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Journal articles on the topic 'Adenosine triphosphatase'

Author: Grafiati

Published: 4 June 2021

Last updated: 30 July 2024

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1

Dunn, P. P. J., A. R. Slabas, and A. L. Moore. "Characterization of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatases." Biochemical Journal 233, no. 3 (February 1, 1986): 839–44. http://dx.doi.org/10.1042/bj2330839.

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The catalytic properties of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatase have been analysed. The pH profile, effect of inhibitors, cold-stability and substrate specificity are characteristic of mitochondrial adenosine triphosphatases, although a high guanosine triphosphatase activity does appear to be restricted to plant mitochondrial adenosine triphosphatases. The kinetic properties of nucleoside 5′-triphosphate hydrolysis by membrane-bound and soluble enzymes have been studied by means of double-reciprocal plots. These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations. It is suggested that the differences in subunit composition of plant and mammalian adenosine triphosphatases reported previously [Dunn, Slabas & Moore (1985) Biochem. J. 225, 821-824] are structurally, rather than functionally, significant.

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2

Kristjansson, Hordur, Martha H. Sadler, and Lawrence I. Hochstein. "Halobacterial adenosine triphosphatases and the adenosine triphosphatase fromHalobacterium saccharovorum." FEMS Microbiology Letters 39, no. 1-2 (July 1986): 151–57. http://dx.doi.org/10.1111/j.1574-6968.1986.tb01856.x.

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3

Weiler, Elmar, Farhad Khalil-Manesh, and Harvey C. Gonick. "Effects of Lead and a Low-Molecular-Weight Endogenous Plasma Inhibitor on the Kinetics of Sodium—Potassium-Activated Adenosine Triphosphatase and Potassium-Activated p-Nitrophenylphosphatase." Clinical Science 79, no. 2 (August 1, 1990): 185–92. http://dx.doi.org/10.1042/cs0790185.

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1. Lead, ouabain and an endogenous plasma inhibitor were all found to be potent inhibitors of purified hog cerebral cortex sodium—potassium-activated adenosine triphosphatase and potassium-stimulated p-nitrophenylphosphatase. 2. The kinetic characteristics of inhibition of both enzymes by lead and the endogenous plasma inhibitor differed in several respects. For sodium—potassium-activated adenosine triphosphatase, lead and the endogenous plasma inhibitor were non-competitive inhibitors with respect to potassium; lead was competitive with respect to sodium, whereas the endogenous plasma inhibitor had no effect; lead was competitive with respect to magnesium adenosine triphosphate, whereas the endogenous plasma inhibitor was uncompetitive. For potassium-activated p-nitrophenylphosphatase, both lead and the endogenous plasma inhibitor were competitive with respect to potassium; lead showed a mixed type of inhibition with respect to p-nitrophenylphosphate, whereas the endogenous plasma inhibitor was non-competitive. 3. Lead and the endogenous plasma inhibitor exhibited synergistic inhibitory activity on sodium—potassium-activated adenosine triphosphatase. 4. These results suggest that lead could play a contributory role in the pathogenesis of essential hypertension via an additive inhibition of vascular smooth muscle sodium—potassium-activated adenosine triphosphatase.

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4

Liu, Gang, Si Qi Li, Ping Ping Hu, and Xiao Yong Tong. "Altered sarco(endo)plasmic reticulum calcium adenosine triphosphatase 2a content: Targets for heart failure therapy." Diabetes and Vascular Disease Research 15, no. 4 (May 15, 2018): 322–35. http://dx.doi.org/10.1177/1479164118774313.

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Sarco(endo)plasmic reticulum calcium adenosine triphosphatase is responsible for transporting cytosolic calcium into the sarcoplasmic reticulum and endoplasmic reticulum to maintain calcium homeostasis. Sarco(endo)plasmic reticulum calcium adenosine triphosphatase is the dominant isoform expressed in cardiac tissue, which is regulated by endogenous protein inhibitors, post-translational modifications, hormones as well as microRNAs. Dysfunction of sarco(endo)plasmic reticulum calcium adenosine triphosphatase is associated with heart failure, which makes sarco(endo)plasmic reticulum calcium adenosine triphosphatase a promising target for heart failure therapy. This review summarizes current approaches to ameliorate sarco(endo)plasmic reticulum calcium adenosine triphosphatase function and focuses on phospholamban, an endogenous inhibitor of sarco(endo)plasmic reticulum calcium adenosine triphosphatase, pharmacological tools and gene therapies.

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5

Ogata, Yumi, and Ikuo Kimura. "Adenosine triphosphate suppresses urea-induced denaturation of shark myosin calcium adenosine triphosphatase." Fisheries Science 85, no. 1 (October 22, 2018): 227–35. http://dx.doi.org/10.1007/s12562-018-1264-8.

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6

Pearson, J. D., S. B. Coade, and N. J. Cusack. "Characterization of ectonucleotidases on vascular smooth-muscle cells." Biochemical Journal 230, no. 2 (September 1, 1985): 503–7. http://dx.doi.org/10.1042/bj2300503.

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We compared the properties of the ectonucleotidases (nucleoside triphosphatase, EC 3.6.1.15; nucleoside diphosphatase, EC 3.6.1.6; 5′-nucleotidase, EC 3.1.3.5) in intact pig aortic smooth-muscle cells in culture with the properties that we previously investigated for ectonucleotidases of aortic endothelial cells [Cusack, Pearson & Gordon (1983) Biochem. J. 214, 975-981]. In experiments with nucleotide phosphorothioate diastereoisomers, stereoselective catabolism of adenosine 5′-[β-thio]triphosphate, but not of adenosine 5′-[α-thio]triphosphate, by the triphosphatase and stereoselective catabolism of adenosine 5′-[α-thio]diphosphate by the diphosphatase were found, as occurs in endothelial cells. In contrast with endothelial ecto-5′-nucleotidase, the smooth-muscle-cell enzyme catabolized adenosine 5′-monophosphorothioate (AMPS) to adenosine: the affinity of the enzyme for AMPS was greater than for AMP, and Vmax for AMPS was about one-sixth that for AMP. In both cell types AMPS was an apparently competitive inhibitor of AMP catabolism by 5′-nucleotidase. The relative rates of catabolism of nucleotide enantiomers in which the natural D-ribofuranosyl moiety is replaced by an L-ribofuranosyl moiety were similar to those in endothelial cells. No ectopyrophosphatase activity was detected in smooth-muscle cells, in contrast with endothelial cells, where modest activity is present.

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7

Antonelli, M. L., V. Carunchio, and M. Luciani. "Microcalorimetric study of the system adenosine-5′-triphosphate—sodium, potassium adenosine-5′-triphosphatase." Analytica Chimica Acta 252, no. 1-2 (November 1991): 17–22. http://dx.doi.org/10.1016/0003-2670(91)87191-9.

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8

Dey, Sandip, Chiranjit Biswas, and Jayati Sengupta. "The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes." Journal of Cell Biology 217, no. 7 (June 21, 2018): 2519–29. http://dx.doi.org/10.1083/jcb.201711131.

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The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Escherichia coli. Although HflX is recognized as a guanosine triphosphatase, several studies have shown that the N-terminal domain 1 of HflX is capable of hydrolyzing adenosine triphosphate (ATP), but the functional role of its adenosine triphosphatase (ATPase) activity remains unknown. We demonstrate that E. coli HflX possesses ATP-dependent RNA helicase activity and is capable of unwinding large subunit ribosomal RNA. A cryo–electron microscopy structure of the 50S–HflX complex in the presence of nonhydrolyzable analogues of ATP and guanosine triphosphate hints at a mode of action for the RNA helicase and suggests the linker helical domain may have a determinant role in RNA unwinding. Heat stress results in inactivation of the ribosome, and we show that HflX can restore heat-damaged ribosomes and improve cell survival.

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9

Vivien, Benoît, Yves Lecarpentier, Bruno Riou, and Catherine Coirault. "Halothane and Isoflurane Do Not Directly Interact with Cardiac Cross-bridge Function." Anesthesiology 102, no. 2 (February 1, 2005): 364–70. http://dx.doi.org/10.1097/00000542-200502000-00019.

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Background Halogenated anesthetics depress myocardial contractility by altering a number of specific mechanisms. These alterations include decreases in inward calcium current and sarcoplasmic reticulum function and reduced calcium myofilament sensitivity. However, the direct effects of volatile anesthetics on cross-bridge function have yet to be precisely determined. Methods Myosin monomers and actin filaments were isolated from fresh rat left ventricles and rabbit skeletal muscles, respectively. Halothane or isoflurane was added at concentrations equivalent to 1 and 2 minimum alveolar concentration (MAC). Motility of actin filaments over myosin was initiated by adding 2 mm adenosine triphosphate and was analyzed at 30 degrees C. Maximum actomyosin adenosine triphosphatase activity and the association constant of myosin for actin were determined from a double-reciprocal Lineweaver-Burk plot of the adenosine triphosphatase rate versus actin concentration. A known inhibitor of actomyosin function, 2,3-butanedione 2-monoxime (2 mm), was used in positive control experiments. Data are presented as mean +/- SD. Results Motility velocities driven by myosin were not significantly different between baseline and 1 and 2 MAC halothane (2.70 +/- 0.33, 2.72 +/- 0.36, and 2.70 +/- 0.40 microm/s, respectively). Similarly, motility velocities driven by myosin were not significantly different between baseline and 1 and 2 MAC isoflurane (2.73 +/- 0.33, 2.72 +/- 0.37, and 2.72 +/- 0.40 microm/s, respectively). Neither of the two halogenated anesthetics, at any concentration tested, significantly modified the maximum actomyosin adenosine triphosphatase activity or the association constant of myosin for actin as compared with baseline. 2,3-Butanedione 2-monoxime induced a drastic reduction in both motility velocity and maximum actomyosin adenosine triphosphatase activity. Conclusion These results indicate that isoflurane and halothane do not directly depress the mechanical or enzymatic properties of cross-bridges in the heart.

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10

Eiam-Ong, Somchai, Melvin E. Laski, and Neil A. Kurtzman. "Diseases of Renal Adenosine Triphosphatase." American Journal of the Medical Sciences 309, no. 1 (January 1995): 13–25. http://dx.doi.org/10.1097/00000441-199501000-00003.

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11

Kakinuma, Yoshimi, and Kazuei Igarashi. "Sodium-translocating adenosine triphosphatase inStreptococcus faecalis." Journal of Bioenergetics and Biomembranes 21, no. 6 (December 1989): 679–92. http://dx.doi.org/10.1007/bf00762686.

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12

Muñoz, E., M. R. J. Salton, M. H. Ng, and M. T. Schor. "Membrane Adenosine Triphosphatase of Micrococcus lysodeikticus." European Journal of Biochemistry 7, no. 4 (March 3, 2005): 490–501. http://dx.doi.org/10.1111/j.1432-1033.1969.tb19635.x.

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13

Campo-Aasen, Imelda, and Mauricio Goihman-Yahr. "Adenosine triphosphatase in yeast phaseParacoccidioides brasiliensis." Mycopathologia 111, no. 3 (September 1990): 169–72. http://dx.doi.org/10.1007/bf02282800.

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14

Ikeda, Mikiko, Rainer Schmid, and Dieter Oesterhelt. "A chloride-translocating adenosine triphosphatase in Acetabularia acetabulum. 1. Purification and characterization of a novel type of adenosine triphosphatase that differs from chloroplast F1 adenosine triphosphatase." Biochemistry 29, no. 8 (February 27, 1990): 2057–65. http://dx.doi.org/10.1021/bi00460a013.

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15

Vinel, Polina K., Valentina V. Tsareva, Pavel G. Baboshko, Anton I. Sinitskii, Artem S. Kozhevnikov, and Alexandr V. Grunin. "Platelet monoamine oxidase and erythrocyte adenosine triphosphatase as biomarkers of necrotizing enterocolitis." Russian Journal of Pediatric Surgery 28, no. 2 (May 30, 2024): 124–32. http://dx.doi.org/10.17816/ps670.

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BACKGROUND: The diagnostics of necrotizing enterocolitis is a complex and often ineffective issue. Biomarkers reflecting key links in the pathogenesis of the disease may serve as early predictors of development, progression, and severe course of necrotizing enterocolitis. AIM: To assess potentials of platelet monoamine oxidase activity and erythrocyte ATPase to predict the development of necrotizing enterocolitis in premature newborns. METHODS: The present study had two stages and included 28 children who were treated at the Chelyabinsk Regional Children’s Clinical Hospital from November 2021 to December 2022. At the first stage, premature newborns were examined; among them a group of newborns with necrotizing enterocolitis IIB–IIIA-B was identified. Venous blood was used for testings. At the second stage, specimens obtained from the intestine during surgical interventions in newborns with surgical pathology were examined additionally as well. RESULTS: Children with necrotizing enterocolitis showed a significant decrease in the specific activity of platelet monoamine oxidase which correlated with the activity of monoamine oxidase in gut specimens. The following changes were registered: decrease in the activity of magnesium adenosine triphosphatasein erythrocytes by 50–100% of the maximum enzyme activity in the control group; decrease of sodium-potassium adenosine triphosphatase activity y 4 times from the maximum values in the control group. There was also a significant increase in the activity of calcium adenosine triphosphatase activity in erythrocytes. CONCLUSION: The obtained data allow to suggest that platelet monoamine oxidase in preterm newborns may potentially serve as an indicator of tissue and organ immaturity, rather than a marker of inflammation and oxidative damage. Changes in erythrocyte adenosine triphosphatase activity in preterm infants with surgical stages of necrotizing enterocolitis indicate a hypoxic hypoenergetic state, accompanied by high concentrations of intracellular calcium. The obtained data are promising for developing new methods for diagnosis/prognosis of necrotizing enterocolitis in newborns.

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16

Fernandez-Belda, Francisco, and Giuseppe Inesi. "Transmembrane gradient and ligand-induced mechanisms of adenosine 5'-triphosphate synthesis by sarcoplasmic reticulum adenosine triphosphatase." Biochemistry 25, no. 24 (December 1986): 8083–89. http://dx.doi.org/10.1021/bi00372a043.

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17

Datta, S. K., and Anjani Kumar. "Histochemical Studies of the Transition from Sapwood to Heartwood in Tectona Grandis." IAWA Journal 8, no. 4 (1987): 363–68. http://dx.doi.org/10.1163/22941932-90000456.

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Histochemistry of the wood of Tectona grandis Linn. f. (Verbenaceae) has been studied during the transition from sapwood to heartwood. Starch, lipids, proteins, nucleic acids, phenolics and the enzymes peroxidase, succinate dehydrogenase, acid phosphatase, adenosine triphosphatase and glucose-6-phosphatase show significant changes during the transition. Peroxidase and adenosine triphosphatase are highly active in the sapwood and moderate in the transition zone while succinate dehydrogenase, glucose-6-phosphatase and acid phosphatase are moderate throughout the sapwood.

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18

Winegrad, S., A. Weisberg, L. E. Lin, and G. McClellan. "Adrenergic regulation of myosin adenosine triphosphatase activity." Circulation Research 58, no. 1 (January 1986): 83–95. http://dx.doi.org/10.1161/01.res.58.1.83.

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19

USTA, JULNAR, HANA BARAKEH, HASHEM MAHFOUZ, and NADIM CORTAS. "Copper-Stimulated Adenosine Triphosphatase from Rat Liver." Annals of the New York Academy of Sciences 834, no. 1 Na/K-ATPase a (November 1997): 475–78. http://dx.doi.org/10.1111/j.1749-6632.1997.tb52305.x.

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20

Townsend, Michael C. "Hepatic Microsomal Adenosine Triphosphatase and Mitochondrial Function." Archives of Surgery 122, no. 7 (July 1, 1987): 813. http://dx.doi.org/10.1001/archsurg.1987.01400190079015.

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21

Hsu, An‐Fei, David Brauer, and Shu‐I Tu. "Adenosine diphosphatase and adenosine triphosphatase activities of maize tonoplast‐enriched vesicles." Journal of Plant Nutrition 18, no. 8 (August 1995): 1637–47. http://dx.doi.org/10.1080/01904169509365009.

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22

Chou, Ming-Lun, Chiung-Chih Chu, Lih-Jen Chen, Mitsuru Akita, and Hsou-min Li. "Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts." Journal of Cell Biology 175, no. 6 (December 11, 2006): 893–900. http://dx.doi.org/10.1083/jcb.200609172.

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Three components of the chloroplast protein translocon, Tic110, Hsp93 (ClpC), and Tic40, have been shown to be important for protein translocation across the inner envelope membrane into the stroma. We show the molecular interactions among these three components that facilitate processing and translocation of precursor proteins. Transit-peptide binding by Tic110 recruits Tic40 binding to Tic110, which in turn causes the release of transit peptides from Tic110, freeing the transit peptides for processing. The Tic40 C-terminal domain, which is homologous to the C terminus of cochaperones Sti1p/Hop and Hip but with no known function, stimulates adenosine triphosphate hydrolysis by Hsp93. Hsp93 dissociates from Tic40 in the presence of adenosine diphosphate, suggesting that Tic40 functions as an adenosine triphosphatase activation protein for Hsp93. Our data suggest that chloroplasts have evolved the Tic40 cochaperone to increase the efficiency of precursor processing and translocation.

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23

Kim, Yoori, Zhubing Shi, Hongshan Zhang, Ilya J. Finkelstein, and Hongtao Yu. "Human cohesin compacts DNA by loop extrusion." Science 366, no. 6471 (November 28, 2019): 1345–49. http://dx.doi.org/10.1126/science.aaz4475.

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Cohesin is a chromosome-bound, multisubunit adenosine triphosphatase complex. After loading onto chromosomes, it generates loops to regulate chromosome functions. It has been suggested that cohesin organizes the genome through loop extrusion, but direct evidence is lacking. Here, we used single-molecule imaging to show that the recombinant human cohesin-NIPBL complex compacts both naked and nucleosome-bound DNA by extruding DNA loops. DNA compaction by cohesin requires adenosine triphosphate (ATP) hydrolysis and is force sensitive. This compaction is processive over tens of kilobases at an average rate of 0.5 kilobases per second. Compaction of double-tethered DNA suggests that a cohesin dimer extrudes DNA loops bidirectionally. Our results establish cohesin-NIPBL as an ATP-driven molecular machine capable of loop extrusion.

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24

Cardy, Jonathan D., and J. Anthony Firth. "Adenosine triphosphate-lead histochemical reactions in ependymal epithelia of murine brains do not represent calcium transport adenosine triphosphatase." Histochemical Journal 25, no. 4 (April 1993): 319–24. http://dx.doi.org/10.1007/bf00159124.

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25

De ANDRADE ROSA, IVONE, MARJOLLY BRIGIDO CARUSO, SILAS PESSINI RODRIGUES, REINALDO BARROS GERALDO, LUIZA WILGES KIST, MAURICIO REIS BOGO, LUIZ GONZAGA, et al. "New insights on the Golgi complex ofTritrichomonas foetus." Parasitology 141, no. 2 (October 18, 2013): 241–53. http://dx.doi.org/10.1017/s0031182013001455.

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SUMMARYTritrichomonas foetusis a protist that causes bovine trichomoniasis and presents a well-developed Golgi. There are very few studies concerning the Golgi in trichomonads. In this work, monoclonal antibodies were raised against Golgi ofT. foetusand used as a tool on morphologic and biochemical studies of this organelle. Among the antibodies produced, one was named mAb anti-Golgi 20.3, which recognized specifically the Golgi complex by fluorescence and electron microscopy. By immunoblotting this antibody recognized two proteins with 60 and 66 kDa that were identified as putative beta-tubulin and adenosine triphosphatase, respectively. The mAb 20.3 also recognized the Golgi complex of theTrichomonas vaginalis, a human parasite. In addition, the nucleotide coding sequences of these proteins were identified and included in theT. foetusdatabase, and the 3D structure of the proteins was predicted. In conclusion, this study indicated: (1) adenosine triphosphatase is present in the Golgi, (2) ATPase is conserved betweenT. foetusandT. vaginalis, (3) there is new information concerning the nucleic acid sequences and protein structures of adenosine triphosphatase and beta-tubulin fromT. foetusand (4) the mAb anti-Golgi 20.3 is a good Golgi marker and can be used in future studies.

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26

Brindha, E., and M. Rajasekapandiyan. "Preventive Effect of Phytic Acid on Isoproterenol-Induced Cardiotoxicity in Wistar Rats." International Journal of Biomedical Science 11, no. 1 (March 15, 2015): 35–41. http://dx.doi.org/10.59566/ijbs.2015.11035.

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This study was aimed to evaluate the preventive role of phytic acid on membrane bound enzymes such as sodium potassium- dependent adenosine triphosphatase (Na+ /K+ ATPase), calcium-dependent adenosine triphosphatase (Ca2+ ATPase) and magnesium- dependent adenosine triphosphatase (Mg2+ ATPase) and glycoproteins such as hexose, hexosamine, fucose and sialic acid in isoproterenol (ISO)-induced myocardial infarction (MI) in rats. Male albino Wistar rats were pretreated with phytic acid (25 and 50 mg/kg, respectively) for a period of 56 days. After the treatment period, ISO (85 mg/kg) was subcutaneously injected to rats at an interval of 24 h for 2 days. ISO-induced rats showed a significant decrease in the activity of Na+ /K+ ATPase and increase in the activities of Ca2+ and Mg2+ ATPase in the heart and a significant (P<0.05) increase in the levels of glycoproteins in serum and the heart were also observed in ISO-induced rats. Pretreatment with phytic acid for a period of 56 days exhibited a significant (P<0.05) effect and altered these biochemical parameters positively in ISO-induced rats. Thus, our study shows that phytic acid has cardioprotective role in ISO-induced MI in rats.

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27

Sun, Junzheng, Hongbin Chen, Yihui Chen, Mengshi Lin, Yen-Con Hung, Yuji Jiang, and Hetong Lin. "ε-Poly-l-Lysine Enhances Fruit Disease Resistance in Postharvest Longans (Dimocarpus longan Lour.) by Modulating Energy Status and ATPase Activity." Foods 11, no. 5 (March 7, 2022): 773. http://dx.doi.org/10.3390/foods11050773.

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ε-poly-l-lysine (ε-PL) holds a strong antibacterial property and is widely used for food preservation. However, the application of ε-PL to enhance fruit disease resistance in postharvest longans (Dimocarpus longan Lour.) has not been explored. The objective of this study was to explore the impact of ε-PL treatment on disease occurrence and energy metabolism of longans infected with Phomopsis longanae Chi (P. longanae). It was found that, in comparison with P. longanae-inoculated longans, ε-PL could decrease the fruit disease index and adenosine monophosphate (AMP) content, increase the amounts of adenosine triphosphate (ATP), adenosine diphosphate (ADP), and energy charge, and enhance the activities of adenosine triphosphatase (ATPase) (such as H+-, Mg2+-, and Ca2+-ATPase) in the mitochondria, protoplasm, and vacuole. The results suggest that the higher levels of ATPase activity and energy status played essential roles in disease resistance of postharvest longan fruit. Therefore, the ε-PL treatment can be used as a safe and efficient postharvest method to inhibit the disease occurrence of longan fruit during storage at room temperature.

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28

Yue, Yang, T. Lynne Blasius, Stephanie Zhang, Shashank Jariwala, Benjamin Walker, Barry J. Grant, Jared C. Cochran, and Kristen J. Verhey. "Altered chemomechanical coupling causes impaired motility of the kinesin-4 motors KIF27 and KIF7." Journal of Cell Biology 217, no. 4 (January 19, 2018): 1319–34. http://dx.doi.org/10.1083/jcb.201708179.

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Kinesin-4 motors play important roles in cell division, microtubule organization, and signaling. Understanding how motors perform their functions requires an understanding of their mechanochemical and motility properties. We demonstrate that KIF27 can influence microtubule dynamics, suggesting a conserved function in microtubule organization across the kinesin-4 family. However, kinesin-4 motors display dramatically different motility characteristics: KIF4 and KIF21 motors are fast and processive, KIF7 and its Drosophila melanogaster homologue Costal2 (Cos2) are immotile, and KIF27 is slow and processive. Neither KIF7 nor KIF27 can cooperate for fast processive transport when working in teams. The mechanistic basis of immotile KIF7 behavior arises from an inability to release adenosine diphosphate in response to microtubule binding, whereas slow processive KIF27 behavior arises from a slow adenosine triphosphatase rate and a high affinity for both adenosine triphosphate and microtubules. We suggest that evolutionarily selected sequence differences enable immotile KIF7 and Cos2 motors to function not as transporters but as microtubule-based tethers of signaling complexes.

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29

Hannon, James D., and Mark J. Cody. "Effects of Volatile Anesthetics on Sarcolemmal Calcium Transport and Sarcoplasmic Reticulum Calcium Content in Isolated Myocytes." Anesthesiology 96, no. 6 (June 1, 2002): 1457–64. http://dx.doi.org/10.1097/00000542-200206000-00027.

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Background The surface membrane Ca(2+)-adenosine triphosphatase and Na(+)-Ca(2+) exchanger transport Ca(2+) out of the ventricular myocyte, competing for cytosolic Ca(2+) with the Ca(2+)-adenosine triphosphatase located in the sarcoplasmic reticulum. In this study the authors examined the effects of halothane, isoflurane, and sevoflurane on Ca(2+) extrusion from the cell and sarcoplasmic reticulum Ca(2+) content. Methods Single myocytes from the right ventricular free wall of adult male ferret hearts were isolated, loaded with the acetoxymethyl ester of the fluorescent Ca(2+) indicator fluo-3, and electrically stimulated at 0.25 Hz to reach a steady state level of intracellular Ca(2+) stores. The effects of halothane, isoflurane, and sevoflurane (1 minimum alveolar concentration) on the peak and rate of decline of the Ca(2+) transient induced by 10 mm caffeine were examined. The peak was used as an index of sarcoplasmic reticulum Ca(2+) content, and the rate of decline was used to monitor Ca(2+) extrusion from the cell. Results During control conditions, halothane reduced the Ca(2+) content of the sarcoplasmic reticulum, isoflurane maintained it, and sevoflurane caused it to increase. Halothane did not affect Ca(2+) extrusion from the cell, but both isoflurane and sevoflurane inhibited it. When Na(+)-Ca(2+) exchange was inhibited by ionic substitution, isoflurane and sevoflurane still reduced the rate of Ca(2+) efflux from the cell. However, when the sarcolemmal Ca(2+)-adenosine triphosphatase was inhibited by carboxyeosin, isoflurane and sevoflurane had no effect on Ca(2+) efflux. Conclusions These results suggest that isoflurane and sevoflurane inhibit Ca(2+) transport from the cell via the sarcolemmal Ca(2+)-adenosine triphosphatase. This effect seems to counteract the decrease in Ca(2+) influx through sarcolemmal L-type Ca(2+) channels and maintains sarcoplasmic reticulum Ca(2+) stores.

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30

Gorelick, Fred S., Christine A. Shugrue, Thomas R. Kolodecik, and Edwin C. Thrower. "Vacuolar adenosine triphosphatase and pancreatic acinar cell function." Journal of Gastroenterology and Hepatology 21, s3 (October 2006): S18—S21. http://dx.doi.org/10.1111/j.1440-1746.2006.04576.x.

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31

ELIMBAN, V., K. DHALLA, P. SINGAL, V. PANAGIA, and N. DHALLS. "Myosin adenosine triphosphatase activities in hypertrophied pig heart*." Journal of Molecular and Cellular Cardiology 18 (1986): 24. http://dx.doi.org/10.1016/s0022-2828(86)80102-x.

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32

Pamnani, M. B., S. Chen, H. J. Bryant, J. F. Schooley, D. C. Eliades, C. M. Yuan, and F. J. Haddy. "Effects of three sodium-potassium adenosine triphosphatase inhibitors." Hypertension 18, no. 3 (September 1991): 316–24. http://dx.doi.org/10.1161/01.hyp.18.3.316.

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33

Amedei, Amedeo, Mathijs P. Bergman, Ben J. Appelmelk, Annalisa Azzurri, Marisa Benagiano, Carlo Tamburini, Ruurd van der Zee, et al. "Molecular Mimicry between Helicobacter pylori Antigens and H+,K+–Adenosine Triphosphatase in Human Gastric Autoimmunity." Journal of Experimental Medicine 198, no. 8 (October 20, 2003): 1147–56. http://dx.doi.org/10.1084/jem.20030530.

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Autoimmune gastritis and Helicobacter pylori–associated gastric atrophy develop through similar mechanisms involving the proton pump H+,K+–adenosine triphosphatase as autoantigen. Here, we report that H. pylori–infected patients with gastric autoimmunity harbor in vivo–activated gastric CD4+ T cells that recognize both H+,K+–adenosine triphosphatase and H. pylori antigens. We characterized the submolecular specificity of such gastric T cells and identified cross-reactive epitopes from nine H. pylori proteins. Cross-reactive H. pylori peptides induced T cell proliferation and expression of T helper type 1 functions. We suggest that in genetically susceptible individuals, H. pylori infection can activate cross-reactive gastric T cells leading to gastric autoimmunity via molecular mimicry.

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34

Adeoya, Abimbola S., Robert I. Norman, and Robert F. Bing. "Erythrocyte Membrane Calcium Adenosine 5′-Triphosphatase Activity in the Spontaneously Hypertensive Rat." Clinical Science 77, no. 4 (October 1, 1989): 395–400. http://dx.doi.org/10.1042/cs0770395.

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1. Ca2+-adenosine 5′-triphosphatase (Ca2+ −Mg2+ – ATPase) activity was studied simultaneously in calmodulin-deficient erythrocyte ghost membranes and inside-out vesicles (IOVs) from 12-week-old female spontaneously hypertensive rats (SHR) and their matched controls: [Wistar-Kyoto normotensive rats (WKY)], and in detergent extracts of ghost membranes. 2. Both adenosine 5′-triphosphate (ATP)-dependent Ca2+ uptake by IOVs and Ca2+-dependent ATP hydrolysis activity of ghost membranes were reduced significantly in the SHR compared with WKY, when either the calmodulin-independent or calmodulin-stimulated activities were compared. 3. The ratios between Ca2+ uptake and ATP hydrolysis activities in the SHR remained approximately 1.0, showing a proportional reduction in both activities. 4. No difference in affinity for calmodulin was observed between SHR and WKY. 5. No significant difference in Ca2+-dependent ATP hydrolysis activity was observed between SHR and WKY after detergent solubilization of erythrocyte ghost membranes. 6. These results suggest that the number of Ca2+-Mg2+-ATPase units are similar in SHR and WKY and that the reduced activity in the intact SHR membrane is due to altered membrane environment.

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35

Zheng, Ying-Ning, Cheng-Yi Xiong, Ying Zhuo, Ya-Qin Chai, Wen-Bin Liang, and Ruo Yuan. "A near-infrared light-controlled, ultrasensitive one-step photoelectrochemical detection of dual cell apoptosis indicators in living cancer cells." Chemical Communications 56, no. 60 (2020): 8488–91. http://dx.doi.org/10.1039/d0cc02996c.

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The proposed near-infrared (NIR) light-controlled, one-step photoelectrochemical (PEC) strategy could simultaneously detect cell apoptosis indicators, phosphatidylserine (Pho) and sodium potassium adenosine triphosphatase (Sat), on living cancer cells.

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36

Zhou, Xinqun, Jianhu Cheng, Jing Sun, Shuzhen Guo, Xuexia Guo, Quan Chen, Xiaomei Wang, Xuan Zhu, and Bangdi Liu. "Effect of Red Visible Lighting on Postharvest Ripening of Bananas via the Regulation of Energy Metabolism." Horticulturae 9, no. 7 (July 23, 2023): 840. http://dx.doi.org/10.3390/horticulturae9070840.

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The mechanism by which LED red light irradiation regulates postharvest banana ripening was evaluated in this study by the continuous irradiation of banana fruits at the mature-green stage. In this study, a self-developed LED banana fresh-keeping container lid was used to continuously irradiate the immature banana fruit. The light wavelength was 655.0 ± 1.0 nm, the light intensity was 800.0 ± 10.0 LX, and the height between the LED lamp and the fruit was 15.0 ± 0.5 cm. Bananas stored under dark conditions were used as the negative control group, and bananas stored under dark conditions after spraying with 500.0 mg/L ethephon diluent were used as the positive control group. Changes in physiological parameters related to postharvest banana ripening, such as the respiration rate, ethylene release, texture, color, carotenoid content, chlorophyll content, adenosine triphosphate content, and energy metabolism-related enzyme activities, were measured during 8 days of storage at 20.0 ± 0.1 °C to analyze the key factors determining postharvest banana ripening in response to red light. The red light-irradiated bananas had higher total color differences and higher rates of chlorophyll degradation and carotenoid synthesis than those of the ethephon-treated group during the storage period. Red light irradiation promoted banana fruit ripening and senescence mainly by promoting carotenoid synthesis, capturing absorbed light energy, accelerating energy metabolism, effectively enhancing the activities of the respiratory and energy metabolism-related enzymes H+ adenosine triphosphatase, Ca2+ adenosine triphosphatase, succinate dehydrogenase, cytochrome C oxidase, and malic enzyme, and promoting organic acid degradation. In conclusion, LED red light can be used as a new physical ripening technology for bananas, with a similar effect to that of traditional ethephon treatment.

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37

Okuno, Takashi, Takashi Ohgita, Tatsunori Sasa, Aoi Nonaka, Noriaki Funasaki, and Kentaro Kogure. "Fluorescence Polarization Analysis for Revealing Molecular Mechanism of Nucleotide-Dependent Phospholipid Membrane Binding of MinD Adenosine 5′-Triphosphate, Adenosine Triphosphatase." Biological & Pharmaceutical Bulletin 33, no. 10 (2010): 1746–50. http://dx.doi.org/10.1248/bpb.33.1746.

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38

Wang, Jui H., Jennifer Cesana, and Joe C. Wu. "Catalytic hydrolysis and synthesis of adenosine 5'-triphosphate by stereoisomers of covalently labeled F1-adenosine triphosphatase and reconstituted submitochondrial particles." Biochemistry 26, no. 17 (August 25, 1987): 5527–33. http://dx.doi.org/10.1021/bi00391a047.

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39

Stark, André, Tomas Aparisi, and Jan L. E. Ericsson. "Human Osteogenic Sarcoma: Fine Structural Localization of Adenosine Triphosphatase." Ultrastructural Pathology 10, no. 2 (January 1986): 145–55. http://dx.doi.org/10.3109/01913128609014591.

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40

Korge, Paavo. "Factors Limiting Adenosine Triphosphatase Function During High Intensity Exercise." Sports Medicine 20, no. 4 (October 1995): 215–25. http://dx.doi.org/10.2165/00007256-199520040-00002.

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41

Brown, R. E., R. I. Montgomery, P. I. Spach, and C. C. Cunningham. "Phospholipid association with the bovine cardiac mitochondrial adenosine triphosphatase." Biochemical Journal 225, no. 3 (February 1, 1985): 597–608. http://dx.doi.org/10.1042/bj2250597.

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The association of different phospholipids with a lipid-depleted oligomycin-sensitive ATPase from bovine cardiac mitochondria [Serrano, Kanner & Racker (1976) J. Biol. Chem. 251, 2453-2461] has been examined using three approaches. First, reconstitution of the ATPase with different synthetic diacyl phospholipids resulted in a 2-10-fold stimulation of ATPase specific activity depending upon the particular phospholipid employed. The phospholipid headgroup region displayed the following order of ATPase reactivation potential: dioleoylphosphatidylglycerol greater than dioleoylphosphatidic acid greater than dioleoylphosphatidylcholine. Furthermore, the ATPase showed higher levels of specific activity when reconstituted with dioleoyl phospholipid derivatives compared with dimyristoyl derivatives. Second, examination of the phospholipid remaining associated with the lipid-depleted ATPase upon purification showed that phosphatidylcholine, phosphatidylethanolamine, and diphosphatidylglycerol were present. No relative enrichment of any of these phospholipids (compared with their distribution in submitochondrial particles) was noted. Therefore, no preferential association between the ATPase and any one phospholipid could be found in the mitochondrial ATPase. Third, the sodium cholate-mediated phospholipid exchange procedure was employed for studying the phospholipid requirements of the ATPase. Replacement of about 50% of the mitochondrial phospholipid remaining with the lipid-depleted ATPase could be achieved utilizing either synthetic phosphatidic acid or phosphatidylcholine. Examination of the displaced mitochondrial phospholipid showed that phosphatidylcholine, phosphatidylethanolamine, and diphosphatidylglycerol were replaced with equal facility.

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42

Durlacher, Cameron T., Kevin Chow, Xiao-Wu Chen, Zhi-Xu He, Xueji Zhang, Tianxin Yang, and Shu-Feng Zhou. "Targeting Na+/K+-translocating adenosine triphosphatase in cancer treatment." Clinical and Experimental Pharmacology and Physiology 42, no. 5 (April 23, 2015): 427–43. http://dx.doi.org/10.1111/1440-1681.12385.

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43

Orlov, Sergei N., Victor V. Petrunyaka, Nikolai I. Pokudin, Yuri V. Kotelevtsev, Yuvenali V. Postnov, Jaroslav Kune??, and Josef Zicha. "Cation transport and adenosine triphosphatase activity in rat erythrocytes." Journal of Hypertension 9, no. 10 (October 1991): H45. http://dx.doi.org/10.1097/00004872-199110000-00012.

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44

Hisa, Yasuo, Leslie T. Malmgren, and Richard R. Gacek. "Actomyosin Adenosine Triphosphatase Activities of the CAT Infrahyoid Muscles." Annals of Otology, Rhinology & Laryngology 98, no. 3 (March 1989): 202–8. http://dx.doi.org/10.1177/000348948909800308.

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By use of actomyosin ATPase histochemistry, it was found that there were large differences among the three cat infrahyoid muscles (sternohyoid, sternothyroid, and thyrohyoid) with respect to their percentages of different muscle fiber types. It has been established that the individual activity patterns of the component motor units in each muscle drive the biochemical and physiologic differentiation of the muscle fibers associated with each motor unit. Therefore, the data obtained in the present investigation provide an indication of the characteristics of long-term use of each of the various types of motor units, as well as the associated differences in the physiologic capacities of the different motor unit types composing each of these infrahyoid muscles.

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45

Wendt, Christine H., Renuka Sharma, Howard Towle, Gregory Gick, and David H. Ingbar. "Hyperoxia Upregulated Na,K-Adenosine Triphosphatase β1 Gene Transcription." Chest 116 (July 1999): 87S—88S. http://dx.doi.org/10.1378/chest.116.suppl_1.87s.

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46

Asai, D. J., and L. Wilson. "A latent activity dynein-like cytoplasmic magnesium adenosine triphosphatase." Journal of Biological Chemistry 260, no. 2 (January 1985): 699–702. http://dx.doi.org/10.1016/s0021-9258(20)71152-x.

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47

Li, Jie, Gen He, Ueno Hiroshi, Wenzhe Liu, Hiroyuki Noji, Chuanmin Qi, and Xuefeng Guo. "Direct Measurement of Single-Molecule Adenosine Triphosphatase Hydrolysis Dynamics." ACS Nano 11, no. 12 (December 11, 2017): 12789–95. http://dx.doi.org/10.1021/acsnano.7b07639.

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48

Ker, Chen-Guo, and Pai-Ching Sheen. "Mitochondrial adenosine triphosphatase activity of hepatocytes in obstructive jaundice." Journal of Hepato-Biliary-Pancreatic Surgery 2, no. 4 (December 1995): 415–18. http://dx.doi.org/10.1007/bf02349260.

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49

Grahnquist, Lena, Tarja Ruuska, and Yigael Finkel. "Early Development of Human Gastric H,K-Adenosine Triphosphatase." Journal of Pediatric Gastroenterology and Nutrition 30, no. 5 (May 2000): 533–37. http://dx.doi.org/10.1097/00005176-200005000-00013.

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50

Cohen, Margo P., Henry Klepser, and Edith Shapiro. "Insulin stimulates renal glomerular sodium-potassium adenosine triphosphatase activity." Biochimica et Biophysica Acta (BBA) - Biomembranes 856, no. 1 (March 1986): 182–84. http://dx.doi.org/10.1016/0005-2736(86)90025-8.

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