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Journal articles on the topic 'Ornithine Ornithine decarboxylase. Fluorination'

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Published: 4 June 2021

Last updated: 3 February 2022

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1

Stefanelli, Claudio, Carmen Rossoni, Fabrizia Ferrari, Flavio Flamigni, and Claudio M. Caldarera. "Ornithine decarboxylase and ornithine decarboxylase-inhibiting activity in rat thymocytes." Cell Biochemistry and Function 10, no. 4 (1992): 243–50. http://dx.doi.org/10.1002/cbf.290100406.

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2

Wen, L., J. K. Huang, and P. J. Blackshear. "Rat Ornithine Decarboxylase Gene." Journal of Biological Chemistry 264, no. 15 (1989): 9016–21. http://dx.doi.org/10.1016/s0021-9258(18)81896-8.

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3

Evans, G. O. "More on ornithine decarboxylase." Clinical Chemistry 35, no. 5 (1989): 897–98. http://dx.doi.org/10.1093/clinchem/35.5.897a.

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4

Pegg, Anthony E. "Regulation of Ornithine Decarboxylase." Journal of Biological Chemistry 281, no. 21 (2006): 14529–32. http://dx.doi.org/10.1074/jbc.r500031200.

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5

Rustgi, A. K. "Ornithine decarboxylase: An oncogene?" Gastroenterology 105, no. 4 (1993): 1255–56. http://dx.doi.org/10.1016/0016-5085(93)90980-q.

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6

Fonzi, W. A., and P. S. Sypherd. "Expression of the gene for ornithine decarboxylase of Saccharomyces cerevisiae in Escherichia coli." Molecular and Cellular Biology 5, no. 1 (1985): 161–66. http://dx.doi.org/10.1128/mcb.5.1.161.

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Diploid cells of Saccharomyces cerevisiae homozygous for the spe1A mutation, which eliminates ornithine decarboxylase activity, were found to sporulate at a greatly reduced frequency in the absence of polyamines. Plasmids which complement the spe1A mutation were isolated by their ability to restore sporulation competence to these cells. Three distinct plasmids were isolated. Each plasmid insert overlapped the same 8.0-kilobase region, and each plasmid restored ornithine decarboxylase activity to spe1A mutants. These plasmids also conferred ornithine decarboxylase activity to Escherichia coli E

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7

Fonzi, W. A., and P. S. Sypherd. "Expression of the gene for ornithine decarboxylase of Saccharomyces cerevisiae in Escherichia coli." Molecular and Cellular Biology 5, no. 1 (1985): 161–66. http://dx.doi.org/10.1128/mcb.5.1.161-166.1985.

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Diploid cells of Saccharomyces cerevisiae homozygous for the spe1A mutation, which eliminates ornithine decarboxylase activity, were found to sporulate at a greatly reduced frequency in the absence of polyamines. Plasmids which complement the spe1A mutation were isolated by their ability to restore sporulation competence to these cells. Three distinct plasmids were isolated. Each plasmid insert overlapped the same 8.0-kilobase region, and each plasmid restored ornithine decarboxylase activity to spe1A mutants. These plasmids also conferred ornithine decarboxylase activity to Escherichia coli E

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8

Halmekytö, M., J. M. Hyttinen, R. Sinervirta, P. Leppänen, J. Jänne, and L. Alhonen. "Regulation of the expression of human ornithine decarboxylase gene and ornithine decarboxylase promoter-driven reporter gene in transgenic mice." Biochemical Journal 292, no. 3 (1993): 927–32. http://dx.doi.org/10.1042/bj2920927.

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We have studied the regulation of the expression of ornithine decarboxylase with the aid of transgenic mice harbouring either functional human ornithine decarboxylase genes or the mouse ornithine decarboxylase promoter-driven chloramphenicol acetyltransferase fusion gene in their genome. We used three different stimuli which are well known to enhance ornithine decarboxylase activity in their appropriate target tissues: (i) testosterone in female kidney, (ii) a phorbol ester in epidermis and (iii) partial hepatectomy in liver. Endogenous mouse ornithine decarboxylase activity was strikingly sti

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9

Levillain, Olivier, Jean-Jacques Diaz, Isabelle Reymond, and Denis Soulet. "Ornithine metabolism along the female mouse nephron: localization of ornithine decarboxylase and ornithine aminotransferase." Pflügers Archiv - European Journal of Physiology 440, no. 5 (2000): 761–69. http://dx.doi.org/10.1007/s004240000340.

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10

DANZIN, Charles, and Lo PERSSON. "l-Ornithine-induced inactivation of mammalian ornithine decarboxylase in vitro." European Journal of Biochemistry 166, no. 1 (1987): 45–48. http://dx.doi.org/10.1111/j.1432-1033.1987.tb13481.x.

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11

GHODA, LUCY, C. C. WANG, and PHILIP COFFINO. "Ornithine decarboxylase of African trypanosomes." Biochemical Society Transactions 18, no. 5 (1990): 739–40. http://dx.doi.org/10.1042/bst0180739.

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12

Schipper, Raymond G., Nadine Romain, Adrianus A. Otten, Jing Tan, Will P. Lange, and Albert A. J. Verhofstad. "Immunocytochemical Detection of Ornithine Decarboxylase." Journal of Histochemistry & Cytochemistry 47, no. 11 (1999): 1395–404. http://dx.doi.org/10.1177/002215549904701106.

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13

Carakostas, M. C. "What is serum ornithine decarboxylase?" Clinical Chemistry 34, no. 12 (1988): 2606–7. http://dx.doi.org/10.1093/clinchem/34.12.2606.

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14

San-Blas, Gioconda, Françoise Sorais, Felipe San-Blas, and José Ruiz-Herrera. "Ornithine decarboxylase in Paracoccidioides brasiliensis." Archives of Microbiology 165, no. 5 (1996): 311–16. http://dx.doi.org/10.1007/s002030050332.

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15

Berezov, T. T. "Ornithine decarboxylase and malignant growth." Bulletin of Experimental Biology and Medicine 115, no. 6 (1993): 667–69. http://dx.doi.org/10.1007/bf00791153.

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16

Persson, L., E. Lövkvist Wallström, S. Nasizadeh, et al. "Regulation of mammalian ornithine decarboxylase." Biochemical Society Transactions 26, no. 4 (1998): 575–79. http://dx.doi.org/10.1042/bst0260575.

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17

Ngo, That T., Kurt L. Brillhart, Rowland H. Davis, et al. "Spectrophotometric assay for ornithine decarboxylase." Analytical Biochemistry 160, no. 2 (1987): 290–93. http://dx.doi.org/10.1016/0003-2697(87)90049-2.

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18

Lobo, C., I. Núñez de Castro, and F. J. Alonso. "In SituMicroassay of Ornithine Decarboxylase." Analytical Biochemistry 238, no. 1 (1996): 95–96. http://dx.doi.org/10.1006/abio.1996.0257.

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19

Seely, J. E., L. Persson, G. J. Sertich, and A. E. Pegg. "Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney." Biochemical Journal 226, no. 2 (1985): 577–86. http://dx.doi.org/10.1042/bj2260577.

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Comparisons were made of ornithine decarboxylase isolated from Morris hepatoma 7777, thioacetamide-treated rat liver and androgen-stimulated mouse kidney. The enzymes from each source were purified in parallel and their size, isoelectric point, interaction with a monoclonal antibody or a monospecific rabbit antiserum to ornithine decarboxylase, and rates of inactivation in vitro, were studied. Mouse kidney, which is a particularly rich source of ornithine decarboxylase after androgen induction, contained two distinct forms of the enzyme which differed slightly in isoelectric point, but not in

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20

Dempsey, Robert J., Bruce E. Maley, David Cowen, and Jack W. Olson. "Ornithine Decarboxylase Activity and Immunohistochemical Location in Postischemic Brain." Journal of Cerebral Blood Flow & Metabolism 8, no. 6 (1988): 843–47. http://dx.doi.org/10.1038/jcbfm.1988.141.

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Ornithine decarboxylase, rate-limiting in polyamine formation, has been found to be necessary for the development of vasogenic edema after cryogenic cerebral injury and is postulated to be of importance in late ischemic brain edema formation. Ornithine decarboxylase activity and accompanying edema was studied after transient cerebral ischemia in Mongolian gerbils. Bilateral carotid artery occlusion was utilized to produce dense forebrain ischemia. After 4 h of reperfusion a significant elevation in ornithine decarboxylase activity was present (72.5 ± 24.7 vs 8.5 ± 2 pmoles/mg protein/h, p <

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21

Bassez, T., J. Paris, F. Omilli, C. Dorel, and H. B. Osborne. "Post-transcriptional regulation of ornithine decarboxylase in Xenopus laevis oocytes." Development 110, no. 3 (1990): 955–62. http://dx.doi.org/10.1242/dev.110.3.955.

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The level at which ornithine decarboxylase expression is regulated in growing oocytes has been investigated. Immunoprecipitation of the in vivo labelled proteins showed that ornithine decarboxylase accumulated less rapidly in stage IV oocytes than in previtellogenic stage I + II oocytes. Quantitative Northern analysis showed that ornithine decarboxylase mRNA is abundant in oocytes (about 8 × 10(8) transcripts/cell) and this number does not significantly change during oogenesis. Polysome analysis showed that this mRNA is present in polysomes in stage I + II oocytes but has passed into puromycin

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22

Schaeffer, J. M., and M. R. Donatelli. "Characterization of a high-affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans." Biochemical Journal 270, no. 3 (1990): 599–604. http://dx.doi.org/10.1042/bj2700599.

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Ornithine decarboxylase has been identified and characterized in the free-living nematode Caenorhabditis elegans. Unlike previously described ornithine decarboxylases, the enzyme activity is membrane-associated and remains in the membrane fraction after treatment with high salt, detergents or phosphatidylinositol-specific phospholipase C. Ornithine has an apparent Km value of 2.7 microM for ornithine decarboxylase. The enzyme is competitively inhibited by arginine and lysine with Ki values of 4.0 and 24.4 microM respectively. None of the other naturally occurring amino acids inhibited more tha

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23

Sertich, G. J., L. Persson, and A. E. Pegg. "Regulation of ovarian ornithine decarboxylase by human chorionic gonadotrophin." American Journal of Physiology-Cell Physiology 253, no. 5 (1987): C687—C692. http://dx.doi.org/10.1152/ajpcell.1987.253.5.c687.

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Treatment of 29-day-old female Sprague-Dawley rats with human chorionic gonadotrophin (hCG) produced a large and rapid increase in the activity of ornithine decarboxylase. Measurements that use a specific radioimmunoassay showed that the increased activity could be accounted for by a parallel change in the amount of ornithine decarboxylase protein. The increased protein content was caused by an increased rate of synthesis, since the half-life of ornithine decarboxylase was not changed by the hormone treatment. The content of mRNA for ornithine decarboxylase was determined by hybridization with

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24

Morrison, R. F., and E. R. Seidel. "Cell spreading and the regulation of ornithine decarboxylase." Journal of Cell Science 108, no. 12 (1995): 3787–94. http://dx.doi.org/10.1242/jcs.108.12.3787.

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The aim of this study was to investigate the effect of cell spreading on the induction of ornithine decarboxylase and the rate of putrescine uptake in anchorage-dependent and anchorage-independent cells. Plating non-transformed IEC-6 epithelial cells at high versus low cell density restricted cell spreading from 900 microns 2 to approximately 140 microns 2, blunted the transient induction of ornithine decarboxylase activity from 202 to 32 pmol 14CO2/mg protein per hour and reduced the rate of [14C] putrescine uptake from 46 to 23 pmol/10(5) cells per hour. The mean spreading area of the cell p

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25

Mayer, M. J. "Polyamine Homeostasis in Transgenic Plants Overexpressing Ornithine Decarboxylase Includes Ornithine Limitation." Journal of Biochemistry 134, no. 5 (2003): 765–72. http://dx.doi.org/10.1093/jb/mvg205.

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26

Correa-Basurto, J., L. Rodríguez-Páez, E. S. Aguiar-Moreno, et al. "Computational and experimental evaluation of ornithine derivatives as ornithine decarboxylase inhibitors." Medicinal Chemistry Research 18, no. 1 (2008): 20–30. http://dx.doi.org/10.1007/s00044-008-9103-6.

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27

Canellakis, E. S., D. A. Kyriakidis, C. A. Rinehart, S. C. Huang, C. Panagiotidis, and W. F. Fong. "Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth." Bioscience Reports 5, no. 3 (1985): 189–204. http://dx.doi.org/10.1007/bf01119588.

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This review considers the role of antizyme, of amino acids and of protein synthesis in the regulation of polyamine biosynthesis.The ornithine decarboxylase of eukaryotic ceils and of Escherichia coli coli can be non-competitively inhibited by proteins, termed antizymes, which are induced by di-and poly- amines. Some antizymes have been purified to homogeneity and have been shown to be structurally unique to the cell of origin. Yet, the E. coli antizyme and the rat liver antizyme cross react and inhibit each other's biosynthetic decarboxylases. These results indicate that aspects of the control

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28

Yarlett, N., B. Goldberg, M. A. Moharrami, and C. J. Bacchi. "Trichomonas vaginalis: characterization of ornithine decarboxylase." Biochemical Journal 293, no. 2 (1993): 487–93. http://dx.doi.org/10.1042/bj2930487.

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Ornithine decarboxylase (ODC), the lead enzyme in polyamine biosynthesis, was partially purified from Trichomonas vaginalis and its kinetic properties were studied. The enzyme appears to be of special significance in this anaerobic parasite, since the arginine dihydrolase pathway generates ATP as well as putrescine from arginine. ODC from T. vaginalis had a broad substrate specificity, decarboxylating ornithine (100%), lysine (1.0%) and arginine (0.1%). The enzyme had a pH optimum of 6.5, a temperature optimum of 37 degrees C and was pyridoxal 5′-phosphate-dependent. Attempts to separate ornit

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29

Persson, L. "Ornithine decarboxylase and S-adenosylmethionine decarboxylase in trypanosomatids." Biochemical Society Transactions 35, no. 2 (2007): 314–17. http://dx.doi.org/10.1042/bst0350314.

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The production of polyamines has been shown to be an effective target for a drug against the West African form of sleeping sickness caused by Trypanosoma brucei gambiense. T. brucei belongs to the group of protozoan parasites classed as trypanosomatids. Parasitic species of this group are the causative agents of various tropical diseases besides African sleeping sickness, e.g. Chagas' disease (Trypanosoma cruzi), cutaneous (Lesihmania spp.) and visceral (Leishmania donovani) leishmaniasis. The metabolism of polyamines in the parasites is a potential target for the development of new drugs for

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30

Gebauer, P. H., M. Turzo, F. Lasitschka, M. A. Weigand, and C. J. Busch. "Inhibition of ornithine decarboxylase restores hypoxic pulmonary vasoconstriction in endotoxemic mice." Pulmonary Circulation 10, no. 4 (2020): 204589402091583. http://dx.doi.org/10.1177/2045894020915831.

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Endotoxemia impairs hypoxic pulmonary vasoconstriction which leads to systemic hypoxemia. This derogation is attributable to increased activity of nitric oxide synthase 2 and arginase metabolism. Gene expression analysis has shown increased expression of ornithine decarboxylase in lungs of endotoxemic mice, a downstream enzyme of arginase metabolism. The aim of this study was to investigate whether inhibition of ornithine decarboxylase increases hypoxic pulmonary vasoconstriction in lungs of endotoxemic mice. Mice received lipopolysaccharides or saline intraperitoneal, and hypoxic pulmonary va

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31

Dodds, R. A., A. A. Pitsillides, and G. T. Frost. "A quantitative cytochemical method for ornithine decarboxylase activity." Journal of Histochemistry & Cytochemistry 38, no. 1 (1990): 123–27. http://dx.doi.org/10.1177/38.1.2104632.

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Although decarboxylases, particularly ornithine decarboxylase, are of considerable importance in cell metabolism, it has been impossible to demonstrate their activity histochemically, as this depends on trapping carbon dioxide at neutral pH values. A new reagent, lead hydroxyisobutyrate, has been shown capable of such trapping. It has been applied to the demonstration of ornithine decarboxylase activity in mouse kidney. Optimal concentrations of substrate, co-factor and trapping agent, as well as the pH optimum, have been determined for cryostat sections stabilized with a collagen polypeptide.

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32

Lu, L., B. A. Stanley, and A. E. Pegg. "Identification of residues in ornithine decarboxylase essential for enzymic activity and for rapid protein turnover." Biochemical Journal 277, no. 3 (1991): 671–75. http://dx.doi.org/10.1042/bj2770671.

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The importance of certain amino acid residues in mammalian ornithine decarboxylase activity and degradation was studied by site-specific mutagenesis. Changes were made to the mouse ornithine decarboxylase cDNA in a plasmid containing a T7 RNA polymerase promoter. The plasmid was then used for the synthesis of RNA, which was translated in a reticulocyte lysate system. The activity of the ornithine decarboxylase formed and the stability of the protein to degradation in a reticulocyte lysate system were determined. Changes of lysine-169 or of histidine-197 to alanine completely abolished enzyme a

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33

Tsirka, S., and P. Coffino. "Dominant negative mutants of ornithine decarboxylase." Journal of Biological Chemistry 267, no. 32 (1992): 23057–62. http://dx.doi.org/10.1016/s0021-9258(18)50055-7.

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34

Badolo, Lassina, Jacques Dubois, Marianne Helson-Cambier, and Michel Hanocq. "Inhibition of ornithine decarboxylase by ifenprodil." European Journal of Pharmacology 342, no. 2-3 (1998): R1—R2. http://dx.doi.org/10.1016/s0014-2999(97)01601-4.

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35

YOSHIDA, TAKEMI, and YUKIO KUROIWA. "Ornithine decarboxylase: Its significance in toxicology." Eisei kagaku 32, no. 2 (1986): 57–69. http://dx.doi.org/10.1248/jhs1956.32.57.

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36

Dempsey, R. J., M. S. Kindy, and J. M. Carney. "Ornithine Decarboxylase Expression in the Brain." Neurosurgery 30, no. 5 (1992): 804. http://dx.doi.org/10.1097/00006123-199205000-00040.

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37

Toth, Charles, and Philip Coffino. "Regulated Degradation of Yeast Ornithine Decarboxylase." Journal of Biological Chemistry 274, no. 36 (1999): 25921–26. http://dx.doi.org/10.1074/jbc.274.36.25921.

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38

Dempsey, R. J., M. S. Kindy, and J. M. Carney. "Ornithine Decarboxylase Expression in the Brain." Neurosurgery 30, no. 5 (1992): 804. http://dx.doi.org/10.1227/00006123-199205000-00040.

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39

Ackermann, Joseph M., Sreenivas Kanugula, and Anthony E. Pegg. "DNAzyme-Mediated Silencing of Ornithine Decarboxylase†." Biochemistry 44, no. 6 (2005): 2143–52. http://dx.doi.org/10.1021/bi047918d.

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40

ASTANCOLLE, S., F. BACCIOTTINI, P. DAVALLI, G. PICCININI, A. CASTI, and A. CORTI. "Ornithine decarboxylase in perfused rat heart." Journal of Molecular and Cellular Cardiology 18, no. 3 (1986): 223–30. http://dx.doi.org/10.1016/s0022-2828(86)80404-7.

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41

D'Orazi, Dario, and Nello Bagni. "Ornithine decarboxylase activity in Helianthus tuberosus." Physiologia Plantarum 71, no. 2 (1987): 177–83. http://dx.doi.org/10.1111/j.1399-3054.1987.tb02864.x.

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42

Dircks, Lori, Ann Grens, Thelma C. Slezynger, and Immo E. Scheffler. "Posttranscriptional regulation of ornithine decarboxylase activity." Journal of Cellular Physiology 126, no. 3 (1986): 371–78. http://dx.doi.org/10.1002/jcp.1041260307.

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43

Kern, Andrew, Marcos A. Oliveira, Ning-Leh Chang, et al. "Crystallization of a mammalian ornithine decarboxylase." Proteins: Structure, Function, and Genetics 24, no. 2 (1996): 266–68. http://dx.doi.org/10.1002/(sici)1097-0134(199602)24:2<266::aid-prot15>3.0.co;2-l.

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44

Ichiba, T., S. Matsufuji, Y. Miyazaki, et al. "Functional Regions of Ornithine Decarboxylase Antizyme." Biochemical and Biophysical Research Communications 200, no. 3 (1994): 1721–27. http://dx.doi.org/10.1006/bbrc.1994.1651.

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45

Nishiyama, Masaki, Senya Matsufuji, Ryuhei Kanamoto, Yasuko Murakami, and Shin-Ichi Hayashi. "Sandwich Enzyme Immunoassay for Ornithine Decarboxylase." Journal of Immunoassay 10, no. 1 (1989): 19–35. http://dx.doi.org/10.1080/01971528908053225.

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46

Ruan, Yibing, Min Cheng, Young Ou, Richard Oko, and Frans A. van der Hoorn. "Ornithine Decarboxylase AntizymeOaz3Modulates Protein Phosphatase Activity." Journal of Biological Chemistry 286, no. 33 (2011): 29417–27. http://dx.doi.org/10.1074/jbc.m111.274647.

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47

Heby, Olle. "Ornithine decarboxylase as target of chemotheraphy." Advances in Enzyme Regulation 24 (January 1985): 103–24. http://dx.doi.org/10.1016/0065-2571(85)90072-x.

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48

Tetzlaff, Wolfram, and Georg W. Kreutzberg. "Ornithine decarboxylase in motoneurons during regeneration." Experimental Neurology 89, no. 3 (1985): 679–88. http://dx.doi.org/10.1016/0014-4886(85)90016-0.

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49

Calvo-Méndez, C., J. C. Villagómez-Castro, and E. López-Romero. "Ornithine decarboxylase activity in Entamoeba invadens." International Journal for Parasitology 23, no. 7 (1993): 847–52. http://dx.doi.org/10.1016/0020-7519(93)90048-4.

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50

Autelli, Riccardo, Ingvar Holm, Olle Heby, and Lo Persson. "Feedback regulation of ornithine decarboxylase expression." FEBS Letters 260, no. 1 (1990): 39–41. http://dx.doi.org/10.1016/0014-5793(90)80060-v.

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