport was examined in rat lungs perfused in situ with tritiated water by testing known inhibitors of aquaporin-1-mediated transmembrane water transport. Mercurial sulfhydryl reagents such as HgCl2 reversibly reduced tritiated water uptake without affecting small solute transport. Just like certain epithelia, endothelia might express physiologically relevant amounts of aquaporin-1 on their cell surface to permit direct, mercurial-sensitive, transcellular transport of water.
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Yang, Baoxue, Jung Kyung Kim, and A. S. Verkman. "Comparative efficacy of HgCl2with candidate aquaporin-1 inhibitors DMSO, gold, TEA+and acetazolamide." FEBS Letters 580, no. 28-29 (November 20, 2006): 6679–84. http://dx.doi.org/10.1016/j.febslet.2006.11.025.

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8

Lee, Wing-Kee, Ulrich Bork, Fatemeh Gholamrezaei, and Frank Thévenod. "Cd2+-induced cytochrome c release in apoptotic proximal tubule cells: role of mitochondrial permeability transition pore and Ca2+ uniporter." American Journal of Physiology-Renal Physiology 288, no. 1 (January 2005): F27—F39. http://dx.doi.org/10.1152/ajprenal.00224.2004.

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Cd2+ induces apoptosis of kidney proximal tubule (PT) cells. Mitochondria play a pivotal role in toxic compound-induced apoptosis by releasing cytochrome c. Our objective was to investigate the mechanisms underlying Cd2+-induced cytochrome c release from mitochondria in rat PT cells. Using Hoechst 33342 or MTT assay, 10 μM Cd2+ induced ∼5–10% apoptosis in PT cells at 6 and 24 h, which was associated with cytochrome c and apoptosis-inducing factor release at 24 h only. This correlated with previously described maximal intracellular Cd2+ concentrations at 24 h, suggesting that elevated Cd2+ may directly induce mitochondrial liberation of proapoptotic factors. Indeed, Cd2+ caused swelling of energized isolated kidney cortex mitochondria (EC50 ∼9 μM) and cytochrome c release, which were independent of permeability transition pore (PTP) opening since PTP inhibitors cyclosporin A or bongkrekic acid had no effect. On the contrary, Cd2+ inhibited swelling and cytochrome c release induced by PTP openers (PO43− or H2O2+Ca2+). The mitochondrial Ca2+ uniporter (MCU) played a key role in mitochondrial damage: 1) MCU inhibitors (La3+, ruthenium red, Ru360) prevented swelling and cytochrome c release; and 2) ruthenium red attenuated Cd2+ inhibition of PO43−-induced swelling. Using the Cd2+-sensitive fluorescent indicator FluoZin-1, Cd2+ was also taken up by mitoplasts. The aquaporin inhibitor AgNO3 abolished Cd2+-induced swelling of mitoplasts. This could be partially mediated by activation of the mitoplast-enriched water channel aquaporin-8. Thus cytosolic Cd2+ concentrations exceeding a certain threshold may directly cause mitochondrial damage and apoptotic development by interacting with MCU and water channels in the inner mitochondrial membrane.
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Chen, Gang, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Hiroshi Yoshimura, and Kazuo Hosoi. "Effects of isoproterenol on aquaporin 5 levels in the parotid gland of mice in vivo." American Journal of Physiology-Endocrinology and Metabolism 306, no. 1 (January 1, 2014): E100—E108. http://dx.doi.org/10.1152/ajpendo.00317.2013.

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In the membrane fraction of mouse parotid gland (PG), the protein level of aquaporin 5 (AQP5), a member of the water channel family, was increased by injection (ip) of isoproterenol (IPR), a β-adrenergic agonist, at 1 h, and stayed at high levels until 6 h; this change occurred simultaneously as amylase secretion. The AQP5 level then decreased and returned toward the original level at 12–48 h. After IPR injection, the AQP5 mRNA gradually increased and reached a maximum at 24 h. The facts suggest a rapid appearance of AQP5 at plasma membrane by IPR and subsequent degradation/metabolism by activation of proteolytic systems. Pretreatment of animals with two calpain inhibitors, N-Ac-Leu-Leu-methininal (ALLM) and calpeptin, as well as a protein synthesis inhibitor, cycloheximide (CHX), significantly suppressed the IPR-induced AQP5 degradation in the PG membrane fraction; such suppression was not observed by two proteasome inhibitors, MG132 and lactacystin, or the lysosome denaturant chloroquine, although most of these inhibitors increased AQP5 protein levels in unstimulated mice. The AQP5 protein was also degraded by μ-calpain in vitro. Furthermore, we demonstrated that μ-calpain was colocalized with AQP5 in the acinar cells by immunohistochemistry, and its activity in the PG was increased at 6 h after IPR injection. These results suggest that the calpain system was responsible for IPR-induced AQP5 degradation in the parotid gland and that such a system was coupled to the secretory-restoration cycle of amylase in the PG.
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Rammos, G., A. Panutsopoulos, K. Xynos, E. Koufogeorga, V. Peppes, K. Kostopoulos, and P. Turli. "Hyponatremia and Selective Serotonin Reuptake Inhibitors." European Psychiatry 24, S1 (January 2009): 1. http://dx.doi.org/10.1016/s0924-9338(09)70746-1.

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Aims:Hyponatremia (HPN) is a potentially lethal electrolytic disturbance. Certain medical treatments are integrated in the etiology of that sodium disorder. We retrospectively studied the rate of HPN in patients examined in the emergency room (ER) of Alexandra Hospital receiving a selective serotonin reuptake inhibitor (SSRI).Methods:17,410 patients, 55.54% women and 44.46% men were examined in the ER over a one year period. 281 patients (1,61% of total) presented with HPN, 162 were women (57.6%) and 121 (42.3%) men. Plasma Sodium values ≤ 133mEq/l defined HPN. 13 of the 281 patients with HPN (4.6%) with no renal, heart or hepatic impairment were on an SSRI regimen.Results:11 of 162 women (6.8%) presented with HPN were receiving concurrently SSRI and either thiazide diuretic (3 ) or furosemide (2 ). 2 of 121 men (1.65%) were on SSRI regimen and furosemide. SSRI dosage was in all cases within suggested therapeutic limits. Table 1 demonstrates mean values and standard deviation of all the parameters examined.PatientsAgePlasma Na+Plasma K+Plasma CreatininePlasma UreaHct1366,9 +/- 17,4 years127,2 +/- 6,1 mEq/4 +/- 0,7 mEq/l1.06 +/-0,5 mg%39,8 +/- 16,2 mg%36,7 +/ 2,9%Conclusion:SSRI therapy presents a potential cause for HPN principally in women older than 65 years old with increasing risk when diuretic is used concomitantly. Syndrome of inappropriate antidiuretic hormone secretion (SIADH) and expression conversion of aquaporin-2 receptors of the collecting ducts are two possible pathophysiologic mechanisms of HPN occurrence.
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Dissertations / Theses on the topic "Aquaporin 1 inhibitors"

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Tomita, Yoko. "Evaluation of Anti-Cancer Effect of Synthetic and Plant-based Inhibitors of Aquaporin 1 in Colon Cancer." Thesis, 2021. https://hdl.handle.net/2440/134152.

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Efficacy of chemotherapy and biological therapy has been established in the management of colorectal cancer (CRC), however, toxicity and development of resistance remain problematic, highlighting the need for more effective and less toxic therapeutics for this disease. Aquaporin (AQP) 1 is a dual water and ion channel, expression of which is induced during early colon cancer tumorigenesis and correlates with clinical features. AqB013 and AqB050 are bumetanide derived synthetic small molecules, while bacopaside (bac) I and II are triterpene saponins isolated from a medicinal plant Bacopa monnieri. These compounds all exhibit anti-AQP1 activity. This thesis describes the research evaluating AQP1 as a prognostic biomarker in CRC patients, down-streaming signalling molecules for AQP1-mediated migration and invasion, and anti-cancer effect of four compounds with anti-AQP1 activity: AqB013, AqB050, bac I and bac II. In vitro cytotoxic, anti-proliferative, anti-migratory, anti-tubulogenic and pro-apoptotic effects of these compounds were examined on HT-29 colon cancer, 2H-11 and 3B-11 murine, and human umbilical vascular endothelial cell (HUVEC) lines, using MTS viability, crystal violet, annexin V and propidium iodide (PI) staining, circular scratch wound, tube formation and caspase 3/7 apoptosis assays. For bac I and II specifically, synergy of the two compounds were assessed using isobologram method and mechanisms underlying their cytotoxicity was explored by examining their effect on Ca2+ flux and the plasma membrane integrity with Fluo-8 calcium flux and PI assays, respectively. In vivo, efficacy of AqB013 and AqB050 was tested with Matrigel assay and in a murine subcutaneous model of colon cancer. In the small cohort of CRC patients from a single institution, no correlation was found between AQP1 transcript expression and overall survival outcome. Expression level of seven EMT associated genes (IL1RN, BMP7, CALD1, CAV2, ITGA5, MMP9 and VCAN) markedly differed between the two colon cancer cell lines with dissimilar AQP1 expression, however, if and how their gene products are involved in AQP1-mediated tumour cell migration and invasion remain unknown. Anti-proliferative, anti-migratory and anti-tubulogenic effect of AqB013 and/or AqB050 was demonstrated in colon cancer and endothelial cells in vitro. Anti-tumour efficacy of AqB050 partly through inhibition of tumour angiogenesis was confirmed in the animal model, raising the potential therapeutic utility of this compound. For bac I and II, their synergism in inhibiting viability of colon cancer and endothelial cells was shown and the combination treatment impaired proliferation, migration and tube formation of colon cancer and endothelial cells in vitro. Treatment-induced induction of apoptosis and disruption of the plasma membrane integrity were cell line-dependent, while cytosolic Ca2+ flux occurred in all three cell lines examined. Findings suggest both apoptotic and non-apoptotic cell death is involved in combined bac I and II-mediated cytotoxicity and support the idea that transmembrane proteins such as AQP1 is a site of their action. Further research is required to better understand their anti-cancer mechanisms and the in vivo efficacy.
Thesis (Ph.D.) -- University of Adelaide, Adelaide Medical School, 2021
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Conference papers on the topic "Aquaporin 1 inhibitors"

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Jiang, Yong, Xin Zhang, Kun Chen, Rui Su, and Tongcun Zhang. "Aquaporin-1 Deletion in Mice Inhibits Hepa1-6 Hepatocellular Carcinoma Growth." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162405.

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Jiang, Yong, Kun Chen, Tongcun Zhang, and Xuegang Luo. "Down-Regulation of Aquaporin-1 in W489 Colon Cancer Cells Inhibits Cell Migration." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162661.

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