Dissertations / Theses on the topic '(Na+,K+)-dependent ATPase'
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Hao, Jingping. "The electrical properties of Bufo marinus Na⁺, K⁺-ATPase." Ohio : Ohio University, 2009. http://www.ohiolink.edu/etd/view.cgi?ohiou1258151062.
Full textCheng, Sam Xian Jun. "Functional significance of phosphorylation of rat renal Na+,K+-ATPase by PKA and PKC /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-2971-8.
Full textNguyen, Khoa Thuy Diem. "Energy metabolism in the brain and rapid distribution of glutamate transporter GLAST in astrocytes." Thesis, The University of Sydney, 2008. http://hdl.handle.net/2123/3996.
Full textNguyen, Khoa Thuy Diem. "Energy metabolism in the brain and rapid distribution of glutamate transporter GLAST in astrocytes." University of Sydney, 2008. http://hdl.handle.net/2123/3996.
Full textGlutamate transporters play a role in removing extracellular excitatory neurotransmitter, L-glutamate into the cells. The rate of the uptake depends on the density of the transporters at the membrane. Some studies claimed that glutamate transporters could transit between the cytoplasm and the membrane on a time-scale of minutes. The present study examined the distribution of glutamate transporter GLAST predominantly expressed in rat cortical cultured astrocytes between the membrane and the cytoplasm by using deconvolution microscopy and then analyzing the images. The regulation of the distribution of GLAST was studied in the presence of glutamate transporter substrate (D-aspartate), purinergic receptor activators (α,β-methylene ATP, adenosine), neuroleptic drugs (clozapine, haloperidol), ammonia (hyperammonia) and Na+/K+-ATPase inhibitors (ouabain, digoxin and FCCP). It was demonstrated that the translocation of GLAST towards the plasma membrane was induced by D-aspartate, α,β-methylene ATP, adenosine, clozapine and ammonia (at 100 μM and very high concentrations of 10 mM). However, the inhibition of Na+/K+-ATPase activity had an opposite effect, resulting in redistribution of GLAST away from the membrane. It has previously been claimed that the membrane-cytoplasm trafficking of GLAST was regulated by phosphorylation catalysed by protein kinase C delta (PKC-delta). Involvement of this mechanism has, however, been put to doubt when rottlerin, a PKC-delta inhibitor, used to test the hypothesis showed to inhibit Na+/K+-ATPase-mediated uptake of Rb+, suggesting that rottlerin influenced the activity of Na+/K+-ATPase. As Na+/K+-ATPase converts ATP to energy and pumps Na+, K+ ions, thus helping to maintain normal electrochemical and ionic gradients across the cell membrane. Its inhibition also reduced D-aspartate transport and could impact on the cytoplasm-to-membrane traffic of GLAST molecules. Furthermore, rottlerin decreased the activity of Na+/K+-ATPase by acting as a mitochondrial inhibitor. The present study has focused on the inhibition of Na+/K+-ATPase activity by rottlerin, ouabain and digoxin in homogenates prepared from rat kidney and cultured astrocytes. The activity of Na+/K+-ATPase was measured by the absorption of inorganic phosphate product generated from the hydrolysis of ATP and the fluorescent transition of the dye RH421 induced by the movement of Na+/K+-ATPase. This approach has a potential to test whether the rottlerin effect on Na+/K+-ATPase is a direct inhibition of the enzyme activity. Rottlerin has been found to block the activity of Na+/K+-ATPase in a dose-dependent manner in both rat kidney and astrocyte homogenates. Therefore, rottlerin inhibited the activity of Na+/K+-ATPase directly in a cell-free preparation, thus strongly indicating that the effect was direct on the enzyme. In parallel experiments, ouabain and digoxin produced similar inhibitions of Na+/K+-ATPase activity in rat kidney while digoxin blocked the activity of Na+/K+-ATPase to a greater extent than ouabain in rat cortical cultured astrocytes. In a separate set of experiments, Na+/K+-ATPase in the astrocytic membrane was found to be unsaturated in E1(Na+)3 conformation in the presence of Na+ ions and this could explain the differences between the effects of digoxin and ouabain on the activity of Na+/K+-ATPase in rat astrocytes. In addition, it was found that at low concentrations of rottlerin, the activity of Na+/K+-ATPase was increased rather than inhibited. This effect was further investigated by studying rottlerin interactions with membrane lipids. The activity of Na+/K+-ATPase has been reported to be regulated by membrane lipids. The enzyme activity can be enhanced by increasing fluidity of the lipid membrane. I have, therefore, proposed that rottlerin binds to the membrane lipids and the effects of rottlerin on Na+/K+-ATPase are mediated by changes in the properties (fluidity) of the membrane. The hypothesis was tested by comparing rottlerin and a detergent, DOC (sodium deoxycholate), for their binding to the lipids by using a DMPC (1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine) monolayer technique. DOC has been shown to both increase and inhibit activity of Na+/K+-ATPase in a manner similar to that displayed by rottlerin. The effects of rottlerin and DOC on the DMPC monolayers were studied by measuring the surface pressure of DMPC monolayers and surface area per DMPC molecule. I established that both rottlerin and DOC decreased the surface pressure of DMPC monolayers and increased the surface area per DMPC molecule. This indicates that both rottlerin and DOC penetrated into the DMPC monolayers. If rottlerin can interact with the lipids, changes in fluidity of the lipid membrane cannot be ruled out and should be considered as a possible factor contributing to the effects of rottlerin on the activity of Na+/K+-ATPase. Overall, the study demonstrates that rottlerin is not only a PKC-delta inhibitor but can have additional effects, both on the enzyme activities (Na+/K+-ATPase) and/or on lipid-containing biological structures such as membranes. The findings have implication not only for studies where rottlerin was used as a supposedly specific PKC-delta inhibitor but also for mechanisms of its toxicity.
Kuznetsova, Irina [Verfasser]. "Inhibition of the influenza A virus-induced, tubulin-dependent apical mislocalization of the Na+,K+-ATPase in infected cells: Improving vectorial water transport and pulmonary edema clearance / Irina Kuznetsova." Gießen : Universitätsbibliothek, 2020. http://d-nb.info/1216143633/34.
Full textSchneeberger, Anne. "Ionenbindung an die Na, K-ATPase." [S.l. : s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=959955968.
Full textLiang, Man. "Na/K ATPase : signaling versus pumping." Toledo, Ohio : University of Toledo, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1173803261.
Full text"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences." Major advisor: Zi-Jian Xie. Includes abstract. Document formatted into pages: iii, 156 p. Title from title page of PDF document. Bibliography: pages 64-67, 97-100, 116-117, 125-155.
Tian, Jiang. "Na/K-ATPase : a signaling receptor." Connect to Online Resource-OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1175177603.
Full text"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences." Major advisor: Zi-Jian Xie. Includes abstract. Title from title page of PDF document. Bibliography: pages 64-70, 104-108, 121-158.
Aizman, Oleg. "Novel aspects of Na⁺,K⁺-ATPase /." Stockholm, 2002. http://diss.kib.ki.se/2002/91-7349-311-2.
Full textCarradus, Maria. "Structural studies of Na'+K'+-ATPase." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342323.
Full textMacGregor, Seona Elizabeth. "Na'+, K'+ - atpase inhibitors from microalgae." Thesis, University of Hertfordshire, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358520.
Full textRaccah, Denis. "Na/k atpase et neuropathie diabetique." Aix-Marseille 2, 1995. http://www.theses.fr/1995AIX20651.
Full textWang, Haojie. "Na+/K+-ATPase and Signal Transduction." University of Toledo Health Science Campus / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=mco1147300366.
Full textTian, Jiang. "Na/K-ATPase, A Signaling Receptor." University of Toledo Health Science Campus / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=mco1175177603.
Full textFABREGUETTES, CLAUDIE. "Na+ - k+ atpase et neuropathie diabetique." Aix-Marseille 2, 1994. http://www.theses.fr/1994AIX20807.
Full textLi, Juan. "Na, K-ATPase as a signaling transducer /." Stockholm : Karolinska institutet, 2007. http://diss.kib.ki.se/2007/978-91-7357-453-2/.
Full textYan, Yanling. "Na/K-ATPase Mediates Renal Sodium Handling." University of Toledo Health Science Campus / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=mco1341210741.
Full textDhir, Rajan. "Na+, K+-AtPase expression in high-K+ and low-K+ sheep red blood cells." Thesis, McGill University, 1989. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=55670.
Full textLi, Zhichuan. "Na/K-ATPase Signaling: from Bench to Bedside." University of Toledo Health Science Campus / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=mco1228945866.
Full textYe, Qiqi. "Regulation of Src by ¿¿¿¿1 Na/K-ATPase." University of Toledo Health Science Campus / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=mco1341538418.
Full textCui, Xiaoyu. "Regulation of Cellular Bioenergetics by Na/K-ATPase." University of Toledo Health Science Campus / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=mco1481294995657855.
Full textJaisser, Frédéric. "Relations structures fonctions de la na,k-atpase et de la h,k-atpase identifiees dans la vessie du crapaud bufo marinus." Paris 7, 1993. http://www.theses.fr/1993PA077352.
Full textHarvey, William John. "Proteolytic modification of the red cell Na,K-ATPase." Thesis, McGill University, 1985. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=72782.
Full textYoung, Elizabeth Ann. "Axonal Na/K ATPase: Localization, Loss, and Lessons Learned." Case Western Reserve University School of Graduate Studies / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=case1278699912.
Full textWang, Xiaoliang. "a1 Na/K-ATPase Integrator Function in Animal Physiology." University of Toledo Health Science Campus / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=mco1501068137400808.
Full textGouty-Dufayet, de La Tour Dominique. "Na,K-ATPase et diabète : facteurs génétiques et environnementaux." Aix-Marseille 2, 1998. http://theses.univ-amu.fr.lama.univ-amu.fr/1998AIX2666U.pdf.
Full textOliveira, Liliana Patrícia Alves. "Efeito do colesterol na atividade da (Na+/K+) ATPase." Master's thesis, Universidade de Aveiro, 2012. http://hdl.handle.net/10773/9807.
Full textO alumínio é o metal mais abundante na crosta terrestre sendo a sua exposição cada vez maior nas sociedades industrializadas. Numa sociedade cada vez mais envelhecida onde o número de casos de doenças neurodegenerativas tendem a aumentar, parece importante esclarecer os mecanismos celulares da neurotoxicidade do alumínio de forma a prevenir os seus efeitos. Estudos in vivo e in vitro indicam que a exposição a alumínio inibe a atividade da (Na+/K+)ATPase, proteína responsável pela manutenção e regulação dos gradientes eletroquímicos das membranas plasmáticas, e que a suscetibilidade à intoxicação por alumínio na dieta pode ser condicionada pelo colesterol, uma vez que, a exposição oral crónica a alumínio reduz a razão molar colesterol/fosfolípidos em sinaptossomas. Assim este trabalho, tem como objetivo esclarecer de que forma os diferentes níveis de colesterol afetam a inibição da (Na+/K+)ATPase sinaptossomal induzida pelo alumínio. Neste contexto foram utilizados como grupos de estudo, o controlo, em que não houve manipulação do teor de colesterol na membrana sinaptossomal; a incorporação, onde o teor de colesterol da membrana sinaptossomal foi aumentado; a depleção, em que o teor de colesterol da membrana sinaptossomal foi reduzido. As alterações do teor de colesterol da membrana dos sinaptossomas foram provocadas usando o composto metil-β-ciclodextrina e a atividade da (Na+/K+)ATPase sinaptossomal medida por colorimetria e por potenciometria. Neste trabalho, houve um aumento de 70% de colesterol sinaptossomal em relação ao controlo, e uma redução do teor de colesterol sinaptossomal em relação ao mesmo de 62%. A exposição in vitro dos sinaptossomas a AlCl3 300 μM inibiu a atividade da (Na+/K+)ATPase nos três grupos (controlo, incorporação e depleção). Nos sinaptossomas controlo onde o teor de colesterol foi de 183 ± 48 μg de colesterol/mg de proteína, a exposição in vitro a AlCl3 300 μM levou a uma inibição da atividade da (Na+/K+)ATPase de 76,39%, enquanto que, na presença de 279 ± 54 μg de colesterol/mg de proteína (incorporação de colesterol) o alumínio teve um efeito inibitório na atividade da (Na+/K+)ATPase de 72,88%. Por outro lado, para baixos níveis de colesterol (57 ± 16 μg de colesterol/mg de proteína) o alumínio teve um efeito inibitório na atividade da (Na+/K+)ATPase de 37,82%. Estes resultados, mostram que alterações do teor de colesterol nas membranas de sinaptossomas desempenham um importante papel na ação do alumínio sobre a (Na+/K+)ATPase. Assim, parece que baixos níveis de colesterol membranar atenuam o efeito inibitório do alumínio sobre a atividade da (Na+/K+)ATPase.
Aluminium is the most abundant metal in the earth's crust and its exposure increasing in industrialized societies. In an increasingly aging society where the number of cases of neurodegenerative diseases is increasing, it seems important to clarify the cellular mechanisms of the neurotoxicity of aluminium to prevent its effects. In vivo and in vitro studies indicate that exposure to aluminium inhibits the activity of (Na+/K+)ATPase, a protein responsible for the maintenance and regulation of the electrochemical gradients of the plasma membranes, and that susceptibility to intoxicaton by aluminium in the diet may be influenced by cholesterol, since chronic oral exposure to aluminium reduces the molar ratio of cholesterol/phospholipid in synaptosomes. Thus this work aims to clarify how the different levels of cholesterol affects the inhibition of synaptosomal (Na+/K+)ATPase induced by aluminium. In this context were used as the study groups, the control in which no manipulation of the content of cholesterol in synaptosomal membrane was made; incorporation, where the cholesterol content was increased synaptosomal membrane; depletion, wherein the cholesterol content of the membrane synaptosomal was reduced. The changes in membrane cholesterol content of synaptosomes were induced using the compound methyl-β-cyclodextrin and the activity of (Na+/K+) ATPase synaptosomal measured by colorimetry and potentiometry. In this study, there was a ~70% increase synaptosomal cholesterol relative to control, and reduced cholesterol content compared to the same synaptosomal ~62%. The in vitro exposure of synaptosomes to 300 μM AlCl3 inhibited the activity of (Na+/K+)ATPase in the three groups (control, incorporation and depletion). In control synaptosomes which the cholesterol content was 183 ± 48 μg cholesterol/mg protein, in vitro exposure to 300 μM AlCl3 led to an inhibition of the activity of (Na+/K+)ATPase of 76.39%, while in the presence of 279 ± 54 μg cholesterol/mg protein (incorporation of cholesterol) aluminium had an inhibitory effect on the activity of (Na+/K+)ATPase of 72.88%. Conversely, lowest cholesterol levels (57 ± 16 μg cholesterol/mg protein) aluminium had an inhibitory effect on the activity of (Na+/K+)ATPase of 37.82%. These results show that changes in cholesterol content of synaptosome membranes play an important role in the action of aluminium on the (Na+/K+)ATPase. Thus, it appears that low levels of membrane cholesterol attenuate the inhibitory effect of aluminium on the activity of (Na+/K+)ATPase.
Belusa, Roger. "Role of Na⁺, K⁺-ATPase in cell adhesion and cell volume regulation : mutagenesis of Na⁺, K⁺-ATPase and transfection in embryonic kidney cell line /." Stockholm, 2001. http://diss.kib.ki.se/2001/91-628-4874-7/.
Full textWard, Douglas. "Subunit structure and dual ATP effects of Na, K-ATPase." Thesis, University of Leicester, 1997. http://hdl.handle.net/2381/29915.
Full textCirri, Erica [Verfasser]. "Regulation of the Na,K-ATPase by FXYD1 / Erica Cirri." Konstanz : Bibliothek der Universität Konstanz, 2012. http://d-nb.info/103636819X/34.
Full textEmery, Aidan Mark. "The Na+/K+-ATPase of Anopheles stephensi and other insects." Thesis, Imperial College London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338838.
Full textWatts, Jude A. "Probing inhibitor binding sites in the gastric H/K-ATPase." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.393990.
Full textFloyd, Rachel Victoria. "The role of the Na, K-ATPase in the uterus." Thesis, University of Liverpool, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.420297.
Full textDong, Shuai. "The Na/K-ATPase/Caveolin-1 Interaction Regulates Cell Growth." University of Toledo Health Science Campus / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=mco1305223012.
Full textHlivko, Jonathan Thomas. "CHARACTERIZATION OF THE HUMAN Na+, K+-ATPASE ALPHA 4 ISOFORM." Miami University / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=miami1070628755.
Full textDuan, Qiming. "Cardiac Na/K-ATPase in Ischemia-Reperfusion Injury and Cardioprotection." University of Toledo Health Science Campus / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=mco1388151402.
Full textBussieres, Laurence. "Etude de la na-k-atpase renale par cytochimie quantitative." Paris 6, 1987. http://www.theses.fr/1987PA066289.
Full textBussieres, Laurence. "Etude de la Na-K-ATPase rénale par cytochimie quantitative." Grenoble : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37593757p.
Full textSpicer, Zachary. "THE ROLE OF H,K-ATPASE ISOFORMS IN GASTROINTESTINAL FUNCTION." Cincinnati, Ohio : University of Cincinnati, 2001. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=ucin991747072.
Full textGarcia, Alvaro. "Effect of posttranslational modification on the Na+, K+ ATPase kinetics." Thesis, The University of Sydney, 2014. http://hdl.handle.net/2123/13258.
Full textMohanty, Basant Kumar. "A cytochemical study of the distribution of Na'+, K'+-ATPase and Ca'2'+-ATPase in Xenopus laevis oocytes." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.281962.
Full textFirmino, Kelly Cristina Silva. "Processos osmorregulatórios no caranguejo Dilocarcinus pagei (Decapoda, Trichodactylidae), um antigo invasor da água doce: estudo das atividades (Na,K)-ATPase e V-ATPase branquiais." Universidade de São Paulo, 2009. http://www.teses.usp.br/teses/disponiveis/59/59138/tde-19082009-112806/.
Full textCrustacean arose in the sea but, during evolution, several species invaded lower salinity biotopes, reaching fresh water. The ability of crustaceans to successfully colonize the freshwater biotope depends on efficient mechanisms of hyperosmoregulation. In dilute media, crustaceans\' hemolymph osmolality and ionic composition reflect a balance between diffusive and urinary ion losses, and active ion capture through the gills. The gill (Na,K)- ATPase plays a pivotal role in Na+ capture from dilute environments and its kinetic characteristics are under investigation in recent years, although freshwater crab enzymes are poorly known. According to the most recent model, the apparent affinity for Na+ is the most variable kinetic parameter among gill enzymes from different species, and reflects the salinity of the species\' habitat. Thus, enzymes from species which are well adapted to freshwater usually present higher affinities for Na+. However, several recent results are incompatible with this model. On the other hand, it has been proposed that a V-ATPase is also involved in Na+ capture through the gills of hololimnetic crustaceans. This enzyme is almost completely unknown: its kinetic characteristics have not been studied yet and the relationship between the magnitude of its activity in the gills and the external medium salinity has not been established. This work aimed to characterize the (Na,K)-ATPase and V-ATPase from the posterior gill from the holimnetic crab Dilocarcinus pagei, considered an old fresh water colonizer. The (Na,K)- ATPase was characterized in animals maintained in fresh water, in order to establish a comparison of its kinetic properties with those of enzymes from other crab species that inhabit more saline media. This comparison may enhance our understanding of the biochemical adaptations associated to fresh water invasion. V-ATPase was characterized in animals kept in fresh water or exposed for varying time intervals to a medium of 21? salinity, or else acclimated for 10 days to media of different salinities (5-21?), aiming to establish a relationship between the enzyme specific activity in the gill tissue and the external salinity, and also investigate the mechanisms involved in enzyme activity regulation. The analysis of D. pagei gill microsomes in a continuous-density sucrose gradient revealed two protein peaks (25-35% and 35-45% sucrose), both showing K+-phosphatase, (Na,K)-ATPase and V-ATPase activities. These results indicate the presence of membrane fractions of distinct densities, both presenting the main ion pumps involved in Na+ capture. These membranes may originate from different places in the asymmetric posterior gill epithelium from this crab. Western compared to those reported for other freshwater animals, but similar to those found for estuarine/marine species. In contrast, the apparent affinity for K+ is 2.5 to 5-fold higher than those estimated for species that inhabit more saline media, and is apparently more related to the animals\' habitat than Na+ affinity. This possibility is consistent with the location of the (Na,K)-ATPase in crabs gill tissue, with K+ binding sites exposed to the hemolymph, allowing the direct modulation of enzyme activity by hemolymph K+ concentration. In contrast to data reported for other crab species, D. pagei gill (Na,K)-ATPase activity was not synergistically stimulated by K+ and NH4 +. However, the presence of one of these ions in the reaction medium results in an increase of about 3-fold in the apparent affinity of the enzyme for the other. This kinetic characteristic may be physiologically relevant to assure the transport of both ions, even in the presence of elevated concentrations of the other. Ouabain (3 mmol L-1) inhibited total ATPase activity (? 78%) through a biphasic curve (KI= 6.21 ± 0.32 mol L-1 and 101.2 ± 5.1 mol L-1) reinforcing previous results suggesting the presence of two isoenzymes in the microsomal preparations. A biphasic inhibition by orthovanadate (10 mol L-1) to about 15% residual activity was also observed. Optimal pH for D. pagei gill V-ATPase activity was 7.5. The modulation of enzyme activity of the animal kept in fresh water by ATP (V= 26.5 ± 1.3 U mg-1; K0.5= 3.9 ± 0.2 mmol L-1) and Mg2+ (V = 27.9 ± 1.4 U mg-1; K0.5 =0.80 ± 0.04 mmol L-1) occurred with positive cooperativity. The inhibition of the orthovanadate insensitive ATPase activity by bafilomycin A1 followed a monophasic curve (KI= 55.0 ± 2.8 nmol L-1). About 44 % of total ATPase activity was inhibited, corresponding to the V-ATPase. Dilocarcinus pagei gill V-ATPase activity substantially decreased in response to animal\'s exposure to 21? salinity. After 1h exposure, the activity diminished about 3-fold, reaching 4- fold after 24h, indicating the action of efficient short-time regulation mechanisms. Interestingly, V-ATPase activity was about 2-fold higher after 120h exposure, compared to 24h, although 2- fold lower compared to that estimated in fresh water. After 240h, the activity returned to the low levels observed for 1 and 24 h, indicating efficient long-term regulation. Besides the decrease in specific activity, it was also observed an increase in enzyme\'s apparent affinity for ATP (12 fold) and Mg2+ (3 fold) in response to animal\'s exposure to 21? salinity. Simultaneously, the enzyme\'s affinity for bafilomycin A1 increased up to 190-fold. We propose that, in response to salinity alteration, conformational changes take place both in V1 (in which the ATP and Mg2+ binding sites are located) and V0 (which contains the bafilomycin A1 bindind site), resulting in higher exposition of the inhibitor binding site and also higher affinity for Mg2+ and ATP. As the affinity increases are observed after just 1h exposure, this regulatory mechanism seems to be independent of protein expression and, thus, should not be related to the expression of distinct isoforms of some enzyme subunit. The lowering of gill V-ATPase activity in D. pagei in response to exposure to an elevated salinity is consistent with the mechanisms proposed for the role of this enzyme in active Na+ capture in hololimnetic crustaceans. After 10 days at 21, the gill microsomal fractions still show a little V-ATPase activity, possibly related to acid-base regulation and ammonia excretion processes. The results obtained for the acclimation of D. pagei for 10 days at salinities in the range 5 to 21? also showed a substantial decrease of V-ATPase activity in response to the increase in medium salinity. However, except for 5?, it was not observed an increase of enzyme\'s affinity for bafilomycin, suggesting that this alteration is limited to shorter periods of exposure. However, a significant increase in the enzyme\'s affinity for ATP and Mg2+ was also observed.
Erichsen, Susan. "Corticosteroid receptors and Na,K-ATPase in the developing mouse cochlea /." Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4526-8/.
Full textMoura, Elisabete Ferreira da Silva. "Expressão e Regulação da Na+ K+ - ATPase em Células Renais Envelhecidas." Doctoral thesis, Faculdade de Medicina da Universidade do Porto, 2010. http://hdl.handle.net/10216/55323.
Full textBarbey, Odile. "Caracterisation des isoformes de la na, k-atpase dans diverses pathologies." Aix-Marseille 2, 1997. http://www.theses.fr/1997AIX20655.
Full textChen, Ying. "Regulation of IP3 Receptor-Mediated Calcium Release by Na/K-ATPase." University of Toledo Health Science Campus / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=mco1203953158.
Full textMadan, Namrata. "Role of Different Isoforms of Na/K-ATPase in Signal Transduction." University of Toledo Health Science Campus / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=mco1418318054.
Full textFan, Xiaoming. "Regulation of Na/K-ATPase and its Role in Cardiac Disease." University of Toledo Health Science Campus / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=mco1544722291840285.
Full textMoura, Elisabete Ferreira da Silva. "Expressão e Regulação da Na+ K+ - ATPase em Células Renais Envelhecidas." Tese, Faculdade de Medicina da Universidade do Porto, 2010. http://hdl.handle.net/10216/55323.
Full textLiang, Pengfei. "The modified Synchronization Modulation technique revealed mechanisms of Na,K-ATPase." Scholar Commons, 2019. https://scholarcommons.usf.edu/etd/7846.
Full text