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Journal articles on the topic 'Purine nucleoside phosphorylase. eng'

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Published: 4 June 2021

Last updated: 6 February 2022

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1

Bzowska, Agnieszka, Lucyna Magnowska, and Zygmunt Kazimierczuk. "Synthesis of 6-Aryloxy- and 6-Arylalkoxy-2-chloropurines and Their Interactions with Purine Nucleoside Phosphorylase from Escherichia coli." Zeitschrift für Naturforschung C 54, no. 12 (1999): 1055–67. http://dx.doi.org/10.1515/znc-1999-1210.

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The phase transfer method was applied to perform the nucleophilic substitution of 2,6- dichloropurines by modified arylalkyl alcohol or phenols. Since under these conditions only the 6-halogen is exchanged, this method gives 2-chloro-6-aryloxy- and 2-chloro-6-arylalkoxypurines. 2-Chloro-6-benzylthiopurine was synthesized by alkylation of 2-chloro-6-thiopurine with benzyl bromide. The stereoisomers of 2-chloro-6-(1-phenyl-1-ethoxy)purine were obtained from R- and S-enantiomers of sec.-phenylethylalcohol and 2,6-dichloropurine. All derivatives were tested for inhibition with purified hexameric E

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2

Arpaia, Enrico, Patricia Benveniste, Antonio Di Cristofano, et al. "Mitochondrial Basis for Immune Deficiency." Journal of Experimental Medicine 191, no. 12 (2000): 2197–208. http://dx.doi.org/10.1084/jem.191.12.2197.

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We generated purine nucleoside phosphorylase (PNP)-deficient mice to gain insight into the mechanism of immune deficiency disease associated with PNP deficiency in humans. Similar to the human disease, PNP deficiency in mice causes an immunodeficiency that affects T lymphocytes more severely than B lymphocytes. PNP knockout mice exhibit impaired thymocyte differentiation, reduced mitogenic and allogeneic responses, and decreased numbers of maturing thymocytes and peripheral T cells. T lymphocytes of PNP-deficient mice exhibit increased apoptosis in vivo and higher sensitivity to gamma irradiat

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3

Gandhi, Varsha, John M. Kilpatrick, William Plunkett, et al. "A proof-of-principle pharmacokinetic, pharmacodynamic, and clinical study with purine nucleoside phosphorylase inhibitor immucillin-H (BCX-1777, forodesine)." Blood 106, no. 13 (2005): 4253–60. http://dx.doi.org/10.1182/blood-2005-03-1309.

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The discovery of purine nucleoside phosphorylase (PNP) deficiency and T lymphocytopenia suggested that inhibition of this enzyme could serve as a therapeutic target. Inhibitors of PNP failed until structure-based synthesis of immucillin-H (BCX-1777, forodesine), a transition-state analog of PNP. The picomolar potency for PNP, T cell-selective cytotoxicity, and animal studies provided the rationale for use of forodesine in T-cell malignancies. Five patients were treated with an intravenous infusion of forodesine (40 mg/m2) on day 1; treatment continued on day 2; forodesine was administered ever

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4

Nguyen, B. T., and W. Sadée. "Compartmentation of guanine nucleotide precursors for DNA synthesis." Biochemical Journal 234, no. 2 (1986): 263–69. http://dx.doi.org/10.1042/bj2340263.

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We have studied the kinetics of guanine incorporation into DNA in mouse T-lymphoma (S-49) mutant cells [PNPase (purine-nucleoside phosphorylase)- and HGPRTase (hypoxanthine: guanine phosphoribosyltransferase)-deficient] that are incapable of converting dGuo (deoxyguanosine) to Gua (guanine) ribonucleotides. Of the two possible pathways for an exogenous guanine source to reach DNA, firstly: dGuo→dGMP→dGDP→dGTP and secondly: Gua→GMP→GDP→dGDP→dGTP only the second pathway was found to be functional in providing guanine for DNA replication, although deoxyguanosine readily produced toxic cellular dG

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5

Pogosian, L. H., and J. I. Akopian. "Purine nucleoside phosphorylase." Biomeditsinskaya Khimiya 59, no. 5 (2013): 483–97. http://dx.doi.org/10.18097/pbmc20135905483.

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Purine nucleoside phosphorylase (PNP) is one of the most important enzymes of the purine metabolism, wich promotes the recycling of purine bases. Nowadays is the actual to search for effective inhibitors of this enzyme which is necessary for creation T-cell immunodeficient status of the organism in the organs and tissues transplantation, and chemotherapy of a number pathologies as well. For their successful practical application necessary to conduct in-depth and comprehensive study of the enzyme, namely a structure, functions, and an affinity of the reaction mechanism. In the review the contem

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6

Furman, Richard R., Varsha V. Gandhi, J. Claude Bennett, Shanta Bantia, and J. Michael Kilpatrick. "Intravenous Forodesine (BCX-1777), a Novel Purine Nucleoside Phosphorylase (PNP) Inhibitor, Demonstrates Clinical Activity in Phase I/II Studies in Patients with B-Cell Acute Lymphoblastic Leukemia." Blood 104, no. 11 (2004): 2743. http://dx.doi.org/10.1182/blood.v104.11.2743.2743.

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Abstract Forodesine is a potent, specific transition-state analog inhibitor of PNP with clinical activity in T-cell malignancies. Pharmacodynamic studies support that this anti-leukemic effect is mediated through the accumulation of plasma 2′-deoxyguanosine (dGuo) and intracellular Dgtp. In vitro studies indicated that B-cell acute lymphoblastic leukemia (B-ALL) cells can also accumulate Dgtp. These preclinical data led to a phase I/II multicenter dose-escalation study to evaluate forodesine in pts with various hematologic malignancies. 15 pts were treated with forodesine, including 6 with B-A

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7

Montgomery, John A. "Inhibitors of purine nucleoside phosphorylase." Expert Opinion on Investigational Drugs 3, no. 12 (1994): 1303–13. http://dx.doi.org/10.1517/13543784.3.12.1303.

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8

Pogosian, L. H., L. S. Nersesova, M. G. Gazariants, Z. S. Mkrtchian, and J. I. Akopian. "Some inhibitors of purine nucleoside phosphorylase." Biomeditsinskaya Khimiya 57, no. 5 (2011): 526–34. http://dx.doi.org/10.18097/pbmc20115705526.

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Purine nucleoside phosphorylase (PNP) catalyzes reversible phosphorolysis of purine deoxy- and ribonucleosides with formation (d)Rib-1-P and corresponding bases. PNP plays a leading role in the cell metabolism of nucleosides and nucleotides, as well as in maintaining the immune status of an organism. The major aim of the majority of studies on the PNP is the detection of highly effective inhibitors of this enzyme, derivatives of purine nucleosides used in medicine as immunosuppressors, which are essential for creating selective T-cell immunodeficiency in a human body for organ and tissue trans

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9

Erion, Mark D., Johanna D. Stoeckler, Wayne C. Guida, and Richard L. Walter. "Purine Nucleoside Phosphorylase. 2. Catalytic Mechanism†." Biochemistry 36, no. 39 (1997): 11735–48. http://dx.doi.org/10.1021/bi961970v.

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10

Šedivá, Katarina, Ivan Votruba, Antonín Holý, and Ivan Rosenberg. "Purine nucleoside phosphorylase: Isolation and characterization." Collection of Czechoslovak Chemical Communications 55, no. 12 (1990): 2987–99. http://dx.doi.org/10.1135/cccc19902987.

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Purine nucleoside phosphorylase (PNP) from mouse leukemia cells L1210 was purified to homogeneity by a combination of ion exchange and affinity chromatography using AE-Sepharose 4B and 9-(p-succinylaminobenzyl)hypoxanthine as the matrix and the ligand, respectively. The native enzyme has a molecular weight of 104 000 and consists of three subunits of equal molecular weight of 34 000. The results of isoelectric focusing showed that the enzyme is considerably microheterogeneous over the pI-range 4.0-5.8 and most likely consists of eight isozymes. The temperature and pH-optimum of phosphorolysis,

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11

Pogosian, L. H., L. S. Nersesova, M. G. Gazariants, Z. S. Mkrtchian, and J. I. Akopian. "Some inhibitors of purine nucleoside phosphorylase." Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry 5, no. 1 (2011): 60–64. http://dx.doi.org/10.1134/s1990750811010094.

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12

Ropp, Patricia A., and Thomas W. Traut. "Allosteric regulation of purine nucleoside phosphorylase." Archives of Biochemistry and Biophysics 288, no. 2 (1991): 614–20. http://dx.doi.org/10.1016/0003-9861(91)90244-d.

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13

Tam, David A., and Robert T. Leshner. "Stroke in purine nucleoside phosphorylase deficiency." Pediatric Neurology 12, no. 2 (1995): 146–48. http://dx.doi.org/10.1016/0887-8994(94)00118-l.

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14

Markert, M. Louise, Bruce D. Finkel, Tanya M. McLaughlin, et al. "Mutations in purine nucleoside phosphorylase deficiency." Human Mutation 9, no. 2 (1997): 118–21. http://dx.doi.org/10.1002/(sici)1098-1004(1997)9:2<118::aid-humu3>3.0.co;2-5.

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15

Cohen, Amos, Eyal Grunebaum, Enrico Arpaia, and Chaim M. Roifman. "IMMUNODEFICIENCY CAUSED BY PURINE NUCLEOSIDE PHOSPHORYLASE DEFICIENCY." Immunology and Allergy Clinics of North America 20, no. 1 (2000): 143–59. http://dx.doi.org/10.1016/s0889-8561(05)70139-9.

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16

Krenitsky, T. A., J. V. Tuttle, W. H. Miller, A. R. Moorman, G. F. Orr, and L. Beauchamp. "Nucleotide analogue inhibitors of purine nucleoside phosphorylase." Journal of Biological Chemistry 265, no. 6 (1990): 3066–69. http://dx.doi.org/10.1016/s0021-9258(19)39734-0.

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17

Erion, Mark D., Kenji Takabayashi, Harry B. Smith, et al. "Purine Nucleoside Phosphorylase. 1. Structure−Function Studies†." Biochemistry 36, no. 39 (1997): 11725–34. http://dx.doi.org/10.1021/bi961969w.

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18

Lecoq, K., I. Belloc, C. Desgranges, M. Konrad, and B. Daignan-Fornier. "YLR209c Encodes Saccharomyces cerevisiae Purine Nucleoside Phosphorylase." Journal of Bacteriology 183, no. 16 (2001): 4910–13. http://dx.doi.org/10.1128/jb.183.16.4910-4913.2001.

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ABSTRACT The yeast YLR209c (PNP1) gene encodes a protein highly similar to purine nucleoside phosphorylases. This protein specifically metabolized inosine and guanosine. Disruption ofPNP1 led to inosine and guanosine excretion in the medium, thus showing that PNP1 plays an important role in the metabolism of these purine nucleosides in vivo.

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19

Kang, You-Na, Yang Zhang, Paula W. Allan, et al. "Structure of grouper iridovirus purine nucleoside phosphorylase." Acta Crystallographica Section D Biological Crystallography 66, no. 2 (2010): 155–62. http://dx.doi.org/10.1107/s0907444909048276.

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Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine ribonucleosides to the corresponding free bases and ribose 1-phosphate. The crystal structure of grouper iridovirus PNP (givPNP), corresponding to the first PNP gene to be found in a virus, was determined at 2.4 Å resolution. The crystals belonged to space groupR3, with unit-cell parametersa= 193.0,c= 105.6 Å, and contained four protomers per asymmetric unit. The overall structure of givPNP shows high similarity to mammalian PNPs, having an α/β structure with a nine-stranded mixed β-barrel flanked by a tota

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20

Morisaki, Takayuki, Naomi Horiuchi, Hisaichi Fujii, and Shiro Miwa. "Characterization of purine nucleoside phosphorylase in leukemia." American Journal of Hematology 23, no. 3 (1986): 263–69. http://dx.doi.org/10.1002/ajh.2830230310.

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21

Walker, P. L. C., Adele Corrigan, Monica Arenas, Emilia Escuredo, Lynette Fairbanks, and Anthony Marinaki. "Purine Nucleoside Phosphorylase Deficiency: A Mutation Update." Nucleosides, Nucleotides and Nucleic Acids 30, no. 12 (2011): 1243–47. http://dx.doi.org/10.1080/15257770.2011.630852.

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22

Morris, Jr., Philip E., and John A. Montgomery. "Inhibitors of the enzyme purine nucleoside phosphorylase." Expert Opinion on Therapeutic Patents 8, no. 3 (1998): 283–99. http://dx.doi.org/10.1517/13543776.8.3.283.

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23

De Luca, E. Carapella, M. Stegagno, C. Dionisi Vici, et al. "Prenatal exclusion of purine nucleoside phosphorylase deficiency." European Journal of Pediatrics 145, no. 1-2 (1986): 51–53. http://dx.doi.org/10.1007/bf00441852.

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24

Roberts, Elton L. L., Russell P. Newton, and Alan T. Axford. "Plasma purine nucleoside phosphorylase in cancer patients." Clinica Chimica Acta 344, no. 1-2 (2004): 109–14. http://dx.doi.org/10.1016/j.cccn.2004.02.008.

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25

Alangari, A. A. A., A. Al-Harbi, A. Alghonaium, and M. Hershfied. "Purine Nucleoside Phosphorylase Deficiency in Saudi Arabia." Journal of Allergy and Clinical Immunology 117, no. 2 (2006): S173. http://dx.doi.org/10.1016/j.jaci.2005.12.689.

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26

Tsuda, Masahiko, Kenichi Horinouchi, Takeshi Sakiyama, and Misao Owada. "Novel missense mutation in the purine nucleoside phosphorylase gene in a Japanese patient with purine nucleoside phosphorylase deficiency." Pediatrics International 44, no. 3 (2002): 333–34. http://dx.doi.org/10.1046/j.1442-200x.2002.01543.x.

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27

Marr, C. L. P., and C. R. Penn. "Stability of Carbovir, a Potent Inhibitor of HIV, to Phosphorolysis by Human Purine Nucleoside Phosphorylase." Antiviral Chemistry and Chemotherapy 3, no. 2 (1992): 121–24. http://dx.doi.org/10.1177/095632029200300207.

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Carbovir, a carbocyclic guanosine analogue, is a selective and potent inhibitor of HIV-1 in vitro. The (-)enantiomer of carbovir has been shown, by spectrophotometric and high pressure liquid chromatography (HPLC) analysis, to be stable to phosphorolytic cleavage by purified human erythrocytic purine nucleoside Phosphorylase. Thus depurination, and the salvage reaction via hypoxanthine-guanine phosphoribosyl transferase, would be unlikely to be involved in the metabolism of carbovir. Inhibition of purine nucleoside Phosphorylase interferes with T-lymphocytic function and would be an undesirabl

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28

Bzowska, A., E. Kulikowska, D. Shugar, Bing-yi Chen, B. Lindborg, and N. G. Johansson. "Acyclonucleoside analogue inhibitors of mammalian purine nucleoside phosphorylase." Biochemical Pharmacology 41, no. 12 (1991): 1791–803. http://dx.doi.org/10.1016/0006-2952(91)90117-n.

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29

Mansouri, Alireza, Weixian Min, Christina J. Cole, et al. "Cerebellar abnormalities in purine nucleoside phosphorylase deficient mice." Neurobiology of Disease 47, no. 2 (2012): 201–9. http://dx.doi.org/10.1016/j.nbd.2012.04.001.

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30

Chu, Samuel Y., Peter Cashion, and Min Jiang. "A new colorimetric assay for purine nucleoside phosphorylase." Clinical Biochemistry 22, no. 5 (1989): 357–62. http://dx.doi.org/10.1016/s0009-9120(89)80032-3.

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31

Grenha, Rosa, Vladimir M. Levdikov, Mark J. Fogg, et al. "Structure of purine nucleoside phosphorylase (DeoD) fromBacillus anthracis." Acta Crystallographica Section F Structural Biology and Crystallization Communications 61, no. 5 (2005): 459–62. http://dx.doi.org/10.1107/s174430910501095x.

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32

Guimarães Silva, Rafael, Diógenes Santiago Santos, Luiz Augusto Basso, et al. "Purine Nucleoside Phosphorylase Activity in Rat Cerebrospinal Fluid." Neurochemical Research 29, no. 10 (2004): 1831–35. http://dx.doi.org/10.1023/b:nere.0000042209.02324.98.

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33

Waalkes, M. P. "Purine Nucleoside Phosphorylase: A Fortuitous Cytosolic Arsenate Reductase?" Toxicological Sciences 70, no. 1 (2002): 1–3. http://dx.doi.org/10.1093/toxsci/70.1.1.

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34

Gregus, Z. "Purine Nucleoside Phosphorylase as a Cytosolic Arsenate Reductase." Toxicological Sciences 70, no. 1 (2002): 13–19. http://dx.doi.org/10.1093/toxsci/70.1.13.

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35

Mason, Jennifer M., Andrew S. Murkin, Lei Li, Vern L. Schramm, Graeme J. Gainsford та Brian W. Skelton. "A β-Fluoroamine Inhibitor of Purine Nucleoside Phosphorylase". Journal of Medicinal Chemistry 51, № 18 (2008): 5880–84. http://dx.doi.org/10.1021/jm800792b.

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36

Toms, Angela V., Weiru Wang, Yingbo Li, Bruce Ganem, and Steven E. Ealick. "Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase." Acta Crystallographica Section D Biological Crystallography 61, no. 11 (2005): 1449–58. http://dx.doi.org/10.1107/s0907444905025503.

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37

Štefanić, Zoran, Ivana Leščić Ašler, Goran Mikleušević, and Marija Luić. "Structural investigations of purine nucleoside phosphorylase fromHelicobacter pyloriI." Acta Crystallographica Section A Foundations and Advances 71, a1 (2015): s234. http://dx.doi.org/10.1107/s2053273315096461.

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38

Luić, Marija, Karolina Gucunski, Ivana Leščić Ašler, and Zoran Štefanić. "Structural investigations of purine nucleoside phosphorylase fromHelicobacter pyloriII." Acta Crystallographica Section A Foundations and Advances 71, a1 (2015): s204. http://dx.doi.org/10.1107/s2053273315096941.

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39

Jenuth, Jack P., Floyd F. Snyder, and John L. Portis. "Nucleotide sequence of murine purine nucleoside phosphorylase cDNA." Nucleic Acids Research 19, no. 7 (1991): 1708. http://dx.doi.org/10.1093/nar/19.7.1708.

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40

Bzowska, A., L. Pogosjan, A. V. Ananiev, E. Kulikowska, and D. Shugar. "Substrate/Inhibitor Properties of Tumour Purine Nucleoside Phosphorylase." Nucleosides, Nucleotides and Nucleic Acids 14, no. 3 (1995): 517–20. http://dx.doi.org/10.1080/15257779508012416.

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41

Liao, Pu, Ana Toro, Weixian Min, Shaun Lee, Chaim M. Roifman, and Eyal Grunebaum. "Lentivirus gene therapy for purine nucleoside phosphorylase deficiency." Journal of Gene Medicine 10, no. 12 (2008): 1282–93. http://dx.doi.org/10.1002/jgm.1261.

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42

Montgomery, John A. "Purine nucleoside phosphorylase: A target for drug design." Medicinal Research Reviews 13, no. 3 (1993): 209–28. http://dx.doi.org/10.1002/med.2610130302.

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43

Nakamura, Charles, Shih-Hsi Chu, Johanna Stoeckler, and Robert Parks. "Inhibition of Purine Nucleoside Phosphorylase by Phosphonoalkylpurines 1." Nucleosides, Nucleotides and Nucleic Acids 8, no. 5 (1989): 1039–40. http://dx.doi.org/10.1080/07328318908054271.

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44

Parvaneh, Nima, Mahmoud-Reza Ashrafi, Mehdi Yeganeh, Nima Pouladi, Fatemeh Sayarifar, and Leila Parvaneh. "Progressive multifocal leukoencephalopathy in purine nucleoside phosphorylase deficiency." Brain and Development 29, no. 2 (2007): 124–26. http://dx.doi.org/10.1016/j.braindev.2006.07.008.

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45

Chang, Chi-Hsiung, L. Lee Benneett, and R. W. Brockman. "A new isotopic assay for purine nucleoside phosphorylase." Analytical Biochemistry 183, no. 2 (1989): 279–82. http://dx.doi.org/10.1016/0003-2697(89)90480-6.

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46

Canduri, Fernanda, Valmir Fadel, Luiz Augusto Basso, Mário Sérgio Palma, Diógenes Santiago Santos, and Walter Filgueira de Azevedo. "New catalytic mechanism for human purine nucleoside phosphorylase." Biochemical and Biophysical Research Communications 327, no. 3 (2005): 646–49. http://dx.doi.org/10.1016/j.bbrc.2004.12.052.

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47

Pant, Pradeep, Amita Pathak, and B. Jayaram. "Symmetric Nucleosides as Potent Purine Nucleoside Phosphorylase Inhibitors." Journal of Physical Chemistry B 125, no. 11 (2021): 2856–62. http://dx.doi.org/10.1021/acs.jpcb.0c10553.

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48

Albar, Rawia, Alaa Alesa, Dina Saqa, Jamanah Abdulaziz, Mohammad Batouk, and Abdullah Alesa. "Purine Nucleoside Phosphorylase (PNP) Deficiency: A Case Report." Egyptian Journal of Hospital Medicine 81, no. 5 (2020): 1967–69. http://dx.doi.org/10.21608/ejhm.2020.123480.

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49

Tomoki, Hamamoto, Noguchi Toshitada, and Midorikawa Yuichiro. "Purification and Characterization of Purine Nucleoside Phosphorylase and Pyrimidine Nucleoside Phosphorylase fromBacillus stearothermophilusTH 6-2." Bioscience, Biotechnology, and Biochemistry 60, no. 7 (1996): 1179–80. http://dx.doi.org/10.1271/bbb.60.1179.

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50

Mably, Ellen R., Ernest Fung, and Floyd F. Snyder. "Genetic deficiency of purine nucleoside phosphorylase in the mouse. Characterization of partially and severely enzyme deficient mutants." Genome 32, no. 6 (1989): 1026–32. http://dx.doi.org/10.1139/g89-547.

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Two independent mutations of purine nucleoside phosphorylase were identified in the first-generation progeny of male mice that had been treated with the mutagen N-ethylnitrosourea and mated to untreated females. The common allele in inbred strains is Np-1a and the mutants are assigned the gene symbols Np-1e and Np-1f. Heterozygotes had approximately half normal purine nucleoside phosphorylase activity in erythrocytes and activity of homozygotes was 17 and 5% of NP-1A for NP-1E and NP-1F, respectively. The following properties are consistent with both Np-1e and Np-1f being point mutations: the

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