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Artículos de revistas sobre el tema "'-nucleotidase"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 20 de febrero de 2023

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1

Darvish, A., R. W. Pomerantz, P. G. Zografides, and P. J. Metting. "Contribution of cytosolic and membrane-bound 5'-nucleotidases to cardiac adenosine production." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 5 (November 1, 1996): H2162—H2167. http://dx.doi.org/10.1152/ajpheart.1996.271.5.h2162.

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The purpose of this study was to evaluate the relative contributions of AMP-specific cytosolic 5'-nucleotidase and ecto-5'-nucleotidase to cardiac adenosine production and its regulation by ADP and Mg2+. 5'-Nucleotidase activity was measured spectrophotometrically in the total homogenate, the 150,000-g supernatant fraction (cytosolic 5'-nucleotidase), and the membrane pellet fraction (ecto-5'-nucleotidase) of dog left ventricles. Increasing [MgCl2] over a range from 0 to 6 mmol/l increased 5'-nucleotidase activity in both the supernatant and pellet; only cytosolic 5'-nucleotidase exhibited an

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2

Stochaj, U., and H. G. Mannherz. "Affinity labelling of 5′-nucleotidases with 5′-p-fluorosulphonylbenzoyladenosine." Biochemical Journal 266, no. 2 (March 1, 1990): 447–51. http://dx.doi.org/10.1042/bj2660447.

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5′-Nucleotidases play an important role in the metabolism of nucleosides; for example, the hydrolysis of AMP generates adenosine, which can modulate a variety of cellular functions. We have used the membrane-bound AMPase from chicken gizzard and a secreted form of these enzymes to analyse their modification by the substrate analogue 5′-p-fluorosulphonylbenzoyladenosine (5′-FSBA). 5′-FSBA irreversibly inactivates 5′-nucleotidases by means of covalent modification of the proteins. ATP, a competitive inhibitor of chicken gizzard and snake-venom 5′-nucleotidase, abolished the inactivation by 5′-FS

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3

Headrick, J. P., and R. J. Willis. "5′-Nucleotidase activity and adenosine formation in stimulated, hypoxic and underperfused rat heart." Biochemical Journal 261, no. 2 (July 15, 1989): 541–50. http://dx.doi.org/10.1042/bj2610541.

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Changes in 5′-nucleotidase activity were calculated on the basis of alterations in ATP, ADP, phosphocreatine, Pi, Mg2+, IMP and AMP, determined by using 31P n.m.r. spectroscopy and h.p.l.c., during isoprenaline infusion, graded hypoxia and graded underperfusion in isolated rat heart. Calculated activity changes were compared with the total efflux of purines (adenosine + inosine + hypoxanthine) in order to assess the involvement of various 5′-nucleotidases in formation of adenosine. Purine efflux exhibited an exponential relation with cytosolic [AMP] during isoprenaline infusion and hypoxia (r

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4

Biswas, Nabanita, Marta Rodriguez-Garcia, Zheng Shen, Sarah G. Crist, Jack E. Bodwell, John V. Fahey, and Charles R. Wira. "Effects of Tenofovir on Cytokines and Nucleotidases in HIV-1 Target Cells and the Mucosal Tissue Environment in the Female Reproductive Tract." Antimicrobial Agents and Chemotherapy 58, no. 11 (August 18, 2014): 6444–53. http://dx.doi.org/10.1128/aac.03270-14.

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ABSTRACTTenofovir (TFV) is a reverse transcriptase inhibitor used in microbicide preexposure prophylaxis trials to prevent HIV infection. Recognizing that changes in cytokine/chemokine secretion and nucleotidase biological activity can influence female reproductive tract (FRT) immune protection against HIV infection, we tested the hypothesis that TFV regulates immune protection in the FRT. Epithelial cells, fibroblasts, CD4+T cells, and CD14+cells were isolated from the endometrium (Em), endocervix (Cx), and ectocervix (Ecx) following hysterectomy. The levels of proinflammatory cytokines (macr

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5

Skladanowski, A. C., G. B. Sala, and A. C. Newby. "Inhibition of IMP-specific cytosolic 5′-nucleotidase and adenosine formation in rat polymorphonuclear leucocytes by 5′-deoxy-5′-isobutylthio derivatives of adenosine and inosine." Biochemical Journal 262, no. 1 (August 15, 1989): 203–8. http://dx.doi.org/10.1042/bj2620203.

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1. The partially purified IMP-specific cytosolic 5′-nucleotidases from rat liver, polymorphonuclear leucocytes and heart were inhibited by 50% by 2-6 mM-5′-deoxy-5′-isobutylthioadenosine (IBTA) or 7-10 mM-5′-deoxy-5′-isobutylthioinosine (IBTI). IBTA and IBTI inhibited the rat liver and polymorphonuclear-leucocyte enzymes non-competitively. IBTA, but not IBTI, also inhibited the ecto-5′-nucleotidase of polymorphonuclear leucocytes. IBTI was, by contrast, a more potent inhibitor than IBTA of the AMP-specific soluble 5′-nucleotidase from pigeon heart. 2. During 2-deoxyglucose-induced ATP-cataboli

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6

Aslam, Nazia, Syeda Fatima, Sofia Khalid, Shahzad Hussain, Mughal Qayum, Khurram Afzal, and Muhammad Hassham Hassan Bin Asad. "Anti-5 ′ -Nucleotidases (5 ′ -ND) and Acetylcholinesterase (AChE) Activities of Medicinal Plants to Combat Echis carinatus Venom-Induced Toxicities." BioMed Research International 2021 (February 4, 2021): 1–10. http://dx.doi.org/10.1155/2021/6631042.

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Echis carinatus is one of the highly venomous snakes of Pakistan that is responsible for numerous cases of envenomation and deaths. In Pakistan, medicinal plants are commonly used traditionally for snakebite treatment because of their low cost and easy availability in comparison with antivenom. The current research is aimed at evaluating the inhibitory activity of Pakistani medicinal plants against acetylcholinesterase and 5 ′ -nucleotidases present in Echis carinatus venom. Acetylcholinesterase and 5 ′ -nucleotidase enzymatic assays were performed at different venom concentrations to check th

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7

Skladanowski, A. C., R. T. Smolenski, M. Tavenier, J. W. de Jong, M. H. Yacoub, and A. M. Seymour. "Soluble forms of 5'-nucleotidase in rat and human heart." American Journal of Physiology-Heart and Circulatory Physiology 270, no. 4 (April 1, 1996): H1493—H1500. http://dx.doi.org/10.1152/ajpheart.1996.270.4.h1493.

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Intracellular AMP hydrolysis probably produces sufficient adenosine in ischemic heart to exert physiological activity. Because data on adenosine-producing systems in human heart are scarce, we measured 1) formation of adenosine (catabolites) in ischemic human heart slices and 2) cytoplasmic 5'-nucleotidase activity in human left ventricle. We also measured the latter in rat ventricle and cardiomyocytes. During the first 5 min of incubation, adenosine production in slices (n = 5) equaled 26 +/- 10 (SD) nmol.min-1.g wet wt-1, and total AMP content was 0.81 +/- 0.46 mM. Cytoplasmic IMP-preferring

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8

Borowiec, Agnieszka, Katarzyna Lechward, Kinga Tkacz-Stachowska, and Andrzej C. Składanowski. "Adenosine as a metabolic regulator of tissue function: production of adenosine by cytoplasmic 5'-nucleotidases." Acta Biochimica Polonica 53, no. 2 (June 12, 2006): 269–78. http://dx.doi.org/10.18388/abp.2006_3339.

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Adenosine is a product of complete dephosphorylation of adenine nucleotides which takes place in various compartments of the cell. This nucleoside is a significant signal molecule engaged in regulation of physiology and modulation of the function of numerous cell types (i.e. neurons, platelets, neutrophils, mast cells and smooth muscle cells in bronchi and vasculature, myocytes etc.). As part a of purinergic signaling system, adenosine mediates neurotransmission, conduction, secretion, vasodilation, proliferation and cell death. Most of the effects of adenosine help to protect cells and tissue

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9

Piec, G., and M. Le Hir. "The soluble ‘low-Km’ 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase." Biochemical Journal 273, no. 2 (January 15, 1991): 409–13. http://dx.doi.org/10.1042/bj2730409.

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A soluble ‘low-Km’ 5′-nucleotidase has been described previously in several organs. It has been presumed to be of cytosolic origin and thus to play a role in the intracellular production of adenosine. Its catalytic properties are similar to those of the ecto-5′-nucleotidase of cell membranes. In the present study we compared molecular properties of the two enzymes in the kidney of the rat. The Mr of the main peak of soluble ‘low-Km‘ 5′-nucleotidase in gel-filtration chromatography was similar to that of the ecto-5′-nucleotidase solubilized by a phosphatidylinositol-specific phospholipase C fro

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10

Moses, G. C., J. F. Tuckerman, and A. R. Henderson. "Biological variance of cholinesterase and 5'-nucleotidase in serum of healthy persons." Clinical Chemistry 32, no. 1 (January 1, 1986): 175–77. http://dx.doi.org/10.1093/clinchem/32.1.175.

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Abstract We measured cholinesterase (EC 3.1.1.8) and 5'-nucleotidase (EC 3.1.3.5) activities in serum of 24 healthy laboratory staff during 12 months. Overall mean activities ranged from 5.3 to 13.4 kU/L for cholinesterase and 5.4 to 9.8 U/L for 5'-nucleotidase. Cholinesterase activity was significantly (p less than 0.01) higher for men than for women. 5'-Nucleotidase activity was significantly (p = 0.01) higher for subjects 40 years or older than for those younger than 40, but was not different with respect to sex or time of year. Average intra- and interindividual variances (SD2) were 0.38 a

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11

Chiarelli, Laurent R., Paola Bianchi, Elisa Fermo, Alessandro Galizzi, Paolo Iadarola, Andrea Mattevi, Alberto Zanella, and Giovanna Valentini. "Functional analysis of pyrimidine 5′-nucleotidase mutants causing nonspherocytic hemolytic anemia." Blood 105, no. 8 (April 15, 2005): 3340–45. http://dx.doi.org/10.1182/blood-2004-10-3895.

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Abstract Inherited pyrimidine 5′-nucleotidase type I (P5′N-1) deficiency is the third most common erythrocyte enzymopathy that causes hemolysis. Fourteen different mutations have been identified to date. We have investigated the molecular bases of the disease by studying the biochemical properties of the recombinant wild-type human enzyme and 4 variant proteins (D87V, L131P, N179S, and G230R) bearing missense mutations found in patients affected by nonspherocytic hemolytic anemia. P5′N-1 is a relatively stable protein and has essentially identical catalytic efficiency toward cytidine monophosp

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12

Olsson, Ray A. "CardiovascularEcto-5′-Nucleotidase." Circulation Research 95, no. 8 (October 15, 2004): 752–53. http://dx.doi.org/10.1161/01.res.0000146278.94064.4b.

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13

Panteghini, M. "Electrophoretic fractionation of 5'-nucleotidase." Clinical Chemistry 40, no. 2 (February 1, 1994): 190–96. http://dx.doi.org/10.1093/clinchem/40.2.190.

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Abstract Human isonucleotidases were separated by electrophoresis on a cellulose acetate membrane. Three 5'-nucleotidase forms, NTP1, NTP2, and NTP3, were resolved with this method and quantified by densitometry. The procedure was not only simple and rapid but also sufficiently precise (between-run CV &lt; 20%) and sensitive (detected nucleotidase fractions of &gt; 0.5 U/L). The effects of various treatments (heat, neuraminidase, glycosidases, proteases, lectins, and detergents) on the electrophoretic pattern of 5'-nucleotidase were studied. NTP1 (mean 12% of total 5'-nucleotidase, SD

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14

Harb, J., K. Meflah, and S. Bernard. "Structural differences between plasma-membrane 5′-nucleotidase in different cell types as evidenced by antibodies." Biochemical Journal 232, no. 3 (December 15, 1985): 859–62. http://dx.doi.org/10.1042/bj2320859.

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Antibodies raised against bovine 5′-nucleotidase inhibit this enzyme as well as 5′-nucleotidase from other bovine tissues, showing common structure(s) between these proteins. However, an IgG fraction directed against the glucidic moiety of the liver enzyme did not cross-react with the enzyme from lymphocyte or caudate nuclei, a clear indication that within the same species the 5′-nucleotidase differs from one cell type to another. In addition, immunoblots after electrophoresis show that the previous antibodies recognize 5′-nucleotidase from human, mouse or chicken origin. However, only human 5

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15

Bengis-Garber, Carmela. "Membrane-bound 5′-nucleotidase in marine luminous bacteria: biochemical and immunological properties." Canadian Journal of Microbiology 31, no. 6 (June 1, 1985): 543–48. http://dx.doi.org/10.1139/m85-101.

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A novel 5′-nucleotidase previously described in halophilic Vibrio costicola was detected in marine Vibrio and Photobacterium strains. The enzyme of marine bacteria was similar in its properties to the 5′-nucleotidase of Vibrio costicola; it was outwardly oriented in the cytoplasmic membrane and dephosphorylated nucleoside 5′-tri-, di-, and mono-phosphates to respective nucleosides before uptake. The enzyme in marine strains was immunologically cross-reactive with the antibody raised against the purified 5′-nucleotidase of Vibrio costicola. The uptake of the products of ATP hydrolysis was studi

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16

Darvish, A., and P. J. Metting. "Purification and regulation of an AMP-specific cytosolic 5'-nucleotidase from dog heart." American Journal of Physiology-Heart and Circulatory Physiology 264, no. 5 (May 1, 1993): H1528—H1534. http://dx.doi.org/10.1152/ajpheart.1993.264.5.h1528.

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The major enzyme responsible for adenosine production during myocardial hypoxia or ischemia is 5'-nucleotidase. We purified an AMP-specific 5'-nucleotidase to homogeneity from the 150,000-g supernatant of dog heart homogenate using phosphocellulose, DEAE-cellulose, and ADP-agarose affinity chromatography. Sodium dodecyl sulfate-poly-acrylamide gel electrophoresis of the purified enzyme yielded a single protein band of 43 kDa. The molecular mass of the holoenzyme, determined by gel filtration and sucrose density-gradient centrifugation, was approximately 166 kDa, suggesting a tetrameric structu

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17

Minamino, T., M. Kitakaze, T. Morioka, K. Node, K. Komamura, H. Takeda, M. Inoue, M. Hori, and T. Kamada. "Cardioprotection due to preconditioning correlates with increased ecto-5'-nucleotidase activity." American Journal of Physiology-Heart and Circulatory Physiology 270, no. 1 (January 1, 1996): H238—H244. http://dx.doi.org/10.1152/ajpheart.1996.270.1.h238.

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We investigated whether loss of myocardial protection after ischemic preconditioning (IP) is related to the extent of deactivation of activated ecto-5'-nucleotidase. The coronary arteries of mongrel dogs were occluded four times for 5 min separated by 5 min of reperfusion (IP). Five (IP1), 30 (IP2), 60 (IP3), and 120 min (IP4) after the fourth 5-min coronary occlusion or after a corresponding nonischemic period (control groups), the coronary arteries were occluded for 90 min followed by 6 h of reperfusion. The infarct size-limited effect of IP gradually disappeared in the IP2 (21.6 +/- 3.9%) a

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18

Loe, D. W., J. R. Glover, S. Head, and F. J. Sharom. "Solubilization, characterization, and detergent interactions of lymphocyte 5′-nucleotidase." Biochemistry and Cell Biology 67, no. 4-5 (April 1, 1989): 214–23. http://dx.doi.org/10.1139/o89-033.

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5′-Nucleotidase is a member of a recently identified class of membrane proteins that is anchored via a phosphatidylinositol-containing glycolipid. The enzyme was readily solubilized with full retention of catalytic activity by nonionic and anionic detergents such as alkylthioglucosides, deoxycholate, and 3-[(3-cholamidopropyl)-dimethylammonio]-1-propane-sulfonate (CHAPS), while the cationic detergent dodecyltrimethylammonium bromide (DTAB) caused loss of activity. 5′-Nucleotidase was released only at high detergent concentrations, suggesting that it is tightly associated with the membrane. DTA

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19

Le Hir, M., and U. C. Dubach. "An ATP-inhibited soluble 5'-nucleotidase of rat kidney." American Journal of Physiology-Renal Physiology 254, no. 2 (February 1, 1988): F191—F195. http://dx.doi.org/10.1152/ajprenal.1988.254.2.f191.

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Hydrolysis of 5'-AMP by 5'-nucleotidase is a possible source of adenosine in the kidney. A renal membrane-bound ecto-5'-nucleotidase has been previously described. The present study deals with the catalytic properties of a 5'-AMP phosphohydrolase partially purified from high-speed supernatants of rat kidney homogenates. It exhibits phosphatase activity toward 5'-AMP, 5'-IMP, and 5'-GMP, but not toward 2'- and 3'-AMP and corresponds therefore to a 5'-nucleotidase. The hydrolysis of 5'-AMP by the soluble 5'-nucleotidase requires divalent cations. Maximal activity is reached with 10 microM of eit

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20

Opdebeeck, Britt, Isabel R. Orriss, Ellen Neven, Patrick C. D’Haese, and Anja Verhulst. "Extracellular Nucleotides Regulate Arterial Calcification by Activating Both Independent and Dependent Purinergic Receptor Signaling Pathways." International Journal of Molecular Sciences 21, no. 20 (October 15, 2020): 7636. http://dx.doi.org/10.3390/ijms21207636.

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Arterial calcification, the deposition of calcium-phosphate crystals in the extracellular matrix, resembles physiological bone mineralization. It is well-known that extracellular nucleotides regulate bone homeostasis raising an emerging interest in the role of these molecules on arterial calcification. The purinergic independent pathway involves the enzymes ecto-nucleotide pyrophosphatase/phosphodiesterases (NPPs), ecto-nucleoside triphosphate diphosphohydrolases (NTPDases), 5′-nucleotidase and alkaline phosphatase. These regulate the production and breakdown of the calcification inhibitor—pyr

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21

Garcia-Gil, Mercedes, Marcella Camici, Simone Allegrini, Rossana Pesi, Edoardo Petrotto, and Maria Tozzi. "Emerging Role of Purine Metabolizing Enzymes in Brain Function and Tumors." International Journal of Molecular Sciences 19, no. 11 (November 14, 2018): 3598. http://dx.doi.org/10.3390/ijms19113598.

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The growing evidence of the involvement of purine compounds in signaling, of nucleotide imbalance in tumorigenesis, the discovery of purinosome and its regulation, cast new light on purine metabolism, indicating that well known biochemical pathways may still surprise. Adenosine deaminase is important not only to preserve functionality of immune system but also to ensure a correct development and function of central nervous system, probably because its activity regulates the extracellular concentration of adenosine and therefore its function in brain. A lot of work has been done on extracellula

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22

Le Hir, M. "A soluble 5′-nucleotidase in rat kidney. Stimulation by decavanadate." Biochemical Journal 273, no. 3 (February 1, 1991): 795–98. http://dx.doi.org/10.1042/bj2730795.

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A soluble 5′-nucleotidase was identified in rat kidney and partially purified. Compared with 5′-IMP, 5′-AMP was a poor substrate. The affinity for 5′-IMP was very low (S0.5 greater than 1 mM) in the absence of an activator, and it was much increased (S0.5 = 0.1 mM) by 2,3-bisphosphoglycerate (2,3-DPG). ATP and bisadenosyl tetraphosphate were further activators. The pH optimum was 6.3. Those properties suggest that the renal soluble 5′-nucleotidase is identical with the ‘high-Km’ 5′-nucleotidase purified previously from liver, heart and erythrocytes. Decavanadate (100 nM) increased the rate of

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23

Rees, David C., John A. Duley, and Anthony M. Marinaki. "Pyrimidine 5′ Nucleotidase Deficiency." British Journal of Haematology 120, no. 3 (February 2003): 375–83. http://dx.doi.org/10.1046/j.1365-2141.2003.03980.x.

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24

Rampazzo, Chiara, Cinzia Gazziola, Paola Ferraro, Lisa Gallinaro, Magnus Johansson, Peter Reichard, and Vera Bianchi. "Human high-Km5′-nucleotidase." European Journal of Biochemistry 261, no. 3 (May 1999): 689–97. http://dx.doi.org/10.1046/j.1432-1327.1999.00320.x.

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25

Itoh, Roichi. "IMP-GMP 5′-nucleotidase." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 105, no. 1 (May 1993): 13–19. http://dx.doi.org/10.1016/0305-0491(93)90163-y.

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26

Pesi, R., M. Turriani, S. Allegrini, C. Scolozzi, M. Camici, P. L. Ipata, and M. G. Tozzi. "The Bifunctional Cytosolic 5′-Nucleotidase: Regulation of the Phosphotransferase and Nucleotidase Activities." Archives of Biochemistry and Biophysics 312, no. 1 (July 1994): 75–80. http://dx.doi.org/10.1006/abbi.1994.1282.

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27

LEHTO, Marty T., and Frances J. SHAROM. "Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5′-nucleotidase by phospholipase C: catalytic activation and modulation by the lipid bilayer." Biochemical Journal 332, no. 1 (May 15, 1998): 101–9. http://dx.doi.org/10.1042/bj3320101.

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Many hydrolytic enzymes are attached to the extracellular face of the plasma membrane of eukaryotic cells by a glycosylphosphatidylinositol (GPI) anchor. Little is currently known about the consequences for enzyme function of anchor cleavage by phosphatidylinositol-specific phospholipase C. We have examined this question for the GPI-anchored protein 5´-nucleotidase (5´-ribonucleotide phosphohydrolase; EC 3.1.3.5), both in the native lymphocyte plasma membrane, and following purification and reconstitution into defined lipid bilayer vesicles, using Bacillus thuringiensis phosphatidylinositol-sp

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28

Baron, M. D., B. Pope, and J. P. Luzio. "The membrane topography of ecto-5′-nucleotidase in rat hepatocytes." Biochemical Journal 236, no. 2 (June 1, 1986): 495–502. http://dx.doi.org/10.1042/bj2360495.

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The transmembrane topography of the rat hepatocyte ectoenzyme 5′-nucleotidase was studied by the use of glycoprotein labelling and limited-proteolysis techniques. Comparison, by one-dimensional peptide mapping, of enzyme iodinated from outside the cell with that iodinated in the solubilized state showed that no additional iodination sites were revealed on solubilization. Incubation of newly synthesized enzyme in a microsomal membrane fraction with proteinase showed that the entire molecule of 5′-nucleotidase was protected from proteolysis. These data suggest that little, if any, of the 5′-nucl

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29

Stochaj, U., K. Flocke, W. Mathes, and H. G. Mannherz. "5′-Nucleotidases of chicken gizzard and human pancreatic adenocarcinoma cells are anchored to the plasma membrane via a phosphatidylinositol–glycan." Biochemical Journal 262, no. 1 (August 15, 1989): 33–40. http://dx.doi.org/10.1042/bj2620033.

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We have analysed the membrane anchorage of plasma-membrane 5′-nucleotidase, an ectoenzyme which can mediate binding to components of the extracellular matrix. We demonstrated that the purified enzyme obtained from chicken gizzard and a human pancreatic adenocarcinoma cell line were both completely transformed into a hydrophilic form by treatment with phospholipases C and D, cleaving glycosylphosphatidylinositol (GPI). These data indicate the presence of a glycolipid linker employed for membrane anchoring of the 5′-nucleotidase obtained from both sources. Incubation of plasma membranes under id

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30

Sharom, Frances J., Ian Lorimer, and Mary P. Lamb. "Reconstitution of lymphocyte 5′-nucleotidase in lipid bilayers: behaviour and interaction with concanavalin A." Canadian Journal of Biochemistry and Cell Biology 63, no. 10 (October 1, 1985): 1049–57. http://dx.doi.org/10.1139/o85-130.

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Pure 5′-nucleotidase (EC 3.1.3.5) and a membrane glycoprotein fraction (partially purified 5′-nucleotidase) were isolated from pig lymphocyte plasma membrane by affinity chromatography techniques, using the cationic detergent dodecyltrimethylammonium bromide as a solubilizing agent. A detergent-dialysis technique was used to reconstitute both partially purified and pure enzyme into large unilamellar phospholipid vesicles, where it remains functional. 5′-Nucleotidase is relatively unstable in detergent solutions, but is highly stable once reconstituted into lipid vesicles. Arrhenius plots of th

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31

Sharom, Frances J., Mary P. Lamb, Christine C. Kupsh, and Susan Head. "Inhibition of lymphocyte 5′-nucleotidase by lectins: effects of lectin specificityand cross-linking ability." Biochemistry and Cell Biology 66, no. 7 (July 1, 1988): 715–23. http://dx.doi.org/10.1139/o88-082.

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5′-Nucleotidase, an integral glycoprotein enzyme of the lymphocyte plasma membrane, is inhibited cooperatively by the lectin concanavalin A. Because divalent succinyl-concanavalin A is a poor enzyme inhibitor, both binding and lectin-induced cross-linking of 5′-nucleotidase may be necessary for inhibition. Succinyl-concanavalin A does not compete with concanavalin A for binding to the enzyme; however, maleyl-concanavalin A, another poor inhibitor, competes effectively with the parent lectin. Thus, maleyl-concanavalin A binds to the same site as concanavalin A but causes little inhibition, wher

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32

Vogel, M., H. J. Kowalewski, H. Zimmermann, A. Janetzko, R. U. Margolis, and H. E. Wollny. "Association of the HNK-1 epitope with 5′-nucleotidase from Torpedo marmorata (electric ray) electric organ." Biochemical Journal 278, no. 1 (August 15, 1991): 199–202. http://dx.doi.org/10.1042/bj2780199.

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5′-Nucleotidase isolated from the electric organ of the electric ray (Torpedo marmorata) has a molecular mass of 62 kDa and, on two-dimensional electrophoresis, separates into up to 13 isoforms within a pI range of 5.9-6.7. The N-terminal sequence data show a 71% identity over 17 amino acids with that previously published for the rat liver enzyme. All forms of 5′-nucleotidase are recognized by the HNK-1 monoclonal antibody. HNK-1 immunoreactivity is found at the surface of the Schwann-cell processes covering the synaptic terminals and in this respect corresponds to that of 5′-nucleotidase in t

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33

ENNES-VIDAL, V., R. O. S. CASTRO, C. BRITTO, H. BARRABIN, C. M. D'AVILA-LEVY, and O. C. MOREIRA. "CrATP interferes in the promastigote-macrophage interaction in Leishmania amazonensis infection." Parasitology 138, no. 8 (June 17, 2011): 960–68. http://dx.doi.org/10.1017/s0031182011000710.

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SUMMARYRecent have shown the relationship between Ecto-Nucleoside-Triphosphate-Diphosphohydrolases (Ecto-NTPDases or ecto-nucleotidases) and virulence and infectivity in trypanosomatids. In this work, the inhibition of the ecto-ATPase activities and promastigote growth of Leishmania amazonensis by CrATP was characterized. Furthermore, this compound was used to investigate the role of ecto-nucleotidase in the interaction of L. amazonensis with resident peritoneal macrophages obtained from BALB/c mice. CrATP partially inhibits the ecto-ATPase activity, presenting Ki values of 575·7±199·1 and 383

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McMILLEN, Lyle, Ifor R. BEACHAM, and Dennis M. BURNS. "Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites." Biochemical Journal 372, no. 2 (June 1, 2003): 625–30. http://dx.doi.org/10.1042/bj20021800.

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Escherichia coli 5′-nucleotidase activity is stimulated 30- to 50-fold in vitro by the addition of Co2+. Seven residues from conserved sequence motifs implicated in the catalytic and metal-ion-binding sites of E. coli 5′-nucleotidase (Asp41, His43, Asp84, His117, Glu118, His217 and His252) were selected for modification using site-directed mutagenesis of the cloned ushA gene. On the basis of comparative studies between the resultant mutant proteins and the wild-type enzyme, a model is proposed for E. coli 5′-nucleotidase in which a Co2+ ion may displace the Zn2+ ion at only one of two metal-io

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Cabezas, Alicia, Iralis López-Villamizar, María Jesús Costas, José Carlos Cameselle, and João Meireles Ribeiro. "Substrate Specificity of Chimeric Enzymes Formed by Interchange of the Catalytic and Specificity Domains of the 5′-Nucleotidase UshA and the 3′-Nucleotidase CpdB." Molecules 26, no. 8 (April 16, 2021): 2307. http://dx.doi.org/10.3390/molecules26082307.

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The 5′-nucleotidase UshA and the 3′-nucleotidase CpdB from Escherichia coli are broad-specificity phosphohydrolases with similar two-domain structures. Their N-terminal domains (UshA_Ndom and CpdB_Ndom) contain the catalytic site, and their C-terminal domains (UshA_Cdom and CpdB_Cdom) contain a substrate-binding site responsible for specificity. Both enzymes show only partial overlap in their substrate specificities. So, it was decided to investigate the catalytic behavior of chimeras bearing the UshA catalytic domain and the CpdB specificity domain, or vice versa. UshA_Ndom–CpdB_Cdom and CpdB

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Lilleker, J. B., A. Rietveld, S. R. Pye, K. Mariampillai, O. Benveniste, M. T. J. Peeters, J. A. L. Miller, et al. "Cytosolic 5′-nucleotidase 1A autoantibody profile and clinical characteristics in inclusion body myositis." Annals of the Rheumatic Diseases 76, no. 5 (January 25, 2017): 862–68. http://dx.doi.org/10.1136/annrheumdis-2016-210282.

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ObjectivesAutoantibodies directed against cytosolic 5′-nucleotidase 1A have been identified in many patients with inclusion body myositis. This retrospective study investigated the association between anticytosolic 5′-nucleotidase 1A antibody status and clinical, serological and histopathological features to explore the utility of this antibody to identify inclusion body myositis subgroups and to predict prognosis.Materials and methodsData from various European inclusion body myositis registries were pooled. Anticytosolic 5′-nucleotidase 1A status was determined by an established ELISA techniq

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Newby, A. C. "The pigeon heart 5′-nucleotidase responsible for ischaemia-induced adenosine formation." Biochemical Journal 253, no. 1 (July 1, 1988): 123–30. http://dx.doi.org/10.1042/bj2530123.

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1. A 5′-nucleotidase with a strong preference for AMP over IMP was characterized in homogenates and subcellular fractions of pigeon heart by using concentrations of ATP, ADP and AMP which mimicked those present in the ischaemic tissue. 2. The AMP-5′-nucleotidase had a neutral pH optimum and an apparent Km in the range 4.6-5.2 mM. It was stimulated by ATP plus ADP, and was inhibited by other nucleoside monophosphates, Pi and p-nitrophenyl phosphate, but not by ribose 5-phosphate or beta-glycerophosphate. The enzyme was not inhibited by [alpha beta-methylene] ADP or by 5′-deoxy-5′-isobutylthioad

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Sala-Newby, Graciela B., Nicola V. E. Freeman, Maria A. Curto, and Andrew C. Newby. "Metabolic and functional consequences of cytosolic 5′-nucleotidase-IA overexpression in neonatal rat cardiomyocytes." American Journal of Physiology-Heart and Circulatory Physiology 285, no. 3 (September 2003): H991—H998. http://dx.doi.org/10.1152/ajpheart.00053.2003.

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Adenosine exerts a spectrum of energy-preserving actions on the heart negative chronotropic effects. The pathways leading to adenosine formation have remained controversial. In particular, although cytosolic 5′-nucleotidases can catalyze adenosine formation in cardiomyocytes, their contribution to the actions of adenosine has not been documented previously. We recently cloned two closely related AMP-preferring cytosolic 5′-nucleotidases (cN-IA and -IB); the A form predominates in the heart. In this study, we overexpressed pigeon cN-IA in neonatal rat cardiomyocytes using an adenovirus. cN-IA o

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Bailyes, E. M., M. A. J. Ferguson, C. A. Colaco, and J. P. Luzio. "Inositol is a constituent of detergent-solubilized immunoaffinity-purified rat liver 5′-nucleotidase." Biochemical Journal 265, no. 3 (February 1, 1990): 907–9. http://dx.doi.org/10.1042/bj2650907.

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myo-Inositol analysis of detergent-solubilized immunoaffinity-purified rat liver 5′-nucleotidase showed the presence of 1 mol of myo-inositol/mol of enzyme monomer. This provides unequivocal evidence that the ectoenzyme 5′-nucleotidase is attached to liver membranes by a glycosyl-phosphatidylinositol lipid anchor.

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Spychala, J., V. Madrid-Marina, P. J. Nowak, and I. H. Fox. "AMP and IMP dephosphorylation by soluble high- and low-Km 5'-nucleotidases." American Journal of Physiology-Endocrinology and Metabolism 256, no. 3 (March 1, 1989): E386—E391. http://dx.doi.org/10.1152/ajpendo.1989.256.3.e386.

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Three distinct 5'-phosphomonoesterase activities were isolated from soluble fractions of human placenta, cultured human T and B lymphoblasts, and rat liver using 5'-AMP-sepharose 4B affinity chromatography. We define these activities as "low-Km" 5'-nucleotidase, "high-Km" 5'-nucleotidase, and nonspecific phosphatase. High-Km 5'-nucleotidase was eluted with 0.5 M NaCl, low-Km 5'-nucleotidase was eluted with 10 mM ADP, and nonspecific phosphatase was not retained on the column. We have found significant variability in the relative content of high- to low-Km activities in the tissues studied with

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ALLEGRINI, Simone, Rossana PESI, Maria Grazia TOZZI, J. Carol FIOL, B. Robert JOHNSON, and Staffan ERIKSSON. "Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli." Biochemical Journal 328, no. 2 (December 1, 1997): 483–87. http://dx.doi.org/10.1042/bj3280483.

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A cDNA coding for bovine cytosolic IMP/GMP-specific 5ʹ-nucleotidase endowed with phosphotransferase activity was cloned from calf thymus RNA, by 5ʹ and 3ʹ rapid amplification of cDNA ends protocols (5ʹ and 3ʹ RACE). Two products were isolated: a 5ʹ RACE 1.6 kb fragment and a 3ʹ RACE 2.0 kb fragment, with an overlapping region of 505 bp, leading to a total length of approx. 2951 bp. The similarity in the coding region to that of the human 5ʹ-nucleotidase cDNA sequence [Oka, Matsumoto, Hosokawa and Inoue (1994) Biochem. Biophys. Res. Commun. 205, 917-922], indirectly identified as a 5ʹ-nucleotid

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Walker, Jon P., John C. Barbato, and Lauren Gerard Koch. "Cardiac adenosine production in rat genetic models of low and high exercise capacity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 283, no. 1 (July 1, 2002): R168—R173. http://dx.doi.org/10.1152/ajpregu.00621.2001.

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We previously demonstrated that Copenhagen (COP) and DA inbred rat strains show a wide difference in a test for aerobic treadmill running that correlated positively with isolated cardiac function. The purpose of this study was to test adenosine production as a candidate intermediate phenotype that may explain part of the difference in running and cardiac performance in these genetic models for low and high aerobic capacity. Adenosine production was measured as the activity of soluble 5′-nucleotidase and membrane-bound ecto-5′-nucleotidase in the membrane pellet and supernatant fractions of lef

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Bontemps, F., G. Van den Berghe, and H. G. Hers. "5′-Nucleotidase activities in human erythrocytes. Identification of a purine 5′-nucleotidase stimulated by ATP and glycerate 2,3-bisphosphate." Biochemical Journal 250, no. 3 (March 15, 1988): 687–96. http://dx.doi.org/10.1042/bj2500687.

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A purine 5′-nucleotidase has been separated by DEAE-Trisacryl chromatography from other 5′-nucleotidase activities present in human haemolysates and purified approx. 30,000-fold by subsequent chromatography on Blue Sepharose. The enzyme has an Mr of around 250,000, displays hyperbolic substrate-saturation kinetics and hydrolyses preferentially IMP, GMP and their deoxy counterparts. It is much less active with AMP and dAMP. The purine 5′-nucleotidase is inhibited by Pi, and is strongly stimulated by ATP, dATP and GTP, and by glycerate 2,3-bisphosphate. Stimulators decrease Km and increase Vmax.

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Faudry, Eric, Silene P. Lozzi, Jaime M. Santana, Marian D'Souza-Ault, Sylvie Kieffer, Carlos R. Felix, Carlos A. O. Ricart, Marcelo V. Sousa, Thierry Vernet, and Antonio R. L. Teixeira. "Triatoma infestansApyrases Belong to the 5′-Nucleotidase Family." Journal of Biological Chemistry 279, no. 19 (February 25, 2004): 19607–13. http://dx.doi.org/10.1074/jbc.m401681200.

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Apyrases are nucleoside triphosphate-diphosphohydrolases (EC 3.6.1.5) present in a variety of organisms. The apyrase activity found in the saliva of hematophagous insects is correlated with the prevention of ADP-induced platelet aggregation of the host during blood sucking. Purification of apyrase activity from the saliva of the triatomine bugTriatoma infestanswas achieved by affinity chromatography on oligo(dT)-cellulose and gel filtration chromatography. The isolated fraction includes fiveN-glycosylated polypeptides of 88, 82, 79, 68 and 67 kDa apparent molecular masses. The isolated apyrase

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Malin, Edyth L., and Jay J. Basch. "Differential release of proteins from bovine fat globule membrane." Biochemistry and Cell Biology 68, no. 5 (May 1, 1990): 899–902. http://dx.doi.org/10.1139/o90-133.

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Alkaline phosphatase and 5′-nucleotidase are covalently linked to phosphatidylinositol in bovine fat globule membrane, as demonstrated by their release following treatment with phospholipase C specific for phosphatidylinositol. The failure of this treatment to liberate phosphodiesterase I may indicate that it has a variant linkage resistant to release. In a test of exposure at the membrane surface, alkaline phosphatase and phosphodiesterase I, but not 5′-nucleotidase, were released from fat globule membrane by treatment with proteinase K. These apparent differences in accessibilities of membra

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Roszek, Katarzyna, Katarzyna Bomastek, Marian Drożdżal, and Michał Komoszyński. "Dramatic differences in activity of purines metabolizing ecto-enzymes between mesenchymal stem cells isolated from human umbilical cord blood and umbilical cord tissue." Biochemistry and Cell Biology 91, no. 6 (December 2013): 519–25. http://dx.doi.org/10.1139/bcb-2013-0050.

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The high quality human mesenchymal stem cells (MSCs) with remarkable expansion potential in culture are demonstrated to possess multifold clinical applications. However, their isolation and characterization are difficult and sometimes ambiguous. We exploited nucleotide metabolizing ecto-enzymes for more complete characterization of MSCs. Using standard methods of cell culturing and analyses, we detected significant differences in the activity of ecto-nucleotidases on the surface of MSCs isolated from umbilical cord tissue and MSC-like cells derived from umbilical cord blood. Interestingly, the

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DOLESKI, PEDRO H., RICARDO E. MENDES, DANIELA B. R. LEAL, NATHIELI B. BOTTARI, MANOELA M. PIVA, ESTER S. DA SILVA, MATEUS E. GABRIEL, et al. "Seric and hepatic NTPDase and 5′ nucleotidase activities of rats experimentally infected byFasciola hepatica." Parasitology 143, no. 5 (March 1, 2016): 551–56. http://dx.doi.org/10.1017/s0031182015001882.

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SUMMARYThe enzymatic activities of NTPDase and 5′nucleotidase are important to regulate the concentration of adenine nucleotides, known molecules involved in many physiological functions. Therefore, the objective of this study was to evaluate the activity of NTPDase and 5′nucleotidase in serum and liver tissue of rats infected byFasciola hepatica. Rats were divided into two groups: uninfected control and infected. NTPDase activity for adenosine triphosphate (ATP) and ADP substrates in the liver was higher compared with the control group at 15 days post-infection (PI), while seric activity was

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Dai, Qin-xue, Shan Li, Miao Ren, Xinlu Wu, Xin-yu Yao, Fei-hong Lin, Xu-qing Ni, Yun-chang Mo, and Jun-lu Wang. "Analgesia with 5' extracellular nucleotidase-mediated electroacupuncture for neuropathic pain." Arquivos de Neuro-Psiquiatria 80, no. 3 (March 2022): 289–95. http://dx.doi.org/10.1590/0004-282x-anp-2021-0149.

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ABSTRACT Background: Acupuncture is a treatment for neuropathic pain, but its mechanism remains unclear. Previous studies showed that analgesia was induced in rats with neuropathic pain when their spinal cord adenosine content increased after electroacupuncture (EA); however, the mechanism behind this electroacupuncture-induced increase has not been clarified. Objective: This study aimed to determine the role that ecto-5’-nucleotidase plays in EA-induced analgesia for neuropathic pain. Methods: We performed electroacupuncture at the Zusanli acupoint on the seventh day after establishing a rat

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Willadsen, P., J. M. Nielsen, and G. A. Riding. "Purification and properties of a novel nucleotide-hydrolysing enzyme (5′-nucleotidase) from Boophilus microplus." Biochemical Journal 258, no. 1 (February 15, 1989): 79–85. http://dx.doi.org/10.1042/bj2580079.

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The tick Boophilus microplus contains a nucleoside phosphate-hydrolysing enzyme which, in many respects, resembles the well characterized 5'-nucleotidase from mammalian tissue. The tick enzyme has been purified to homogeneity. It is a membrane-bound glycoprotein with an apparent Mr of 67,000 and, although it fails to hydrolyse a range of nucleoside 2'- or 3'-monophosphates, it has broad specificity for the 5' derivatives. Further investigation of the enzyme's substrate specificity, however, shows some important differences from the mammalian nucleotidases. It hydrolyses both bis-p-nitrophenyl

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Özsoylu, Şinasi. "About Pyrimidine 5’-Nucleotidase Deficiency." Turkish Journal of Hematology 30, no. 2 (June 5, 2013): 227. http://dx.doi.org/10.4274/tjh.2013.0050.

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