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Published: 4 June 2021
Last updated: 20 February 2023

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1

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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2

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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3

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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4

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 from renal brush-border membranes. In phase-partition experiments using Triton X-114, the soluble enzyme appeared to be hydrophobic. Its hydrophobicity was decreased on treatment with a phosphatidylinositol-specific phospholipase C, suggesting that the soluble ‘low-Km’ 5′-nucleotidase contains the phosphatidylinositol anchor which is characteristic for the ecto-enzyme. An anti-ecto-5′-nucleotidase antiserum provoked an almost complete inhibition of the soluble enzyme. Immunoblotting using anti-ecto-5′-nucleotidase antiserum revealed in the high-speed supernatants a polypeptide with a similar Mr to the subunit of the ecto-5′-nucleotidase. The soluble ‘low-Km’ 5′-nucleotidase, like the ecto-5′-nucleotidase, bound specifically to concanavalin A. We conclude that the soluble ‘low-Km’ 5′-nucleotidase is not a cytosolic enzyme, but that it most probably originates from the solubilization of the ecto-5′-nucleotidase, and that it therefore cannot participate in the intracellular production of adenosine.
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5

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 absolute requirement for Mg2+. ADP, (20-480 mumol/l) activated supernatant and inhibited membrane-bound 5'-nucleotidase activity. At 80 mumol/l ADP, 5 mmol/l MgCl2, 100 mumol/l AMP, and pH 7.3, the average 5'-nucleotidase activities of the supernatant vs. pellet were 74% of total and 26% of total, respectively. Total adenosine production in unfractionated samples of ventricular homogenates decreased an average of 73% by specific inhibition of cytosolic 5'-nucleotidase, using antibodies against the cytosolic enzyme, and 46% by specific inhibition of ecto-5'-nucleotidase with alpha, beta-methylene adenosine 5'-diphosphate (AOPCP). These findings support the hypotheses that 1) both cytosolic and ecto-5'-nucleotidase contribute to cardiac adenosine production in dog heart homogenates; 2) AMP-specific cytosolic 5'-nucleotidase activity exceeds ecto-5'-nucleotidase activity at physiological concentrations of ADP, AMP, and Mg2+; and 3) Mg2+ is an important regulator of cardiac adenosine production via activation of both ecto- and AMP-specific cytosolic 5'-nucleotidases.
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6

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 < 20%) and sensitive (detected nucleotidase fractions of > 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 5%), NTP2 (mean 30%, SD 8%), and NTP3 (mean 58%, SD 8%) were found in all normal persons studied. The increase in total 5'-nucleotidase in patients with hepatobiliary disease was mainly due to the NTP1 isoform.
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7

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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8

Hansen, Thor Willy Ruud, Martin Seip, Carl-Henric Verdier, and ÅKe Ericson. "Erythrocyte Pyrimidine 5‘-Nucleotidase Deficiency." Scandinavian Journal of Haematology 31, no. 2 (April 24, 2009): 122–28. http://dx.doi.org/10.1111/j.1600-0609.1983.tb01518.x.

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9

Ramaswamy, S. G., and W. B. Jakoby. "(2')3',5'-Bisphosphate nucleotidase." Journal of Biological Chemistry 262, no. 21 (July 1987): 10044–47. http://dx.doi.org/10.1016/s0021-9258(18)61072-5.

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10

Colaco, Camilo A. L. S. "Potocytosis, 5′-nucleotidase and transport." Trends in Cell Biology 2, no. 8 (August 1992): 223. http://dx.doi.org/10.1016/0962-8924(92)90299-3.

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11

Hunsucker, Sally Anne, Jozef Spychala, and Beverly S. Mitchell. "Human Cytosolic 5′-Nucleotidase I." Journal of Biological Chemistry 276, no. 13 (December 22, 2000): 10498–504. http://dx.doi.org/10.1074/jbc.m011218200.

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12

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 and 2.69 for cholinesterase and 1.41 and 0.97 for 5'-nucleotidase, respectively. Intra- to interindividual standard deviation ratios were 0.38 for cholinesterase and 1.21 for 5'-nucleotidase. Average within-run analytical variances were 0.13 and 0.3 (4% and 13% of total variance) for cholinesterase and 5'-nucleotidase, respectively. The importance of these findings in regards to diagnostic interpretation of serum cholinesterase and 5'-nucleotidase results is discussed.
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13

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 either Mn2+ or Co2+, whereas half-maximal activity is obtained with approximately 400 microM Mg2+. The soluble 5'-nucleotidase exhibits Michaelis-Menten kinetics with a Km of 9.5 microM for 5'-AMP. In the presence of 1 mM of free Mg2+, physiological concentrations of ATP provoke an increase of the Km for 5'-AMP and a decrease of Vmax. An increase of the pH of 0.4 units in the pH range 6.4-7.4 roughly doubles the rate of hydrolysis of 5'-AMP. The effects of ATP and of the pH are compatible with a role of the renal soluble 5'-nucleotidase in the hydrolysis of 5'-AMP and in the production of adenosine during hypoxia.
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14

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. DTAB and deoxycholate caused a loss of heat stability, while alkylthioglucosides had no effect. CHAPS produced a remarkable increase in the heat stability of the partially purified (glycoprotein fraction) and purified enzyme. Arrhenius plots of solubilized 5′-nucleotidase showed "break points" for all detergents in the temperature range 30–37 °C. SDS-PAGE of pure 5′-nucleotidase showed a single subunit of molecular mass 70 kilodaltons (kDa), while sucrose density gradient sedimentation gave a peak of activity corresponding to 132 kDa, indicating that the enzyme exists as a dimer. Gel filtration of the solubilized enzyme in several detergents showed apparent molecular masses between 200–630 kDa, suggesting that lymphocyte 5′-nucleotidase may be present in high molecular mass aggregates in its native state.Key words: 5′-nucleotidase, plasma membrane, detergents, solubilization, stability, activation energy.
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15

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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16

WADA, Ikuo, Shigeki ETO, Masaru HIMENO, and Keitaro KATO. "5′-Nucleotidase in Rat Liver Lysosomes." Journal of Biochemistry 101, no. 5 (1987): 1077–85. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a121972.

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17

Yamazaki, Yukiko, Vu L. Truong, and John M. Lowenstein. "5'-Nucleotidase I from rabbit heart." Biochemistry 30, no. 6 (February 12, 1991): 1503–9. http://dx.doi.org/10.1021/bi00220a009.

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18

Subkhankulova, A. F. "5′ - Nucleotidase activity in immunoconflict pregnancy." Journal of Reproductive Immunology 15 (July 1989): 122. http://dx.doi.org/10.1016/0165-0378(89)90254-4.

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19

Kiviluoma, K. "Subcellular distribution of myocardial 5′-nucleotidase." Journal of Molecular and Cellular Cardiology 22, no. 7 (July 1990): 827–35. http://dx.doi.org/10.1016/0022-2828(90)90093-h.

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20

Trummal, Katrin, Mari Samel, Anu Aaspõllu, Külli Tõnismägi, Tiina Titma, Juhan Subbi, Jüri Siigur, and Ene Siigur. "5′-Nucleotidase from Vipera lebetina venom." Toxicon 93 (January 2015): 155–63. http://dx.doi.org/10.1016/j.toxicon.2014.11.234.

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21

Keller, P. M., S. A. McKee, and J. A. Fyfe. "Cytoplasmic 5'-nucleotidase catalyzes acyclovir phosphorylation." Journal of Biological Chemistry 260, no. 15 (July 1985): 8664–67. http://dx.doi.org/10.1016/s0021-9258(17)39398-5.

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22

Amano, Shigeru, Tsunehisa Watanabe, Masanori Ikeuchi, Masakiyo Sasahara, Eiji Yamada, and Fumitada Hazama. "5′-Nucleotidase Activities in Human Fetus." Neonatology 47, no. 5 (1985): 253–58. http://dx.doi.org/10.1159/000242125.

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23

Ho, May Y. K., Garry A. Rechnitz, and Ted K. Chen. "Potentiometric determination of serum 5′-nucleotidase." Journal of Clinical Laboratory Analysis 2, no. 2 (1988): 117–23. http://dx.doi.org/10.1002/jcla.1860020209.

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24

Pinto, Rosa M., José Canales, María A. Günther Sillero, and Antonio Sillero. "Diadenosine tetraphosphate activates cytosol 5′-nucleotidase." Biochemical and Biophysical Research Communications 138, no. 1 (July 1986): 261–67. http://dx.doi.org/10.1016/0006-291x(86)90274-3.

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25

Sträter, Norbert. "Ecto-5’-nucleotidase: Structure function relationships." Purinergic Signalling 2, no. 2 (May 16, 2006): 343–50. http://dx.doi.org/10.1007/s11302-006-9000-8.

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26

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 hydrolysis of 1 mM-5′-IMP 16-fold. The effect was specific for the decameric form of vanadate, since it was not reproduced by either decavanadate-free orthovanadate or pervanadate. Half-maximal activation was obtained at 1.4 nM-decavanadate. Decavanadate increased the affinity of the soluble 5′-nucleotidase for 5′-IMP. The effects of 2,3-DPG and of vanadate were not additive. Thus decavanadate probably influences the soluble 5′-nucleotidase in the same way as 2,3-DPG, but with a much higher potency.
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27

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%) and IP3 (33.8 +/- 3.6%) groups compared with the IP1 group (8.3 +/- 1.6%) and returned to the control level in the IP4 group (39.9 +/- 5.2%). The increased ecto-5' -nucleotidase activity due to the IP procedure decreased according to the order of IP1 to IP4 groups. Infarct size was inversely correlated with ecto-5'-nucleotidase activity (P < 0.001). An inhibitor of ecto-5'-nucleotidase blunted the infarct size-limiting effect of IP. The infarct size-limiting effect of IP decreased as the activation of ecto-5'-nucleotidase was blunted. These results suggest that ecto-5'-nucleotidase activity plays a key role in the cardioprotection of IP.
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28

Hirono, Akira, Hisaichi Fujii, Hideyo Natori, Izumi Kurokawa, and Shiro Miwa. "Chromatographic analysis of human erythrocyte pyrimidine 5'-nucleotidase from five patients with pyrimidine 5'-nucleotidase deficiency." British Journal of Haematology 65, no. 1 (January 1987): 35–41. http://dx.doi.org/10.1111/j.1365-2141.1987.tb06132.x.

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29

Cook, L. R., C. R. Angle, and S. J. Stohs. "Erythrocyte arginase, pyrimidine 5'-nucleotidase (P5N), and deoxypyrimidine 5'-nucleotidase (dP5N) as indices of lead exposure." Occupational and Environmental Medicine 43, no. 6 (June 1, 1986): 387–90. http://dx.doi.org/10.1136/oem.43.6.387.

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30

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′-nucleotidase activity can be inhibited by the antibodies. Thus at least three groups of antigenic determinants must exist on the 5′-nucleotidase: one related to the glucidic moiety of the glycoprotein whose binding inhibits the enzyme activity, another related to the catalytic site, as its binding also led to enzyme inhibition, and a last one of structural nature. It seems that the third group of determinant is common to many species, whereas the second one is more restricted.
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31

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 studied in Vibrio harveyi, and it was shown that both adenosine and inorganic phosphate released upon the action of 5′-nucleotidase were rapidly taken up by the cell.
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32

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 model of neuropathic pain induced through chronic constriction injuries. We observed the mechanical withdrawal threshold and thermal pain threshold and detected the expression of ecto-5’-nucleotidase in the spinal cord using Western blot. Chronic constriction injury rat models were intraperitoneally injected with α,β-methyleneadenosine 5'-diphosphate, an ecto-5’-nucleotidase inhibitor, 30 min before electroacupuncture. The adenosine content of the spinal cord was detected using high-performance liquid chromatography. Lastly, the adenosine A1 receptor agonist N6-cyclopentyladenosine was intrathecally injected into the lumbar swelling of the rats, and the mechanical withdrawal and thermal pain thresholds were reevaluated. Results: Analgesia and increased ecto-5’-nucleotidase expression and adenosine content in the spinal cord were observed 1 h after electroacupuncture. α,β-methyleneadenosine 5'-diphosphate was able to inhibit upregulation of adenosine content and electroacupuncture-induced analgesia. After administration of N6-cyclopentyladenosine, electroacupuncture-induced analgesia was restored. Conclusions: Our results suggest that electroacupuncture at Zusanli can produce analgesia in chronic constriction injury rat models, possibly via the increased ecto-5’-nucleotidase expression induced through electroacupuncture, thus leading to increased adenosine expression in the spinal cord.
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33

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 structure. Dog heart cytosolic 5'-nucleotidase was active at physiological pH (6.8-7.8) and demonstrated a preference for AMP over IMP as substrate. The enzyme exhibited sigmoidal saturation kinetics, with half-maximal activity at 2.6 mM AMP in the absence of ADP. ADP (0-250 microM) activated cytosolic 5'-nucleotidase by increasing maximal velocity and affinity for AMP. The enzyme was inhibited by 4 mM ATP, but 5'-nucleotidase activity increased as [ATP] was reduced. Mg2+ was required for activity, with maximal activation at approximately 3.5 mM free Mg2+. These data suggest that the regulation of AMP-specific cytosolic 5'-nucleotidase by adenine nucleotides and free Mg2+ may be important in the production of adenosine during conditions promoting ATP hydrolysis, such as myocardial hypoxia or ischemia.
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34

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′-nucleotidase molecule is present on the cytoplasmic side of the plasma membrane. No evidence was found for a previously proposed interaction between 5′-nucleotidase and actin, although the ability of preparations of 5′-nucleotidase to prevent inhibition of deoxyribonuclease I by actin was explained by minute traces of ATPase activity. Comparison of peptide maps of enzyme labelled by iodination or by methods specific for carbohydrate showed that in both cases predominantly one section of the molecule was labelled. It is proposed that the enzyme is a short-stalked integral membrane protein without a cytoplasmic domain in which about one-third of the molecule forms the accessible molecular surface.
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35

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′-isobutylthioadenosine, an inhibitor of the previously purified IMP-preferring cytosolic 5′-nucleotidase. 3. Subcellular-fractionation studies indicated that the enzyme has access to cytosolic AMP, although it may be associated by weak ionic interactions with an organelle present in the low-speed particulate fraction. 4. A 5′-nucleotidase was detected under similar conditions in homogenates of rat heart. 5. The activity of the pigeon heart AMP-5′-nucleotidase was sufficient to account for previously measured rates of ischaemia-induced adenosine formation. The similar activity in rat heart could, however, account for only part of ischaemia-induced adenosine formation in this tissue.
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36

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-specific phospholipase C (PI-PLC). Membrane-bound, detergent-solubilized and cleaved 5´-nucleotidase all obeyed Michaelis–Menten kinetics, with a Km for 5´-AMP in the range 11–16 µM. The GPI anchor was removed from essentially all 5´-nucleotidase molecules, indicating that there is no phospholipase-resistant pool of enzyme. However, the phospholipase was much less efficient at cleaving the GPI anchor when 5´-nucleotidase was present in detergent solution, dimyristoyl phosphatidylcholine, egg phosphatidylethanolamine and sphingomyelin, compared with the native plasma membrane, egg phosphatidylcholine and a sphingolipid/cholesterol-rich mixture. Lipid molecular properties and bilayer packing may affect the ability of PI-PLC to gain access to the GPI anchor. Catalytic activation, characterized by an increase in Vmax, was observed following PI-PLC cleavage of reconstituted 5´-nucleotidase from vesicles of several different lipids. The highest degree of activation was noted for 5´-nucleotidase in egg phosphatidylethanolamine. An increase in Vmax was also noted for a sphingolipid/cholesterol-rich mixture, the native plasma membrane and egg phosphatidylcholine, whereas vesicles of sphingomyelin and dimyristoyl phosphatidylcholine showed little activation. Km generally remained unchanged following cleavage, except in the case of the sphingolipid/cholesterol-rich mixture. Insertion of the GPI anchor into a lipid bilayer appears to reduce the catalytic efficiency of 5´-nucleotidase, possibly via a conformational change in the enzyme, and activity is restored on release from the membrane.
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37

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. Glycerate 2,3-bisphosphate is the most potent stimulator of the enzyme and, under physiological conditions, over-rides the influence of the other effectors. Glycerate 2,3-bisphosphate also influences the binding of the enzyme to DEAE-Trisacryl, as evidenced by the different elution profile obtained with fresh as compared with outdated blood. It is concluded that the glycerate 2,3-bisphosphate-stimulated purine 5′-nucleotidase is responsible for the dephosphorylation of IMP and GMP, but not of AMP, in human erythrocytes.
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38

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 the enzyme in bilayers of dimyristoyl phosphatidylcholine show a break point at 22–23 °C, with a different activation energy above and below the phospholipid gel-to-liquid crystalline phase transition. 5′-Nucleotidase in intact plasma membrane is inhibited more than 95% by concanavalin A in a positively cooperative fashion (Hill coefficient = 2.1), as is partially purified reconstituted enzyme. Purification of the enzyme before reconstitution results in less than 50% inhibition by concanavalin A and a complete loss of positive cooperativity (Hill coefficient < 1.0). The inhibition properties of the enzyme can be fully restored by co-reconstituting pure 5′-nucleotidase with the remaining lymphocyte glycoproteins.
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39

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, whereas succinyl-concanavalin A does not bind to this site. The monovalent lectin from Ricinus communis (RCA-60) is a more effective enzyme inhibitor than the related divalent lectin (RCA-120), and inactivation of the second low-affinity sugar binding site on RCA-60 does not abolish inhibition, suggesting that multivalent cross-linking is not required for 5′-nucleotidase inhibition. Peanut and wheat germ agglutinins do not inhibit the enzyme, whereas lectins from lentil, pea, soybean, Griffonia simplicifolia, and Phaseolus vulgaris inhibit 5′-nucleotidase with various degrees of effectiveness. The only lectin showing strong positive cooperativity in its interaction with 5′-nucleotidase is concanavalin A.
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40

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′-FSBA, demonstrating that the inactivation was due to the modification of amino acid residues essential for AMPase activity. We have synthesized radioactive 5′-FSBA, which was employed for the radiolabelling of chicken gizzard 5′-nucleotidase. Incorporation of radioactivity was completely abolished in the presence of ATP, which showed that 5′-FSBA acted by the selective modification of amino acid residues at the active site whereas other potential reactive residues of the protein were not attacked. Limited proteolysis of affinity-labelled chicken gizzard 5′-nucleotidase permitted the identification of digestion products containing the catalytic centre. Pseudo-first-order kinetics indicate that modification of a minimum of one amino acid side chain at the active centre is sufficient to result in inactivation of both chicken gizzard and snake-venom 5′-nucleotidases. Incorporation of the radioactive p-sulphonylbenzoyladenosine moiety parallels the inactivation of 5′-nucleotidase by 5′-FSBA and further substantiated the idea that modification of one amino acid residue at the active centre results in loss of the AMPase activity.
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41

Jensen, Henning. "5-NUCLEOTIDASE ACTIVITY IN THE HUMAN BREAST." Acta Pathologica Microbiologica Scandinavica Section A Pathology 80A, no. 5 (August 15, 2009): 665–70. http://dx.doi.org/10.1111/j.1699-0463.1972.tb00332.x.

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42

Picher, Maryse, Lauranell H. Burch, Andrew J. Hirsh, Josef Spychala, and Richard C. Boucher. "Ecto 5′-Nucleotidase and Nonspecific Alkaline Phosphatase." Journal of Biological Chemistry 278, no. 15 (January 30, 2003): 13468–79. http://dx.doi.org/10.1074/jbc.m300569200.

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43

Nadkarni, Anita H., K. Ghosh, D. Mohanty, and R. Colah. "Hemoglobin E and Pyrimidine 5′ Nucleotidase Deficiency." Blood 90, no. 4 (August 15, 1997): 1716. http://dx.doi.org/10.1182/blood.v90.4.1716a.

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44

Nadkarni, Anita H., K. Ghosh, D. Mohanty, and R. Colah. "Hemoglobin E and Pyrimidine 5′ Nucleotidase Deficiency." Blood 90, no. 4 (August 15, 1997): 1716. http://dx.doi.org/10.1182/blood.v90.4.1716a.1716a_1716_1716.

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45

Bitto, Eduard, Craig A. Bingman, Gary E. Wesenberg, Jason G. McCoy, and George N. Phillips. "Structure of Pyrimidine 5′-Nucleotidase Type 1." Journal of Biological Chemistry 281, no. 29 (May 3, 2006): 20521–29. http://dx.doi.org/10.1074/jbc.m602000200.

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46

Schmies, Constanze C., Georg Rolshoven, Riham M. Idris, Karolina Losenkova, Christian Renn, Laura Schäkel, Haneen Al-Hroub, et al. "Fluorescent Probes for Ecto-5′-nucleotidase (CD73)." ACS Medicinal Chemistry Letters 11, no. 11 (September 3, 2020): 2253–60. http://dx.doi.org/10.1021/acsmedchemlett.0c00391.

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47

Ubeidat, Muatasem, Can M. Eristi, and Charles L. Rutherford. "Expression pattern of 5′-nucleotidase in Dictyostelium." Mechanisms of Development 110, no. 1-2 (January 2002): 237–39. http://dx.doi.org/10.1016/s0925-4773(01)00580-9.

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48

Renkawek, Krystyna. "5'-nucleotidase activity in cultured rat Ieptomeninges." Acta Histochemica 82, no. 1 (1987): 77–82. http://dx.doi.org/10.1016/s0065-1281(87)80055-7.

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49

Wang, Li, Shaoxian Tang, Yingjian Wang, Siguang Xu, Jerry Yu, Xiuling Zhi, Zhouluo Ou, Jiayin Yang, Ping Zhou, and Zhimin Shao. "Ecto-5′-nucleotidase (CD73) promotes tumor angiogenesis." Clinical & Experimental Metastasis 30, no. 5 (March 19, 2013): 671–80. http://dx.doi.org/10.1007/s10585-013-9571-z.

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50

Stochaj, Ursula, Matthias Cramer, and Hans Georg Mannherz. "Limited proteolysis of chicken gizzard 5′-nucleotidase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1122, no. 3 (August 1992): 327–32. http://dx.doi.org/10.1016/0167-4838(92)90413-8.

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