Relevant bibliographies by topics / AQP8

Academic literature on the topic 'AQP8'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "AQP8"

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Geyer, R. Ryan, Raif Musa-Aziz, Xue Qin, and Walter F. Boron. "Relative CO2/NH3 selectivities of mammalian aquaporins 0–9." American Journal of Physiology-Cell Physiology 304, no. 10 (May 15, 2013): C985—C994. http://dx.doi.org/10.1152/ajpcell.00033.2013.

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Previous work showed that aquaporin 1 (AQP1), AQP4-M23, and AQP5 each has a characteristic CO2/NH3 and CO2/H2O permeability ratio. The goal of the present study is to characterize AQPs 0–9, which traffic to the plasma membrane when heterologously expressed in Xenopus oocytes. We use video microscopy to compute osmotic water permeability ( Pf) and microelectrodes to record transient changes in surface pH (ΔpHS) caused by CO2 or NH3 influx. Subtracting respective values for day-matched, H2O-injected control oocytes yields the channel-specific values Pf* and ΔpHS*. We find that Pf* is significantly >0 for all AQPs tested except AQP6. (ΔpHS*)CO2 is significantly >0 for AQP0, AQP1, AQP4-M23, AQP5, AQP6, and AQP9. (ΔpHS*)NH3 is >0 for AQP1, AQP3, AQP6, AQP7, AQP8, and AQP9. The ratio (ΔpHS*)CO2/ Pf* falls in the sequence AQP6 (∞) > AQP5 > AQP4-M23 > AQP0 ≅ AQP1 ≅ AQP9 > others (0). The ratio (ΔpHS*)NH3/ Pf* falls in the sequence AQP6 (∞) > AQP3 ≅ AQP7 ≅ AQP8 ≅ AQP9 > AQP1 > others (0). Finally, the ratio (ΔpHS*)CO2/(−ΔpHS*)NH3 falls in the sequence AQP0 (∞) ≅ AQP4-M23 ≅ AQP5 > AQP6 > AQP1 > AQP9 > AQP3 (0) ≅ AQP7 ≅ AQP8. The ratio (ΔpHS*)CO2/(−ΔpHS*)NH3 is indeterminate for both AQP2 and AQP4-M1. In summary, we find that mammalian AQPs exhibit a diverse range of selectivities for CO2 vs. NH3 vs. H2O. As a consequence, by expressing specific combinations of AQPs, cells could exert considerable control over the movements of each of these three substances.
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Kendall, B., J. E. J. Maxwell, A. J. German, D. Marples, M. D. Royal, and A. Mobasheri. "Immunohistochemical localisation of aquaporin water channels in the bovine mammary gland." Proceedings of the British Society of Animal Science 2007 (April 2007): 1. http://dx.doi.org/10.1017/s1752756200019049.

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The aquaporins (AQPs) are a family of small integral membrane proteins 28-35kDa in size, sub classified into 2 groups; those selectively permeated by water (the aquaporins; AQP0, AQP1, AQP2, AQP4, AQP5, AQP6 and AQP8) or by water and small organic osmolytes such as glycerol and urea (the aquaglyceroporins; AQP3, AQP7, AQP9 and AQP10). AQPs are expressed in a variety of epithelial tissues where they are responsible for rapid water movement driven by osmotic gradients. The mammary gland produces and secretes milk which consists of water, lipids, electrolytes, vitamins, sugars and specific milk proteins. However, little is known about AQP expression, distribution and function in mammary tissue or about the process of water transport across the mammary epithelium. The only information available relates to the identification of AQP1 and AQP3 in capillary endothelia and epithelial cells of mouse mammary glands respectively (Matsuzaki et al., 2005). Since water delivery to the mammary gland is critical for milk production, which is of major economic importance to the dairy industry, it is necessary to understand the underlying physiology involved. The aim of this study was to determine the expression and distribution of AQPs within the bovine mammary gland.
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Cao, Yixin, Ying He, Cong Wei, Jing Li, Lejing Qu, Huiqin Zhang, Ying Cheng, and Boling Qiao. "Aquaporins Alteration Profiles Revealed Different Actions of Senna, Sennosides, and Sennoside A in Diarrhea-Rats." International Journal of Molecular Sciences 19, no. 10 (October 17, 2018): 3210. http://dx.doi.org/10.3390/ijms19103210.

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Senna and its main components sennosides are well-known effective laxative drugs and are used in the treatment of intestinal constipation in the world. Their potential side effects have attracted more attention in clinics but have little scientific justification. In this study, senna extract (SE), sennosides (SS), and sennoside A (SA) were prepared and used to generate diarrhea rats. The diarrhea rats were investigated with behaviors, clinical signs, organ index, pathological examination, and gene expression on multiple aquaporins (Aqps) including Aqp1, Aqp2, Aqp3, Aqp4, Aqp5, Aqp6, Aqp7, Aqp8, Aqp9, and Aqp11. Using qRT-PCR, the Aqp expression profiles were constructed for six organs including colon, kidney, liver, spleen, lung, and stomach. The Aqp alteration profiles were characterized and was performed with Principle Component Analysis (PCA). The SE treatments on the rats resulted in a significant body weight loss (p < 0.001), significant increases (p < 0.001) on the kidney index (27.72%) and liver index (42.55%), and distinguished changes with up-regulation on Aqps expressions in the kidneys and livers. The SS treatments showed prominent laxative actions and down regulation on Aqps expression in the colons. The study results indicated that the SE had more influence/toxicity on the kidneys and livers. The SS showed more powerful actions on the colons. We suggest that the caution should be particularly exercised in the patients with kidney and liver diseases when chronic using senna-based products.
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de Oliveira, Vanessa, Jennifer Schaefer, Basim Abu-Rafea, George A. Vilos, Angelos G. Vilos, Moshmi Bhattacharya, Sally Radovick, and Andy V. Babwah. "Uterine aquaporin expression is dynamically regulated by estradiol and progesterone and ovarian stimulation disrupts embryo implantation without affecting luminal closure." Molecular Human Reproduction 26, no. 3 (January 16, 2020): 154–66. http://dx.doi.org/10.1093/molehr/gaaa007.

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Abstract 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.
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Hurley, Patricia T., Carole J. Ferguson, Tae-Hwan Kwon, Marie-Louise E. Andersen, Alexander G. Norman, Martin C. Steward, Søren Nielsen, and R. Maynard Case. "Expression and immunolocalization of aquaporin water channels in rat exocrine pancreas." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 4 (April 1, 2001): G701—G709. http://dx.doi.org/10.1152/ajpgi.2001.280.4.g701.

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Both the acinar and ductal cells of the pancreas secrete a near-isotonic fluid and may thus be sites of aquaporin (AQP) water channel expression. Northern blot analysis of mRNA from whole rat pancreas revealed high levels of AQP1 and AQP8 expression, whereas lower levels of AQP4 and AQP5 expression were just detectable by RT-PCR Southern blot analysis. Immunohistochemistry showed that AQP1 is localized in the microvasculature, whereas AQP8 is confined to the apical pole of the acinar cells. No labeling of acinar, ductal, or vascular tissue was detected with antibodies to AQP2–7. With immunoelectron microscopy, AQP8 labeling was observed not only at the apical membrane of the acinar cells but also among small intracellular vesicles in the subapical cytoplasm, suggesting that there may be regulated trafficking of AQP8 to the apical plasma membrane. To evaluate the contribution of AQPs to the membrane water permeability, video microscopy was used to measure the swelling of acinar cells in response to hypotonic stress. Osmotic water permeability was reduced by 90% following exposure to Hg2+. Since AQP8 is confined to the apical membrane, the marked effect of Hg2+ suggests that other water channels may be expressed in the basolateral membrane.
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Zhou, Zuoyi, Jiangshan Zhan, Qingyun Cai, Fanqing Xu, Ruichao Chai, Kalista Lam, Zuo Luan, et al. "The Water Transport System in Astrocytes–Aquaporins." Cells 11, no. 16 (August 18, 2022): 2564. http://dx.doi.org/10.3390/cells11162564.

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Astrocytes have distinctive morphological and functional characteristics, and are found throughout the central nervous system. Astrocytes are now known to be far more than just housekeeping cells in the brain. Their functions include contributing to the formation of the blood–brain barrier, physically and metabolically supporting and communicating with neurons, regulating the formation and functions of synapses, and maintaining water homeostasis and the microenvironment in the brain. Aquaporins (AQPs) are transmembrane proteins responsible for fast water movement across cell membranes. Various subtypes of AQPs (AQP1, AQP3, AQP4, AQP5, AQP8 and AQP9) have been reported to be expressed in astrocytes, and the expressions and subcellular localizations of AQPs in astrocytes are highly correlated with both their physiological and pathophysiological functions. This review describes and summarizes the recent advances in our understanding of astrocytes and AQPs in regard to controlling water homeostasis in the brain. Findings regarding the features of different AQP subtypes, such as their expression, subcellular localization, physiological functions, and the pathophysiological roles of astrocytes are presented, with brain edema and glioma serving as two representative AQP-associated pathological conditions. The aim is to provide a better insight into the elaborate “water distribution” system in cells, exemplified by astrocytes, under normal and pathological conditions.
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Okada, Naoko, Tetsuya Kawakita, Masataka Ito, and Kazuo Tsubota. "Aquaporins 8 and 9 as Possible Markers for Adult Murine Lacrimal Gland Cells." BioMed Research International 2021 (September 9, 2021): 1–9. http://dx.doi.org/10.1155/2021/6888494.

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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 Aqp8 and Aqp9 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 Aqp3 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.
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He, Jinzhao, and Baoxue Yang. "Aquaporins in Renal Diseases." International Journal of Molecular Sciences 20, no. 2 (January 16, 2019): 366. http://dx.doi.org/10.3390/ijms20020366.

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Aquaporins (AQPs) are a family of highly selective transmembrane channels that mainly transport water across the cell and some facilitate low-molecular-weight solutes. Eight AQPs, including AQP1, AQP2, AQP3, AQP4, AQP5, AQP6, AQP7, and AQP11, are expressed in different segments and various cells in the kidney to maintain normal urine concentration function. AQP2 is critical in regulating urine concentrating ability. The expression and function of AQP2 are regulated by a series of transcriptional factors and post-transcriptional phosphorylation, ubiquitination, and glycosylation. Mutation or functional deficiency of AQP2 leads to severe nephrogenic diabetes insipidus. Studies with animal models show AQPs are related to acute kidney injury and various chronic kidney diseases, such as diabetic nephropathy, polycystic kidney disease, and renal cell carcinoma. Experimental data suggest ideal prospects for AQPs as biomarkers and therapeutic targets in clinic. This review article mainly focuses on recent advances in studying AQPs in renal diseases.
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Yang, Jinying, Shengjun Yu, Guanglan Zhang, Zheng Zheng, Ping Li, Shanshan Mei, and Xinjia Han. "Different expressions of aquaporin water channels and macrophages infiltration in human cervix remodeling during pregnancy." Biology of Reproduction 106, no. 1 (October 19, 2021): 173–84. http://dx.doi.org/10.1093/biolre/ioab191.

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Abstract 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.
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Pellavio, Giorgia, Federica Todaro, Paola Alberizzi, Claudia Scotti, Giulia Gastaldi, Marco Lolicato, Claudia Omes, Laura Caliogna, Rossella E. Nappi, and Umberto Laforenza. "HPV Infection Affects Human Sperm Functionality by Inhibition of Aquaporin-8." Cells 9, no. 5 (May 17, 2020): 1241. http://dx.doi.org/10.3390/cells9051241.

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Human sperm cells express different aquaporins (AQPs), AQP3, 7, 8, 11, which are localized both in the plasma membrane and in intracellular structures. Besides cell volume regulation and end stage of cytoplasm removal during sperm maturation, the role of AQPs extends also to reactive oxygen species (ROS) elimination. Moreover, oxidative stress has been shown to inhibit AQP-mediated H2O2 permeability. A decrease in AQPs functionality is related to a decrease in sperm cells number and motility. Here we investigate the possible effect of human Papillomavirus (HPV) on both expression and function of AQPs in human sperm cells of patients undergoing infertility couple evaluation. Stopped-flow light-scattering experiments demonstrated that HPV infection heavily reduced water permeability of sperm cells in normospermic samples. Confocal immunofluorescence experiments showed a colocalization of HPV L1 protein with AQP8 (Pearson’s correlation coefficient of 0.61), confirmed by co-immunoprecipitation experiments. No interaction of HPV with AQP3 and AQP7 was observed. A 3D model simulation of L1 protein and AQP8 interaction was also performed. Present findings may suggest that HPV infection directly inhibits AQP8 functionality and probably makes sperm cells more sensitive to oxidative stress.
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Dissertations / Theses on the topic "AQP8"

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BESTETTI, STEFANO. "AQP8, a redoxtat controlling tyrosine kinase signalling." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2017. http://hdl.handle.net/10281/170789.

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AQP8-mediated H2O2 transport allows efficient amplification of tyrosine kinase signalling, therefore influencing pathways frequently dysregulated under tumour progression. Besides, control of H2O2 cell permeability impacts life-death cell decisions in response to stress. Despite the important consequences of AQP8 gating, the precise biochemical modification that inhibits H2O2 transport still remains to be identified. We show here that the mechanism of regulation implies sulphydration of AQP8. Addition of an exogenous H2S donor (NaHS) is sufficient to block H2O2 entry and dampen EGF receptor signalling, bypassing stress. Moreover, cells expressing non-inhibitable AQP8 mutant (e.g. C53S) are able to transport H2O2 also upon H2S treatment. Stress-induced blockade of transport requires cystathionine-beta-synthase, a key enzyme in the transulphuration pathway. These findings identify a novel circuit modulating the strength and duration of key signalling pathways based on AQP8 regulation by sulphydration.
AQP8-mediated H2O2 transport allows efficient amplification of tyrosine kinase signalling, therefore influencing pathways frequently dysregulated under tumour progression. Besides, control of H2O2 cell permeability impacts life-death cell decisions in response to stress. Despite the important consequences of AQP8 gating, the precise biochemical modification that inhibits H2O2 transport still remains to be identified. We show here that the mechanism of regulation implies sulphydration of AQP8. Addition of an exogenous H2S donor (NaHS) is sufficient to block H2O2 entry and dampen EGF receptor signalling, bypassing stress. Moreover, cells expressing non-inhibitable AQP8 mutant (e.g. C53S) are able to transport H2O2 also upon H2S treatment. Stress-induced blockade of transport requires cystathionine-beta-synthase, a key enzyme in the transulphuration pathway. These findings identify a novel circuit modulating the strength and duration of key signalling pathways based on AQP8 regulation by sulphydration.
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Felemban, Dalal Nouruldeen. "The Effects of Cold and Freezing Temperatures on The Blood Brain Barrier and Aquaporin 1, 4, and 9 Expression in Cope's Gray Treefrog (Hyla Chrysoscelis)." Wright State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=wright1484650973702078.

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Stávale, Leila Miguel 1985. "Envolvimento da AQP4 no envenenamento por Phoneutria nigriventer = Involvement of AQP4 in Phoneutria nigriventer envenoming." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/317745.

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Orientador: Maria Alice da Cruz Höfling
Dissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-23T19:45:28Z (GMT). No. of bitstreams: 1 Stavale_LeilaMiguel_M.pdf: 25008584 bytes, checksum: 8754f8fc3865217986eb0137679176e9 (MD5) Previous issue date: 2013
Resumo: O veneno da aranha Phoneutria nigriventer (PNV), também conhecida como aranha armadeira, é uma mistura complexa de peptídeos com ação neurotóxica em alguns canais iônicos. No sistema nervoso central (SNC) alguns peptídeos do PNV causam permeabilização da barreira hematoencefálica (BHE) e interferem na liberação de neurotransmissores. A BHE, embora essencial para a manutenção da homeostase do SNC, pode representar uma barreira muito restritiva para o acesso de drogas terapêuticas ao microambiente neural. O entendimento dos mecanismos associados à disfunção da BHE é relevante do ponto de vista científico e médico. O objetivo do estudo foi investigar alguns mecanismos envolvidos na neurotoxicidade do veneno da Phoneutria nigriventer em ratos Wistar (Rattus norvegicus). Para esse fim, o efeito vasogênico causado pela neurotoxicidade do veneno no cérebro, foi examinado através da avaliação da expressão de aquaporina 4 (AQP4), uma proteína formadora dos canais de água e abundantemente localizada nos pés astrocitários perivasculares e relacionada com o aparecimento de edema no cérebro. A análise da expressão da proteína foi feita por imunohistoquímica e western blotting e a expressão de RNAm por PCR em tempo real no cerebelo e hipocampo de animais neonatos (14 dias) e adultos (8 semanas). Os resultados obtidos mostraram aumento da expressão de AQP4 e seu RNAm nos animais envenenados, que entretanto foi variável em função do tempo de envenenamento (2, 5 ou 24 h), da região do cerebelo ou hipocampo examinada e da idade dos animais. Os resultados mostraram também intensa marcação anti-AQP4 ao redor de vasos com edema perivascular ou não, como também entre os corpos neuronais e seus prolongamentos. Concluímos que a AQP4 tem papel nas alterações de volume dos astrócitos perivasculares e na formação e resolução do edema ao redor da BHE causado pelo PNV. A dinâmica da expressão da AQP4 no cerebelo e hipocampo em função do tempo, região e idade dos animais sugere a existência de fatores intrínsicos que modulam diferencialmente a funcionalidade da BHE em função do microambiente local. A compreensão dos mecanismos envolvidos no envenenamento por PNV pode contribuir para o desenvolvimento de ferramentas úteis para a intervenção clínica, bem como pode ser relevante para o entendimento dos mecanismos relacionados ao funcionamento da BHE e de proteínas envolvidas na formação de canais de água, como a AQP4
Abstract: The Phoneutria nigriventer spider venom (PNV), also known as armed-spider, is a complex mixture of ion channels-acting peptides which exhibit neurotoxic action. In the central nervous system (CNS), PNV-containing peptides cause permeabilization of the blood-brain barrier (BBB) and interfere with neurotransmitter release. The BBB, although essential for the maintenance of homeostasis of the CNS, may represent a very restrictive barrier for the access of therapeutic drugs into the neural microenvironment. The understanding of BBB impairment-associated mechanisms are of scientific and medical importance. The aim of this study was to investigate some of the mechanisms involved in the neurotoxicity caused by Phoneutria nigriventer venom in Wistar rats (Rattus norvegicus). To this end, the vasogenic effect caused by the venom neurotoxicity in the brain was examined by evaluating the expression of aquaporin 4 (AQP4), a water channel forming protein abundantly expressed in perivascular astrocytic endfeet processes and associated to the formation and resolution of edema in the brain. The analysis of AQP4 expression was assessed in the cerebellum and hippocampus of neonate (14 day-old) and adult rats (8 week-old) through immunohistochemistry and western blotting, and the expression of mRNA by Real Time-PCR. The results showed increases of AQP4 expression and its mRNA in the envenomed animals, which though showed time- (2, 5 or 24h), regional- (regions of the cerebellum and hippocampus examined) and age-associated differences. Marked anti-AQP4 labeling was found around vessels with or without edema and among the neuron bodies and their processes. We conclude that AQP4 has a role in the volume alterations of the perivascular astrocytes and in the formation and resolution of edema around the BBB induced by PNV. The variability of the dynamics of AQP4 expression in the cerebellum and hippocampus in function of the time, region and animals age suggests the existence of intrinsic factors that modulate the BBB functionality depending on the molecular biology dynamics of the local microenvironment. The understanding of the mechanisms involved in the envenomation by PNV can contribute to the development of useful tools for clinical intervention, and may be relevant for understanding the mechanisms related to the functioning of the BBB and proteins involved in the formation of water channels, such as AQP4
Mestrado
Histologia
Mestra em Biologia Celular e Estrutural
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Sharma, Mansi. "Regulatory mechanisms of Leishmania Aquaglyceroporin AQP1." FIU Digital Commons, 2015. http://digitalcommons.fiu.edu/etd/2300.

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Pentavalent antimonials [Sb(V)] are the primary drug of choice against all forms of leishmaniasis. Emergence of antimony unresponsiveness is a major issue. There is a dire need of understanding antimony resistance mechanisms in Leishmania. One important mechanism is the down regulation of the trivalent antimony [Sb(III)] (the active form of Sb(V)) uptake system. To date, Leishmania aquaglyceroporin AQP1 is the only reported facilitator of Sb(III). Leishmania do not have promoters. They primarily regulate their genes at post-transcriptional and/or post-translational levels. We reported that mitogen activated protein kinase 2 (MPK2) positively regulated AQP1 stability through the phosphorylation of the threonine 197 (T197) residue of AQP1. The goal of this study was to elucidate the regulatory mechanism(s) of AQP1 in Leishmania in order to advance our understanding about the physiological role(s) of AQP1 in Leishmania biology. When Leishmania promastigotes were treated with the proteasome inhibitor MG132, SbIII accumulation was increased due to upregulation of AQP1. Alteration of lysine 12 of AQP1 to either alanine or arginine improved protein stability. Cells co-expressing a dominant-negative MPK2 mutant exhibited severely reduced AQP1 expression, which was reversed upon addition of MG132. Interestingly, the dominant-negative MPK2 mutant could not destabilize either AQP1K12A /AQP1K12R. Stabilization of AQP1 by MPK2 led to its relocalization from the flagellum to the entire surface of the parasite. Both altered AQP1K12A and AQP1K12R were restricted to the flagellum only. The data demonstrated that lysine12 was targeted for AQP1 proteasomal degradation playing an integral role in subcellular localization of AQP1 as well as its interaction with MPK2. This study also demonstrated that the stability of AQP1 mRNA in different Leishmania species was regulated by their respective 3’-untranslated regions. Cutaneous leishmaniasis causing species accumulated more antimonite and therefore, exhibited higher sensitivity to antimonials than species responsible for visceral leishmaniasis. This species-specific differential sensitivity to antimonite was found to be directly proportional to the expression levels of AQP1 mRNA. The differential regulation of AQP1 mRNA explained the distinct antimonial sensitivity of each species. This study will help us to identify new drugs for treatment in the future and also lead to a novel understanding of parasite biology aspects such as integral membrane protein trafficking and regulation.
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Arif, Muhammad. "The role of aquaporin 3 (AQP3) in breast cancer." Thesis, Aston University, 2014. http://publications.aston.ac.uk/23183/.

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The increasing prevalence of breast cancer (BC) in different parts of the world, particularly in the UK, highlights the importance of research into the aetiology and pathology of the disease. BC is the most common malignancy affecting women worldwide. Aquaporins (AQPs) are membrane protein channels that regulate cellular water flow. Recently, studies have demonstrated that expression of AQP3 is up-regulated in cancerous breast tissue. The present study examines the role of AQP3 in BC cell biology. Examination of clinical cases of BC showed higher AQP3 gene and protein expression in cancer tissues compared to healthy border tissues. In distinct clinicopathological groups however there were no differences observed with regards to AQP3 expression, suggesting that AQP3 expression may not be a predictor of lymph node infiltration or tumour grade. shRNA technology was used to knockdown gene expression of AQP3 in the invasive MDA-MB-231 BC cellular model. Cellular proliferation, migration, invasion, adhesion and response to the 5- fluorouracil (5-FU) based chemotherapy treatment were investigated in parental and knockdown cell line. AQP3 knockdown cells showed reduction in cellular proliferation, migration, invasion and increase in cell sensitivity to 5-FU compared with wild type (WT) or scrambled control (SC) cells. The effects of AQP3 knockdown on cellular glycolytic ability and ATP cellular content were quantified. Indirect glucose uptake was also measured by quantifying reconditioned media. AQP3 knockdown cells showed significantly lower levels of glucose uptake as compared to WT or SC. However there was no difference in the glycolytic ability and ATP content of the cells suggesting AQP3 has no role in cancer cell energetics. These data collectively suggest AQP3 expression is associated with the BC disease clinically and plays a role in multiple important aspects of BC pathophysiology, thus AQP3 represents a novel target for therapeutic intervention.
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Dahlke, Agnes Maria [Verfasser], Michael [Gutachter] Adamzik, and Andrea [Gutachter] Tannapfel. "Methylierungsanalyse des AQP5-Promotors bei Septikern und Kontrollpatienten in Abhängigkeit vom AQP5 A (-1364) C Promotorpolymorphismus / Agnes Dahlke ; Gutachter: Michael Adamzik, Andrea Tannapfel." Bochum : Ruhr-Universität Bochum, 2017. http://d-nb.info/1129452484/34.

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Dahlke, Agnes [Verfasser], Michael [Gutachter] Adamzik, and Andrea [Gutachter] Tannapfel. "Methylierungsanalyse des AQP5-Promotors bei Septikern und Kontrollpatienten in Abhängigkeit vom AQP5 A (-1364) C Promotorpolymorphismus / Agnes Dahlke ; Gutachter: Michael Adamzik, Andrea Tannapfel." Bochum : Ruhr-Universität Bochum, 2017. http://d-nb.info/1129452484/34.

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Siordia, Juan Arturo. "V2 Receptor and AQP2 Distribution in the Kangaroo Rat Kidney." Thesis, The University of Arizona, 2011. http://hdl.handle.net/10150/144945.

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Roudier, Nathalie. "Caractérisation Structurale et Fonctionnelle de l'Aquaglycéroporine AQP3 exprimée dans divers Systèmes." Phd thesis, Université Paris Sud - Paris XI, 2000. http://tel.archives-ouvertes.fr/tel-00004048.

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Abstract:
La famille des protéines MIPs est composée de canaux hydriques et de facilitateurs de glycérol. Parmi les canaux hydriques, certains sont sélectivement perm&ables à l'eau, les aquaporines (AQP1, AQP2,...), et les autres sont également perméables aux petits solutés comme le glycérol: les aquaglycéroporines, dont AQP3 fait partie. Nous avons montré dans un premier temps que la perméabilité au glycérol du globule rouge était due à la présence d'AQP3. Dans l'intention de mieux connaître quels étaient les éléments protéiques impliqués dans la sélectivité des protéines MIPs, nous avons construit des chimères entre AQP2 et AQP3. L'une d'entre elle, AQP3-AQP2 Cter, après expression dans l'ovocyte de Xénope, a permis de montrer que la partie C terminale cytoplasmique est impliquée dans le transport d'eau mais pas dans le transport de glycérol d'AQP3. Nous avons également montré que les ovocytes de xénope non matures possédaient des perméabilités à l'eau et au glycérol supérieurs à celles des ovocytes matures suggérant l'expression d'un canal ou d'un transporteur endogène. Enfin, nous avons envisagé de déterminer pour la première fois la structure quaternaire d'une aquaglycéroporine: AQP3. Alors qu'AQP1 dévoile sa forme tétramérique sur gradient de saccharose, après solubilisation en conditions non dénaturantes, AQP3 sédimente dans des fractions plus légères sous forme d'un monomère et d'un dimère très résistant au SDS et aux agents réducteurs hydrophiles. Nous n'avons pu conclure quant à son organisation dans les membranes du fait de son éventuelle sensibilité spécifique aux détergents non dénaturants utilisés. Nous avons donc engagé des études de microscopie électronique de cryofractures de membranes d'ovocytes exprimant AQP1 et AQP3. Nous en avons déduit que la taille d'AQP3 n'était pas suffisamment différente de celle d'AQP1 pour suggérer une organisation membranaire également différente.
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Yang, Ming-Hui. "A water channel (AQP9) in retinal ganglion cell apoptosis and glaucoma." Fort Worth, Tex. : Texas Christian University, 2007. http://etd.tcu.edu/etdfiles/available/etd-04202007-153701/unrestricted/yang.pdf.

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Books on the topic "AQP8"

1

Stamatis, D. H. Advanced quality planning: A commonsense guide to AQP and APQP. Portland, Or: Productivity, 1998.

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Stamatis, D. H. Advanced quality planning: A commonsense guide to AQP and APQP. New York: Quality Resources, 1998.

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Hutchinson. CE/Wn31/D6/WP&Awp6/P&Ap45/Qp&Aqp5 P. Irwin, 1995.

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Advanced Quality Planning A Commonsense Guide To Aqp And Apqp. Productivity Press, 2001.

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Advanced Quality Planning : A Commonsense Guide to AQP and APQP. Quality Resources., 1998.

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Schreiner, Teri L., and Jeffrey L. Bennett. Neuromyelitis Optica. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0088.

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Neuromyelitis optica (NMO), or Devic’s disease is an inflammatory disorder of the central nervous system that preferentially affects the optic nerves and spinal cord. Initially considered a variant of multiple sclerosis (MS), NMO is now clearly recognized to have distinct clinical, radiographic, and pathologic characteristics. Historically, the diagnosis of NMO required bilateral optic neuritis and transverse myelitis; however, the identification of a specific biomarker, NMO-IgG, an autoantibody against the aquaporin-4 (AQP4) water channel, has broadened NMO spectrum disease to include patients with diverse clinical and radiographic presentations. This chapter addresses the diagnosis, pathophysiology, and management of the disease.
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Book chapters on the topic "AQP8"

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Saparov, Sapar M., Ulrich Rothe, Mario J. Borgnia, Peter Agre, and Peter Pohl. "Volume Flux Across Red Cell AQP1 and E. Coli AQPZ Water Channel Proteins Reconstituted into Planar Lipid Bilayers." In Molecular Biology and Physiology of Water and Solute Transport, 41–48. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-1203-5_6.

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Bazzarelli, Fabio, and Lidietta Giorno. "Aquaporins (AQPs) or Water Channels." In Encyclopedia of Membranes, 110–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-44324-8_30.

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Bazzarelli, Fabio, and Lidietta Giorno. "Aquaporins (AQPs) or Water Channels." In Encyclopedia of Membranes, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-40872-4_30-1.

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Han, Jin Suk, Un Sil Jeon, Kwon Wook Joo, Ho Joon Chin, Woosung Huh, Jung Sang Lee, Gheun-Ho Kim, et al. "Oxytocin: One of the Factors for Regulating AQP2 Localization and Urinary AQP2 Excretion." In Molecular Biology and Physiology of Water and Solute Transport, 97–105. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-1203-5_14.

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Kaufman, Kenneth A., and Ryszard S. Michalski. "Learning from inconsistent and noisy data: The AQ18 approach." In Lecture Notes in Computer Science, 411–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/bfb0095128.

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Li, Chunling, Weidong Wang, SØren Nielsen, and JØrgen FrØkiær. "Dysregulation of AQP2 in Bilateral and Unilateral Ureteral Obstruction." In Molecular Biology and Physiology of Water and Solute Transport, 225–29. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-1203-5_31.

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Sougrat, Rachid, Maryse Morand, Catherine Gondran, Frédéric Bonté, Marc Dumas, and Jean-Marc Verbavatz. "Functional Expression of AQP3 in Human Epidermis and Keratinocyte Cell Cultures." In Molecular Biology and Physiology of Water and Solute Transport, 179–83. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-1203-5_25.

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Nicchia, Grazia P., Beatrice Nico, Laura M. A. Camassa, Maria G. Mola, Domenico Ribatti, David C. Spray, Alejandra Bosco, Maria Svelto, and Antonio Frigeri. "Responsive Astrocytic Endfeet: The Role of AQP4 in BBB Development and Functioning." In Blood-Brain Barriers, 209–36. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2007. http://dx.doi.org/10.1002/9783527611225.ch9.

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Zelenin, Sergey M., Eli Gunnarson, Tatyana Yu Alikina, Alexander A. Bondar, and Anita Aperia. "Identification of a New Form of AQP4 MRNA that is Developmentally Expressed in Brain." In Molecular Biology and Physiology of Water and Solute Transport, 185–93. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-1203-5_26.

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Taya, Keisuke, Salih Gulsen, Kenji Okuno, Ruth Prieto, Christina R. Marmarou, and Anthony Marmarou. "Modulation of AQP4 expression by the selective V1a receptor antagonist, SR49059, decreases trauma-induced brain edema." In Acta Neurochirurgica Supplements, 425–29. Vienna: Springer Vienna, 2008. http://dx.doi.org/10.1007/978-3-211-85578-2_83.

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Conference papers on the topic "AQP8"

1

Peng, Jinglin, Dongxiang Zhang, Jiannan Wang, and Jian Pei. "AQP++." In SIGMOD/PODS '18: International Conference on Management of Data. New York, NY, USA: ACM, 2018. http://dx.doi.org/10.1145/3183713.3183747.

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Geraghty, Jack, Jiazheng Li, Alessandro Ragano, and Andrew Hines. "AQP." In MMSys '22: 13th ACM Multimedia Systems Conference. New York, NY, USA: ACM, 2022. http://dx.doi.org/10.1145/3524273.3532885.

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Tent, Michiel. "Ravulizumab significantly reduced relapses in AQP4+ NMOSD." In ECTRIMS Congress 2022, edited by Hans-Peter Hartung. Baarn, the Netherlands: Medicom Medical Publishers, 2022. http://dx.doi.org/10.55788/761fbd52.

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Naumov, Denis, Dina Gassan, Olesya Kotova, Elizaveta Sheludko, Juliy Perelman, and Victor Kolosov. "Role of AQP5 polymorphisms in predisposition to asthma." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa2338.

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Reis Junior, Silvio dos, Natália Yumi Shirozu Soares Matias, Rodrigo Lorenzetti Serrano, Karla David Barbosa Rodrigues de Souza, Bruna Romagna Peterle, Lucas de Castro Barroti, Leonardo Afonso Costa, et al. "SJÖGREN’S SYNDROME PLUS SERUM ANTI-AQP4 NEUROMYELITIS OPTICA." In XXXIX Congresso Brasileiro de Reumatologia. Sociedade Brasileiro de Reumatologia, 2022. http://dx.doi.org/10.47660/cbr.2022.2077.

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Lopez-Campos, J., R. Sanchez Silva, L. Gomez Izquierdo, P. Cejudo, E. Marquez Martin, F. Ortega, J. Toledo Aral, E. Barrot, and M. Echevarria. "Overexpression of AQP1 in Lung Adenocarcinomas and Pleural Mesoendotheliomas." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2682.

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Samuelson, Gay, Burt Feuerstein, Anjan Misra, and Kevin Bennett. "Abstract 433: Role of AQP1 in invasion of GBM." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-433.

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Sanca, Viktor, and Anastasia Ailamaki. "Sampling-Based AQP in Modern Analytical Engines." In SIGMOD/PODS '22: International Conference on Management of Data. New York, NY, USA: ACM, 2022. http://dx.doi.org/10.1145/3533737.3535095.

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Azuma, Masaaki. "Epithelial and cellular mechanisms of aquaporins (AQPs) in lepidopteran caterpillar." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.92903.

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Sirimalle, Srinivas, Eric Chau, Landon S. King, and Venkataramana Sidhaye. "Effect Of Aquaporin 5 (AQP5) Alteration On Epithelial Barrier Function." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3524.

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