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Academic literature on the topic 'ATPase'

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Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "ATPase"

1

Martins, Samantha M., Christiane R. Torres, and Sérgio T. Ferreira. "Inhibition of the Ecto-ATPdiphosphohydrolase of Schistosoma mansoni by Thapsigargin." Bioscience Reports 20, no. 5 (October 1, 2000): 369–81. http://dx.doi.org/10.1023/a:1010330017583.

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ATPdiphosphohydrolases (ATPDases) are ubiquitous enzymes capable ofhydrolyzing nucleoside di- and triphosphates. Although a number ofpossible physiological roles have been proposed for ATPDases, detailedstudies on structure-function relationships have generally been hamperedby the lack of specific inhibitors of these enzymes. We have previouslycharacterized a Ca2+-activated ATPDase on the external surface ofthe tegument of Schistosoma mansoni, the etiologic agent of humanschistosomiasis. In the present work, we have examined the effectsof thapsigargin, a sesquiterpene lactone known as a high affinityinhibitor of sarco-endoplasmic reticulum calcium transport (SERCA)ATPase, on ATPDase activity. Whereas other lactones tested had littleor no inhibitory action, thapsigargin inhibited ATP hydrolysis by the ATPDase (Ki∼20 μM). Interestingly, hydrolysis of ADP was notinhibited by thapsigargin. The lack of inhibition of ATPase activityby orthovanadate, a specific inhibitor of P-type ATPases, and theinhibition of the Mg2+-stimulated ATP hydrolysis by thapsigarginruled out the possibility that the observed inhibition of the ATPDaseby thapsigargin could be due to the presence of contaminating SERCAATPases in our preparation. Kinetic analysis indicated that a singleactive site in the ATPDase is responsible for hydrolysis of both ATPand ADP. Thapsigargin caused changes in both Vmax and Km for ATP, indicating a mixed type of inhibition. Inhibition by thapsigarginwas little or not affected by changes in free Ca2+ or Mg2+concentrations. These results suggest that interaction of thapsigarginwith the S. mansoni ATPDase prevents binding of ATP or its hydrolysisat the active site, while ADP can still undergo catalysis.
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2

Zhao, Dayuan, and Naranjan S. Dhalla. "Influence of gramicidin S on cardiac membrane Ca2+/Mg2+ ATPase activities and contractile force development." Canadian Journal of Physiology and Pharmacology 67, no. 6 (June 1, 1989): 546–52. http://dx.doi.org/10.1139/y89-088.

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The effects of gramicidin S (GS), an antibiotic, on the rat heart membrane ATPases and contractile activity of the right ventricle strips were investigated. GS inhibited sarcolemmal Ca2+-stimulated ATPase (IC50 = 3 μM), Ca2+/Mg2+ ATPase which is activated by millimolar Ca2+ or Mg2+ (IC50 = 3.4 μM), and sarcoplasmic reticulum Ca2+-stimulated ATPase (IC50 = 6 μM). The type of inhibition for the sarcolemmal Ca2+/Mg2+ ATPase by GS was apparently uncompetitive, while that for Ca2+-stimulated ATPases in sarcolemma or sarcoplasmic reticulum was of mixed type. Other ATPases, including mitochondrial ATPase, sarcolemmal Na+–K+ ATPase, and myofibrillar ATPase, were not inhibited by this agent. GS also decreased the rat right ventricle maximum force development (half-maximal inhibitory concentration was 2–4 μM), maximum velocity of contraction, and maximum velocity of relaxation. The resting tension was increased by GS to over 200%. The contractile actions of GS were mostly irreversible upon washing the muscle 3 times over a 10-min period. Decreased Ca2+, Mg2+, Na+, K+ concentrations in the perfusate increased the effects of GS. These findings showed that GS was a potent inhibitor of divalent cation ATPases of heart sarcolemma and sarcoplasmic reticulum and it is suggested that these membrane effects may explain the cardiodepressant action of this agent.Key words: gramicidin S, rat heart sarcolemma, rat heart sarcoplasmic reticulum, Ca2+/Mg2+ ATPase, Ca2+-stimulated ATPase, rat heart contraction.
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Rawson, Shaun, Michael A. Harrison, and Stephen P. Muench. "Rotating with the brakes on and other unresolved features of the vacuolar ATPase." Biochemical Society Transactions 44, no. 3 (June 9, 2016): 851–55. http://dx.doi.org/10.1042/bst20160043.

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The rotary ATPase family comprises the ATP synthase (F-ATPase), vacuolar ATPase (V-ATPase) and archaeal ATPase (A-ATPase). These either predominantly utilize a proton gradient for ATP synthesis or use ATP to produce a proton gradient, driving secondary transport and acidifying organelles. With advances in EM has come a significant increase in our understanding of the rotary ATPase family. Following the sub nm resolution reconstructions of both the F- and V-ATPases, the secondary structure organization of the elusive subunit a has now been resolved, revealing a novel helical arrangement. Despite these significant developments in our understanding of the rotary ATPases, there are still a number of unresolved questions about the mechanism, regulation and overall architecture, which this mini-review aims to highlight and discuss.
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4

Russell, V. E., U. Klein, M. Reuveni, D. D. Spaeth, M. G. Wolfersberger, and W. R. Harvey. "Antibodies to mammalian and plant V-ATPases cross react with the V-ATPase of insect cation-transporting plasma membranes." Journal of Experimental Biology 166, no. 1 (May 1, 1992): 131–43. http://dx.doi.org/10.1242/jeb.166.1.131.

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In immunobiochemical blots, polyclonal antibodies against subunits of plant and mammalian vacuolar-type ATPases (V-ATPases) cross-react strongly with corresponding subunits of larval Manduca sexta midgut plasma membrane V-ATPase. Thus, rabbit antiserum against Kalanchoe daigremontiana tonoplast V-ATPase holoenzyme cross-reacts with the 67, 56, 40, 28 and 20 kDa subunits of midgut V-ATPase separated by SDS-PAGE. Antisera against bovine chromaffin granule 72 and 39 kDa V-ATPase subunits cross-react with the corresponding 67 and 43 kDa subunits of midgut V-ATPase. Antisera against the 57 kDa subunit of both beet root and oat root V-ATPase cross-react strongly with the midgut 56 kDa V-ATPase subunit. In immunocytochemical light micrographs, antiserum against the beet root 57 kDa V-ATPase subunit labels the goblet cell apical membrane of both posterior and anterior midgut in freeze-substituted and fixed sections. The plant antiserum also labels the apical brush-border plasma membrane of Malpighian tubules. The ability of antibodies against plant V-ATPase to label these insect membranes suggests a high sequence homology between V-ATPases from plants and insects. Both of the antibody-labelled insect membranes transport K+ and both membranes possess F1-like particles, portasomes, on their cytoplasmic surfaces. This immunolabelling by xenic V-ATPase antisera of two insect cation-transporting membranes suggests that the portasomes on these membranes may be V-ATPase particles, similar to those reported on V-ATPase-containing vacuolar membranes from various sources.
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5

Tadini-Buoninsegni, Francesco, Stine A. Mikkelsen, Louise S. Mogensen, Robert S. Molday, and Jens Peter Andersen. "Phosphatidylserine flipping by the P4-ATPase ATP8A2 is electrogenic." Proceedings of the National Academy of Sciences 116, no. 33 (August 1, 2019): 16332–37. http://dx.doi.org/10.1073/pnas.1910211116.

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Phospholipid flippases (P4-ATPases) utilize ATP to translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes, thus generating and maintaining transmembrane lipid asymmetry essential for a variety of cellular processes. P4-ATPases belong to the P-type ATPase protein family, which also encompasses the ion transporting P2-ATPases: Ca2+-ATPase, Na+,K+-ATPase, and H+,K+-ATPase. In comparison with the P2-ATPases, understanding of P4-ATPases is still very limited. The electrogenicity of P4-ATPases has not been explored, and it is not known whether lipid transfer between membrane bilayer leaflets can lead to displacement of charge across the membrane. A related question is whether P4-ATPases countertransport ions or other substrates in the opposite direction, similar to the P2-ATPases. Using an electrophysiological method based on solid supported membranes, we observed the generation of a transient electrical current by the mammalian P4-ATPase ATP8A2 in the presence of ATP and the negatively charged lipid substrate phosphatidylserine, whereas only a diminutive current was generated with the lipid substrate phosphatidylethanolamine, which carries no or little charge under the conditions of the measurement. The current transient seen with phosphatidylserine was abolished by the mutation E198Q, which blocks dephosphorylation. Likewise, mutation I364M, which causes the neurological disorder cerebellar ataxia, mental retardation, and disequilibrium (CAMRQ) syndrome, strongly interfered with the electrogenic lipid translocation. It is concluded that the electrogenicity is associated with a step in the ATPase reaction cycle directly involved in translocation of the lipid. These measurements also showed that no charged substrate is being countertransported, thereby distinguishing the P4-ATPase from P2-ATPases.
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6

Parra, Karlett J., Chun-Yuan Chan, and Jun Chen. "Saccharomyces cerevisiae Vacuolar H+-ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals." Eukaryotic Cell 13, no. 6 (April 4, 2014): 706–14. http://dx.doi.org/10.1128/ec.00050-14.

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ABSTRACTVacuolar H+-ATPases (V-ATPases) are highly conserved ATP-driven proton pumps responsible for acidification of intracellular compartments. V-ATPase proton transport energizes secondary transport systems and is essential for lysosomal/vacuolar and endosomal functions. These dynamic molecular motors are composed of multiple subunits regulated in part by reversible disassembly, which reversibly inactivates them. Reversible disassembly is intertwined with glycolysis, the RAS/cyclic AMP (cAMP)/protein kinase A (PKA) pathway, and phosphoinositides, but the mechanisms involved are elusive. The atomic- and pseudo-atomic-resolution structures of the V-ATPases are shedding light on the molecular dynamics that regulate V-ATPase assembly. Although all eukaryotic V-ATPases may be built with an inherent capacity to reversibly disassemble, not all do so. V-ATPase subunit isoforms and their interactions with membrane lipids and a V-ATPase-exclusive chaperone influence V-ATPase assembly. This minireview reports on the mechanisms governing reversible disassembly in the yeastSaccharomyces cerevisiae, keeping in perspective our present understanding of the V-ATPase architecture and its alignment with the cellular processes and signals involved.
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7

Dane, Michaela, Kerstin Steinert, Kordula Esser, Susanne Bickel-Sandkötter, and Francisco Rodriguez-Valera. "Properties Of The Plasma Membrane Atpases Of The Halophilic Archaebacteria Haloferax Mediterranei And Haloferax Volcanii." Zeitschrift für Naturforschung C 47, no. 11-12 (December 1, 1992): 835–44. http://dx.doi.org/10.1515/znc-1992-11-1209.

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Both, Haloferax mediterranei and Haloferax volcanii membranes contain ATPases which are capable of hydrolyzing ATP in presence of Mg2+ or Mn2+. The ATPases require high concentrations of NaCl, a pH value of 9, and high temperatures up to 60 °C. Free manganese ions inhibited the enzyme activity of either ATPase. The ATPases of Hf. mediterranei and Hf. volcanii, respectively, show different sensitivities to inhibitors of ATP hydrolysis. ATP hydrolysis of isolated Hf. mediterranei ATPase was inhibited by NaN3, which was reported to be specific for F-ATPases, by nitrate and N-ethylmaleimide (NEM), which are specific inhibitors of V-ATPases. ATP hydrolysis of Haloferax mediterranei membranes was not inhibited by DCCD , but [14C]DCCD was bound to a 14 kDa peptide of the isolated, partially purified enzyme. Furthermore, the ATPase was inactivated by preincubation with 7-chloro-4-nitrobenzofurazan (NBD-Cl). The ATPase activity of Hf. volcanii membranes was inhibited by NEM but not by nitrate and NaN3. SDS gel electrophoresis of the partially purified enzyme of Haloferax mediterranei showed putative ATPase subunits of 53.5, 49, 42, 22, 21, 14, 12, and 7.5 kDa. Immunoblots showed cross reactivity between a 53 kDa peptide and anti-β (chloroplast F1), as well as between 53, 50 and 47 kDa peptides and an ATPase antibody of Methanosarcina barkeri. The results will be discussed in context with the placement of the archaebacterial ATPases (A-ATPases) between F- and V-ATPases
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8

Schütze, S., and H. D. Söling. "Does a calmodulin-dependent Ca2+-regulated Mg2+-dependent ATPase contribute to hepatic microsomal calcium uptake?" Biochemical Journal 243, no. 3 (May 1, 1987): 729–37. http://dx.doi.org/10.1042/bj2430729.

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Solubilization of microsomal proteins followed by calmodulin affinity chromatography resulted in the separation of two distinct Ca2+-Mg2+-ATPases (Ca2+-regulated Mg2+-dependent ATPases), one being insensitive to calmodulin (ATPase-1), the other being stimulated about 5-fold by calmodulin (ATPase-2). ATPase-2 accounts for only 8% of total microsomal Ca2+-Mg2+-ATPase-activity. ATPase-1 and -2 can also be distinguished by different pH optima, different sensitivity towards inhibition by vanadate and LaCl3, and different apparent Mr values of the phosphoenzyme intermediates (115,000 and 150,000 for ATPase-1 and ATPase-2 respectively). ATPase-1 from liver co-migrated with Ca2+-Mg2+-ATPase from rat skeletal-muscle sarcoplasmic reticulum, whereas ATPase-2 from liver co-migrated with calmodulin-dependent Ca2+-Mg2+-ATPase derived from rat skeletal-muscle sarcolemma. After separation of parenchymal and nonparenchymal liver cells, a calmodulin-dependent Ca2+-Mg2+-ATPase of Mr 150,000 was found only in the non-parenchymal cells. The kinetic parameters of ATPase-2 and the similarity of the apparent Mr of its phosphoenzyme intermediate to that of skeletal-muscle sarcolemma Ca2+-Mg2+-ATPase makes it likely that the calmodulin-sensitive Ca2+-Mg2+-ATPase found in rat liver microsomal fractions reflects a contamination with plasma membranes (possibly from non-parenchymal cells) rather than a true location in the endoplasmic reticulum of parenchymal liver cells.
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9

Missiaen, L., F. Wuytack, H. De Smedt, M. Vrolix, and R. Casteels. "AlF4- reversibly inhibits ‘P’-type cation-transport ATPases, possibly by interacting with the phosphate-binding site of the ATPase." Biochemical Journal 253, no. 3 (August 1, 1988): 827–33. http://dx.doi.org/10.1042/bj2530827.

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The only known cellular action of AlF4- is to stimulate the G-proteins. The aim of the present work is to demonstrate that AlF4- also inhibits ‘P’-type cation-transport ATPases. NaF plus AlCl3 completely and reversibly inhibits the activity of the purified (Na+ + K+)-ATPase (Na+- and K+-activated ATPase) and of the purified plasmalemmal (Ca2+ + Mg2+)-ATPase (Ca2+-stimulated and Mg2+-dependent ATPase). It partially inhibits the activity of the sarcoplasmic-reticulum (Ca2+ + Mg2+)-ATPase, whereas it does not affect the mitochondrial H+-transporting ATPase. The inhibitory substances are neither F- nor Al3+ but rather fluoroaluminate complexes. Because AlF4- still inhibits the ATPase in the presence of guanosine 5′-[beta-thio]diphosphate, and because guanosine 5′-[beta gamma-imido]triphosphate does not inhibit the ATPase, it is unlikely that the inhibition could be due to the activation of an unknown G-protein. The time course of inhibition and the concentrations of NaF and AlCl3 required for this inhibition differ for the different ATPases. AlF4- inhibits the (Na+ + K+)-ATPase and the plasmalemmal (Ca2+ + Mg2+)-ATPase noncompetitively with respect to ATP and to their respective cationic substrates, Na+ and Ca2+. AlF4- probably binds to the phosphate-binding site of the ATPase, as the Ki for inhibition of the (Na+ + K+)-ATPase and of the plasmalemmal (Ca2+ + Mg2+)-ATPase is shifted in the presence of respectively 5 and 50 mM-Pi to higher concentrations of NaF. Moreover, AlF4- inhibits the K+-activated p-nitrophenylphosphatase of the (Na+ + K+)-ATPase competitively with respect to p-nitrophenyl phosphate. This AlF4- –induced inhibition of ‘P’-type cation-transport ATPases warns us against explaining all the effects of AlF4- on intact cells by an activation of G-proteins.
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Imada, Katsumi, Tohru Minamino, Yumiko Uchida, Miki Kinoshita, and Keiichi Namba. "Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator." Proceedings of the National Academy of Sciences 113, no. 13 (March 16, 2016): 3633–38. http://dx.doi.org/10.1073/pnas.1524025113.

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FliI and FliJ form the FliI6FliJ ATPase complex of the bacterial flagellar export apparatus, a member of the type III secretion system. The FliI6FliJ complex is structurally similar to the α3β3γ complex of F1-ATPase. The FliH homodimer binds to FliI to connect the ATPase complex to the flagellar base, but the details are unknown. Here we report the structure of the homodimer of a C-terminal fragment of FliH (FliHC2) in complex with FliI. FliHC2shows an unusually asymmetric homodimeric structure that markedly resembles the peripheral stalk of the A/V-type ATPases. The FliHC2–FliI hexamer model reveals that the C-terminal domains of the FliI ATPase face the cell membrane in a way similar to the F/A/V-type ATPases. We discuss the mechanism of flagellar ATPase complex formation and a common origin shared by the type III secretion system and the F/A/V-type ATPases.
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Dissertations / Theses on the topic "ATPase"

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Recipon, Hervé. "Contribution à l'étude des gènes mitochondriaux codant pour des sous-unités du complexe ATP synthase dans un couple isogénique mâle-fertile mâle-stérile de tournesol (Hélianthus annuus L. )." Paris 11, 1989. http://www.theses.fr/1989PA112312.

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Une banque complète de l'ADN mitochondrial de la lignée HA89 B de tournesol a été construite dans le cosmide pHC79 au site SaII. En utilisant des sondes de mais codant pour les sous-unités α, 6 et 9 du complexe ATPase les gènes de tournesol correspondants ont été identifiés, isolés de la banque et cartographiés. Chez le tournesol, ces trois gènes ne sont présents qu'en une seule copie par génome mitochondrial et respectivement portés par les fragments de restriction SaII de (13,5 et 4,5), 13 et 7 kbp. Dans une première partie, nous avons comparé l'organisation moléculaire et la transcription, au niveau des fleurs, des gènes atpase α, 6 et 9 entre les lignées male-fertile (b) et male-stérile (a) de deux formes (cd et 62) d'un même couple isogénique HA 89. Les deux formes, CD et 62, sont identiques pour les caractères testés. Une recombinaison a été detectée de facon spécifique chez les lignées male-stériles en amont du gène codant pour l'atpase α. Les études de transcription réalisées révèlent, chez les lignées male-stériles, l'existence d'un profil d'ARN codant pour l'atpase α modifiés par rapport à ceux des lignées male-fertiles. Dans une deuxième partie, nous avons déterminé la séquence du gène codant pour l'atpase 9. Le gène de tournesol est actuellement le plus long gène atpase 9 trouvé chez les plantes supèrieures avec 252 nucléotides. La comparaison de cette séquence avec celles obtenues chez 17 autres organismes bactériens, de champignons (gènes nucléaires et mitochondriaux), et de plantes supèrieures (gènes chloroplastiques et mitochondriaux) nous a permis d'ériger un arbre phylogénétique des gènes atpase 9
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RIZZA, TERESA. "Caratterizzazione molecolare e funzionale di nuove mutazioni nelle encefalomiopatie mitocondriali." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2009. http://hdl.handle.net/2108/1004.

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Le encefalomiopatie mitocondriali rappresentano un gruppo di malattie estremamente eterogeneo ed in continua crescita sia per il sempre maggiore numero di fenotipi clinici descritti che per le conoscenze delle basi molecolari che le sottendono. Esse sono, collettivamente, il risultato di una diminuita capacità da parte dei mitocondri di soddisfare le richieste energetiche della cellula, a causa per lo più della ridotta attività enzimatica della catena respiratoria e la conseguente compromessa produzione di ATP intracellulare. In questo studio sono state indagate le conseguenze patogenetiche delle quattro mutazioni più frequentemente associate alla NARP/MILS - T8993G (L156R), T9176G (L217R), T8993C (L156P) e T9176C (L217P) - nel gene mitocondriale ATPasi 6, che codifica per una subunità del complesso V. La F1F0-ATP sintetasi (complesso V) è un enzima ubiquitario, presente nelle membrane dei batteri, dei cloroplasti e nella membrana interna dei mitocondri dove sintetizza ATP, l' ultimo step della fosforilazione ossidativa (Garcia, 2002). L' enzima è costituito da due subcomplessi F0 e F1. L' attività catalitica dell' enzima è localizzata nella porzione F1, che è estrinseca alla membrana ed utilizza il gradiente protonico per convertire ADP in ATP e viceversa; la subunità F0 si trova nella membrana mitocondriale interna e permette il flusso di protoni dallo spazio intermembrana alla matrice. Valutando la capacità duplicativa delle cellule in terreno standard, abbiamo potuto osservare che i fibroblasti di pazienti con la mutazione T->G, crescono con maggiore difficoltà rispetto a quelli con la mutazione T->C ed ai fibroblasti di controllo. Questa condizione si aggrava ulteriormente quando le cellule vengono sottoposte a stress, come la sostituzione del glucosio con il galattosio, un metabolita che entrando nella glicolisi più a valle, fornisce un numero minore di molecole di ATP e mette in evidenza i danni a carico della catena respiratoria. L' attività del complesso V, in termini di sintesi ed idrolisi, della catena respiratoria è stata valutata sui mitocondri ottenuti sia dai fibroblasti omoplasmici per le quattro mutazioni, che da cloni a diversa percentuale di mutazione. Tali indagini, effettuate mediante metodiche di tipo spettrofotometrico, hanno confermato la gravità delle mutazioni T->G rispetto alle varianti alleliche in entrambi i tipi cellulari. Lâ utilizzo inoltre di cloni a diversa percentuale di mutazione, ha consentito di determinare la soglia del fenotipo patologico per le mutazioni T->G. Inoltre abbiamo studiato lâ effetto dell' oligomicina e della sonicazione sull' attività dell' ATPasi nelle cellule primarie e nei cloni. I nostri risultati suggeriscono che le linee primarie con la mutazione L156R esibiscono una porzione F1 debolmente legata alla membrana poiché l' attività idrolitica non è pienamente sensibile alla oligomicina e poiché a 20â di sonicazione l' ATPasi diventa insensibile all'inibitore, probabilmente per il dovuto rilascio della porzione F1 dalla membrana.
Mitocondrial ATP synthase consists of two functional domains, F1 and F0. F1 protudes in to the matrix, is hydrophilic, and contains five subunits (3α,3β,γ,δ,ε) and inibibitor protein. F0 is hydrophobic, is embedded in the mitochondrial inner membrane, and contains subunits a, b, c, d, e, f, g, F6, OSCP and A6L. F1 is connected to F0 by a stalk that contains the subunits OSCP, F6, b, d. Subunits 6 and A6L are encoded by the mitochondrial genome whereas all of the other subunits are encoded by nuclear genes. ATP synthase deficiency can therefore be due to mutations of either nuclear or mitochondrial genes. Mutations in the ATPase 6 gene, characterized by a profound defect of the activity of the enzyme, are recognized as a cause of maternally-inherited LS. Leighâ s syndrome (LS) is a neurodegenerative disorder of infancy characterized by developmental delay, psychomotor regression, seizures, and symptons of brainstem dysfunction. In addition, biochemical defects in complex I, complex IV and PDHC underlie most of the LS patients. In order to know the different pathogenic mechanism leading to diverse clinical severity, of the mutations in the ATPase 6 gene, we compared cellular ATP production, cell growth and entity of cellular response upon use of metabolic stressors in primary cell cultures obtained from patients harboring either the T8993G, or T8993C, or T9176G, or T9176C and in cybrids clones obtained after fusion of each primary cell lines with Ï 0 cells. Arginine (â â Râ â ) mutations were associated with a much more severe phenotype than Proline ( P ) mutations, in terms of both biochemical activity and growth capacity. Also, a threshold effect in both R mutations appeared at 50% mutation load. Different mechanisms seemed to emerge for the two R mutations: the F1 seemed loosely bound to the membrane in the L156R mutant, whereas the L217R mutant induced low activity of complex V, possibly the result of a reduced rate of proton flow through the A6 channel.
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3

Fortier, Louis-Charles. "Cloning and characterization of the genes encoding Oenococcus oeni H+-ATPase and Cu+-ATPase." Thesis, McGill University, 2000. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=36927.

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Two enzymatic systems from the lactic acid bacterium Oenococcus oeni, isolated from wine, have been studied. The first one is the H+-ATPase for which the activity was characterized under various conditions of growth. The activity gradually increased by l.6 to 1.9-fold upon inoculation at pH 3.5. The H+-ATPase activity did not vary significantly in function of the growth rate or with and without malic acid. However, acidification of the medium in the absence of malic acid induced the activity by 1.5 to 2.2-fold depending on the initial pH. The partially cloned H+-ATPase genes shared high homologies with those from other bacterial F0F1-ATPases. A mRNA of about 7 kb was detected by Northern blot and its size suggests that the genetic organization of O. oeni atp operon is similar to most F0F 1-ATPases. Furthermore, the amount of atp mRNA was shown to increase in acidic conditions. O. oeni H +-ATPase activity was pH-inducible and regulation of the expression seems to occur at the level of mRNA synthesis. Thus, the results confirmed the proposed role of the H+-ATPase in acid tolerance in O. oeni.
The second system studied was a chromosome-encoded P-type ATPase (CopB) and its putative transcriptional regulator (CopR). The copB gene encodes a protein showing great similarities with other Cu2+-ATPases of the CPx-type family of heavy-metal ATPases like Enterococcus hirae copB. Another gene (copR) was found 250 bp upstream of copB and displays great similarities with proteins of the MecI/BlaI family of transcriptional regulators, including En. hirae CopY repressor. O. oeni was shown to be highly resistant to copper and growth occurred in up to 30 mM CuSO4. Northern blot analyses indicated that the amount of copB mRNA increased upon a 0.2 to 4.0 mM copper stress suggesting that expression of the enzyme might be regulated at the level of mRNA synthesis. Whether CopR is involved in this regulation remains to be determined, but the results suggest that copRB genes might be involved in copper resistance in O. oeni.
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4

Schempp, Christina Maria. "The V-ATPase inhibitor archazolid." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-168586.

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Fighting metastasis is a major challenge in cancer therapy and novel therapeutic targets and drugs are highly appreciated. Resistance of invasive cells to anoikis, a particular type of apoptosis induced by loss of cell-extracellular matrix (ECM) contact, is a major prerequisite for their metastatic spread. Inducing anoikis in metastatic cancer cells is therefore a promising therapeutic approach. The vacuolar H+-ATPase (V-ATPase), a proton pump located at the membrane of acidic organelles, has recently come to focus as an anti-metastatic cancer target. As V-ATPase inhibitors have shown to prevent invasion of tumor cells and are able to induce apoptosis we proposed that V-ATPase inhibition induces anoikis related pathways in invasive cancer cells. In this study the V-ATPase inhibitor archazolid A was used to investigate the mechanism of anoikis induction in various metastatic cancer cells (T24, MDA-MB-231, 4T1, 5637). Therefore, cells were forced to stay in a detached status to mimic loss of cell-ECM engagement following treatment with archazolid. Indeed, anoikis induction by archazolid was characterized by decreased expression of the caspase-8 inhibitor c-FLIP and caspase-8 activation, thus triggering the extrinsic apoptotic pathway. Interestingly, active integrin β1, which is known to play a major role in anoikis induction and resistance, is reduced on the cell surface of archazolid treated cells. Furthermore, a diminished phosphorylation of the integrin downstream target focal adhesion kinase could be demonstrated. The intrinsic apoptotic pathway was initiated by the pro-apoptotic protein BIM, increasing early after treatment. BIM activates cytochrome C release from the mitochondria consequently leading to cell death and is described as one major inducer of anoikis in non-malignant and anoikis sensitive cancer cells. Of note, we observed that archazolid also induces mechanisms opposing anoikis such as proteasomal degradation of BIM mediated by the pro-survival kinases ERK, c-Src and especially Akt at later time points. Moreover, induction of reactive oxygen species (ROS) influences BIM removal as well, as moderate levels of ROS have second messenger properties amplifying cell survival signals. Thus, to antagonize these anoikis escape strategies a combination of archazolid with proteasome or ROS inhibitors amplified cancer cell death synergistically. Most importantly, intravenous injection of archazolid treated 4T1-Luc2 mouse breast cancer cells in BALB/cByJRj mice resulted in reduced lung metastases in vivo. To summarize this work we propose archazolid as a very potent drug in inducing anoikis pathways in metastatic cancer cells even though having learned that detachment together with treatment triggers multiple resistance mechanisms opposing cell death. Hence, V-ATPase inhibition is not only an interesting option to reduce cancer metastasis but also to better understand anoikis resistance and to find choices to fight against it.
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Husain, I. "Studies on the mitochondrial Hsup(+)-ATPase complex and its interaction with the Hsup(+)-ATPase inhibitor protein." Thesis, University of Leeds, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355705.

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Lheureux, Karine. "Transduction mécano-chimique dans le muscle squelettique : étude comparative des complexes acto-myosine à l'état monomérique et filamenteux." Montpellier 1, 1995. http://www.theses.fr/1995MON1T015.

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Schneeberger, Anne. "Ionenbindung an die Na, K-ATPase." [S.l. : s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=959955968.

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Peinelt, Christine. "Kinetische Untersuchungen der SR-Ca-ATPase." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972881220.

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Liang, Man. "Na/K ATPase : signaling versus pumping." Toledo, Ohio : University of Toledo, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1173803261.

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Thesis (Ph.D.)--University of Toledo, 2006.
"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.
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Tian, Jiang. "Na/K-ATPase : a signaling receptor." Connect to Online Resource-OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1175177603.

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Thesis (Ph.D.)--University of Toledo, 2006.
"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.
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Books on the topic "ATPase"

1

L, Beaugé, Gadsby David C, and Garrahan Patricio J, eds. Na/K-ATPase and related transport ATPases: Structure, mechanism, and regulation. New York: New York Academy of Sciences, 1997.

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International Conference on the Na/K-ATPase and Related ATPases (9th 1999 Sapporo, Japan). Na/K-ATPase and related ATPases: Proceedings of the 9th International Conference on the Na/K-ATPase and Related ATPases, Sapporo, Japan, 18-23 August 1999. Edited by Kaya Shunji and Taniguchi Kazuya 1966-. Amsterdam: Elsevier, 2000.

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Chakraborti, Sajal, and Naranjan S. Dhalla, eds. Regulation of Membrane Na+-K+ ATPase. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-24750-2.

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Horisberger, Jean-Daniel. The Na,K-ATPase: Structure-function relationship. Austin: R.G. Landes, 1994.

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Kinoshita, Masahiro. Mechanism of Functional Expression of F1-ATPase. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-33-6232-1.

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Plasma membrane ATPase of plants and fungi. Boca Raton, Fla: CRC Press, 1985.

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Bowman, Sharen. Mitochondrial ATPase: Biochemical and molecular genetic analysis. [s.l.]: typescript, 1989.

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Connerton, Ian. Biochemical and molecular genetic studies on mitochondrial ATPase. [s.l.]: typescript, 1986.

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Bousselsela, Haoues. Studies on the sarcoplasmic reticulum-(Ca2plus plus Mg2plus)ATPase. Salford: University of Salford, 1992.

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Tentes, Ioannis. Studies of the sarcoplasmic reticulum (Ca2 plus plus Mg 2plus)-ATPase. Salford: University of Salford, 1987.

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Book chapters on the topic "ATPase"

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Abad, José Pascual. "ATPase." In Encyclopedia of Astrobiology, 123–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_135.

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Abad, José Pascual. "ATPase." In Encyclopedia of Astrobiology, 209–13. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_135.

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Abad, José Pascual. "ATPase." In Encyclopedia of Astrobiology, 1–7. Berlin, Heidelberg: Springer Berlin Heidelberg, 2022. http://dx.doi.org/10.1007/978-3-642-27833-4_135-3.

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Abad, José Pascual. "ATPase." In Encyclopedia of Astrobiology, 1–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_135-2.

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Abad, José Pascual. "ATPase." In Encyclopedia of Astrobiology, 282–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_135.

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Ishmukhametov, Robert. "ATPase: Overview." In Encyclopedia of Biophysics, 134–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_207.

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Arnold, R. "ATPase-Hemmer." In Verhandlungen der Deutschen Gesellschaft für Innere Medizin, 276–81. Munich: J.F. Bergmann-Verlag, 1988. http://dx.doi.org/10.1007/978-3-642-85461-3_55.

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Miki, Toru, Randa Hilal-Dandan, Laurence L. Brunton, Jean Sévigny, Kwok-On Lai, Nancy Y. Ip, Renping Zhou, et al. "Ecto-ATPase." In Encyclopedia of Signaling Molecules, 544. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100380.

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Penefsky, Harvey S. "Mitochondrial ATPase." In Advances in Enzymology - and Related Areas of Molecular Biology, 223–80. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122945.ch6.

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Kartner, Norbert, and Morris F. Manolson. "The Vacuolar Proton ATPase (V-ATPase): Regulation and Therapeutic Targeting." In Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 407–37. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_20.

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Conference papers on the topic "ATPase"

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Lestari, Silvia W., Aucky Hinting, Hamdani Lunardi, Debby Aditya, Dessy Noor Miati, and Meidika Dara Rizki. "Sperm Na+,K+-ATPase and dynein ATPase activity: A study of embryo development in in vitro fertilization (IVF)." In SECOND INTERNATIONAL CONFERENCE OF MATHEMATICS (SICME2019). Author(s), 2019. http://dx.doi.org/10.1063/1.5096752.

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Lee, Sangwook, Takatoki Yamamoto, Shigeki Segawa, Kimura Hiroshi, Hiroyuki Noji, and Teruo Fujii. "Development and Analysis of Multi-Laminar Chemical Delivery Platform Toward Single Molecular Application." In ASME 4th International Conference on Nanochannels, Microchannels, and Minichannels. ASMEDC, 2006. http://dx.doi.org/10.1115/icnmm2006-96164.

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The fluidic operations in microfluidic system such as chemical delivery, solution exchange, and chemical reactions by mixing are one of the most important technical issues to realize high-throughput and automated chemical / biochemical analysis with extremely small amount of species down to single molecular level. In order to realize such fluidic operations in micro and nano scale, we have been trying to develop a chemical delivery system to transport reagents to an arbitrary location in microchannel. In this work, we have developed and demonstrated a chemical delivery system in microchannel using precisely controlled multilaminar flow created by our previously developed multi-channel micropump embedded on the system. As a demonstration of the chemical delivery system, a single-molecule analysis of ATP dependent rotation of F1- ATPase was investigated. As a result, ATP dependent rotation of F1-ATPase was successfully investigated by addressing one of the streams, which are included or not included ATP, to the immobilized single-molecule of F1-ATPase.
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Shu, Yao-Gen, and Zhong-Can Ou-Yang. "microRNA detection with an active nanodevice FoF1-ATPase." In 9th International Conference on Biomedical Electronics and Devices. SCITEPRESS - Science and and Technology Publications, 2016. http://dx.doi.org/10.5220/0005692301660169.

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Li Xiaojuan, Chen Cunshe, and Lv Huitian. "The Research of Biosensor Building on F0F1-ATPase." In 2007 IEEE International Conference on Control and Automation. IEEE, 2007. http://dx.doi.org/10.1109/icca.2007.4376325.

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Obroucheva, N. V., S. V. Lityagina, and I. A. Sinkevich. "ROLE OF PLASMALEMMA H+-ATPASE IN SEED GERMINATION." In The All-Russian Scientific Conference with International Participation and Schools of Young Scientists "Mechanisms of resistance of plants and microorganisms to unfavorable environmental". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-319-8-571-574.

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Pogrebnaya, Alexandra F., Yury M. Romanovsky, and Alexander N. Tikhonov. "Electrostatic interactions in catalytic centers of F1-ATPase." In SPIE Proceedings, edited by Valery V. Tuchin. SPIE, 2003. http://dx.doi.org/10.1117/12.518627.

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Enouf, J., R. Breadux, N. Bourdeau, and S. Levy-Toledano. "EVIDENCE FOR TWO DIFFERENT Ca2+TRANSPORT SYSTEMS ASSOCIATED WITH PLASMA AND INTRACELLULAR HUMAN PLATELET MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644490.

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The regulation of Ca2+ concentration in different cells involves two Ca2+ pumps. The presence of such mechanisms in human platelets is still controverted. We then investigated this question by using plasma and intracellular membranes obtained after simultaneous isolation by centrifugation ca 40% sucrose from a mixed 100,000 g membrane fraction.The Ca2+ uptake by the different membrane vesicles has been studied. Both membrane fractions took up Ca2+ and the Ca2+ transport systems exhibited a high affinity towards Ca 2+.However, the two associated Ca2+ transport systems showed a different time course and exhibited different oxalate sensitivity. The plasma membranes are not permeable to potassium oxalate, while the Ca2+ uptake was stimulated by potassium oxalate in intracellular membranes.Two Ca2+ activated ATPase activities are associated with the isolated membrane fractions and appeared different for the following parameters : 1) a different time course of the two enzyme activities; 2)a similar apparent affinity towards Ca2+ (10−7 M), though inhibition of the Ca2+ ATPase activity was only observed in intracellular membranes at 10−6 M Ca2+ ; 3)a different pH dependence with a maximum at pH 7 for the enzyme of intracellular membranes and pH 8 for the enzyme of plasma membranes; 4)a 10 fold difference in the ATP requirement of the enzymes, thus the maximal response was obtained with 20 uM for the intracellular membrane enzyme and with 200 uM for the plasma membrane enzyme ; 5) a different affinity for various nucleotides as energy donors with a higher specificity of the plasma membrane enzyme towards ATP ; 6) a different vanadate inhibition-dose reponse which did not exceed 60% for the plasma enzyme while it reached 100% for the intracellular enzyme.Taken together, these studies agree with the possible role of both a plasma membrane and a dense tubular system Ca2+ -ATPases in the regulation of Ca2+ concentration in human platelets.
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Onken, Horst. "V-ATPase and Na+/K+-ATPase energize postprandial fluid absorption from the isolated midgut of female yellow fever mosquitoes (Aedes aegypti)." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.93236.

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"FoF1-ATPase STATOR REGULATION STUDIED WITH A RESONANCE MODEL." In International Conference on Biomedical Electronics and Devices. SciTePress - Science and and Technology Publications, 2012. http://dx.doi.org/10.5220/0003753401320137.

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Bolognani, Lorenzo, Michele Costato, and Marziale Milani. "Low-energy laser-ATPase enzyme interaction: theory and experiment." In Europto Biomedical Optics '93, edited by Kazuhiko Atsumi, Cornelius Borst, Frank W. Cross, Herbert J. Geschwind, Dieter Jocham, Jan Kvasnicka, Hans H. Scherer, Mario A. Trelles, and Eberhard Unsoeld. SPIE, 1994. http://dx.doi.org/10.1117/12.169116.

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Reports on the topic "ATPase"

1

Valdes, James J., Roy G. Thompson, Mia Paterno, Darrel E. Menking, and James P. Chambers. Bovine Brain Ca(++) Mg(++) ATPase: Partial Characterization. Fort Belvoir, VA: Defense Technical Information Center, March 1988. http://dx.doi.org/10.21236/ada196441.

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Nelson, Nathan, and Randy Schekman. Functional Biogenesis of V-ATPase in the Vacuolar System of Plants and Fungi. United States Department of Agriculture, September 1996. http://dx.doi.org/10.32747/1996.7574342.bard.

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The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It pumps protons into the vacuolar system of eukaryotic cells and provides the energy for numerous transport systems. Through our BARD grant we discovered a novel family of membrane chaperones that modulate the amount of membrane proteins. We also elucidated the mechanism by which assembly factors guide the membrane sector of V-ATPase from the endoplasmic reticulum to the Golgi apparatus. The major goal of the research was to understand the mechanism of action and biogenesis of V-ATPase in higher plants and fungi. The fundamental question of the extent of acidification in organelles of the vacuolar system was addressed by studying the V-ATPase of lemon fruit, constructing lemon cDNAs libraries and study their expression in mutant yeast cells. The biogenesis of the enzyme and its function in the Golgi apparatus was studied in yeast utilizing a gallery of secretory mutants available in our laboratories. One of the goals of this project is to determine biochemically and genetically how V-ATPase is assembled into the different membranes of a wide variety of organelles and what is the mechanism of its action.The results of this project advanced out knowledge along these lines.
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Carmeli, Chanoch, Lincoln Taiz, and Ezra Yagil. Structure, Function and REgulation of the H+ATPase in Plant Tonoplast Membrane. United States Department of Agriculture, June 1993. http://dx.doi.org/10.32747/1993.7603810.bard.

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Colton, Joel S., Sara C. Gilman, and Carol A. Colton. Effect of the Thiol-Oxidizing Agent, Diamide, on Cerebral Cortical Na(+) -K(+) ATPase. Fort Belvoir, VA: Defense Technical Information Center, September 1988. http://dx.doi.org/10.21236/ada205311.

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Taiz, L. Regulation of the synthesis and assembly of the plant vacuolar H sup + -ATPase. Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/5618759.

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Sweadner, Kathleen J. Creation of a Mouse with Stress-Induced Dystonia: Control of an ATPase Chaperone. Fort Belvoir, VA: Defense Technical Information Center, October 2012. http://dx.doi.org/10.21236/ada573942.

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Sweadner, Kathleen J. Creation of a Mouse with Stress-Induced Dystonia: Control of an ATPase Chaperone. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada583979.

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VanHouten, Joshua N. Does Increased Expression of the Plasma Membrane Calcium-ATPase Isoform 2 Confer Resistance to Apoptosis on Breast Cancer Cells? Fort Belvoir, VA: Defense Technical Information Center, September 2008. http://dx.doi.org/10.21236/ada493700.

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Taiz, L. Regulation of the synthesis and assembly of the plant vacuolar H{sup +}-ATPase. Progress report, [April 1, 1991--March 31, 1992]. Office of Scientific and Technical Information (OSTI), April 1992. http://dx.doi.org/10.2172/10135025.

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Prusky, Dov, Noel T. Keen, and Stanley Freeman. Elicitation of Preformed Antifungal Compounds by Non-Pathogenic Fungus Mutants and their Use for the Prevention of Postharvest Decay in Avocado Fruits. United States Department of Agriculture, January 1996. http://dx.doi.org/10.32747/1996.7570573.bard.

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C. gloeosporioides attacks unripe avocado fruits in the orchard. Germinated spores produce appressoria that germinate and breach the cuticle, but the resultant subcuticular hyphae become quiescent and do not develop further until fruit is harvested and ripens. Resistance of unripe avocado to attach by C. gloeosporioides is correlated with the presence of fungitoxic concentrations of the preformed antifungal compound, 1-acetoxy-2-hydroxy-4-oxoheneicosa-12, 15 diene in the pericarp of unripe fruits. The objective of this proposal was to study the signal transduction process by which elicitors induce resistance in avocado. It was found that abiotic elicitors, infection of avocado fruit with C. gloeosporioides or treatment of avocado cell suspension with cell-wall elicitor induced a significant production of reactive oxygen species (ROS). Ripe and unripe fruit tissue differ with regard to the ROS production. The unripe, resistant fruit are physiologically able to react and to produce high levels of ROS and increased activity of H+ATPase that can enhance the phenylpropanoid pathway ad regulate the levels of the antifungal compound-diene, inhibit fungal development, resulting in its quiescence. Interestingly, it was also found that growth regulators like cytokinin could do activation of the mechanism of resistance. Postharvest treatments of cytokinins strongly activated the phenylpropanoid pathway and induce resistance. We have developed non-pathogenic strains of C. gloeosporioides by Random Enzyme Mediated Integration and selected a hygromycin resistance, non-pathogenic strain Cg-142 out of 3500 transformants. This non-pathogenic isolate activates H+ATPase and induces resistance against Colletotrichum attack. As a basis for studying the importance of PL in pathogenicity, we have carried out heterologous expression of pel from C. gloeosporioides in the non-pathogenic C. magna and determine the significant increase in pathogenicity of the non-pathogenic strain. Based on these results we can state that pectate lyase is an important pathogenicity factor of C. gloeosporioides and found that fungal pathogenicity is affected not by pel but by PL secretion. Our results suggest that PH regulates the secretion of pectate lyase, and support its importance as a pathogenicity factor during the attack of avocado fruit by C. gloeosporioides . This implicates that if these findings are of universal importance in fungi, control of disease development could be done by regulation of secretion of pathogenicity factors.
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