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Relevant bibliographies by topics / Ornithine Ornithine decarboxylase

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Academic literature on the topic 'Ornithine Ornithine decarboxylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Ornithine Ornithine decarboxylase"

1

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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2

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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3

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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4

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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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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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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7

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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8

Romano, Andrea, Hein Trip, Aline Lonvaud-Funel, Juke S. Lolkema, and Patrick M. Lucas. "Evidence of Two Functionally Distinct Ornithine Decarboxylation Systems in Lactic Acid Bacteria." Applied and Environmental Microbiology 78, no. 6 (2012): 1953–61. http://dx.doi.org/10.1128/aem.07161-11.

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ABSTRACTBiogenic amines are low-molecular-weight organic bases whose presence in food can result in health problems. The biosynthesis of biogenic amines in fermented foods mostly proceeds through amino acid decarboxylation carried out by lactic acid bacteria (LAB), but not all systems leading to biogenic amine production by LAB have been thoroughly characterized. Here, putative ornithine decarboxylation pathways consisting of a putative ornithine decarboxylase and an amino acid transporter were identified in LAB by strain collection screening and database searches. The decarboxylases were prod

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9

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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10

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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Dissertations / Theses on the topic "Ornithine Ornithine decarboxylase"

1

Lövkvist, Wallström Eva. "On the regulation of ornithine decarboxylase." Lund : Lund University, 1998. http://catalog.hathitrust.org/api/volumes/oclc/68945009.html.

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Kern, Andrew David. "Structure of ornithine decarboxylase from mouse /." Digital version accessible at:, 1999. http://wwwlib.umi.com/cr/utexas/main.

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De, Villiers Jandré. "Attempted routes towards the synthesis of fluorinated analogues of ornithine as potential inhibitors of ornithine decarboxylase /." Link to the online version, 2007. http://hdl.handle.net/10019/417.

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Parsanejad, Reza. "Phosphoenolpyruvate carboxykinase and ornithine decarboxylase genes : allelic variations and associations with traits in poultry." Thesis, McGill University, 2003. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=84307.

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The objectives of this study were to identify genetic variants, develop the respective haplotypes (combination of alleles) and investigate the association of identified variants with economically important traits in two candidate genes. The first gene was Phosphoenolpyruvate carboxykinase (PEPCK) which is a key regulatory enzyme of gluconeogenesis. The second candidate gene, Ornithine decarboxylase (ODC), is a rate-limiting enzyme in polyamine biosynthesis. It has a significant role in DNA synthesis and cell proliferation. We first analyzed the genetic variability of PEPCK-C, the gene w

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Chu, Yi-wen 1962. "Amino acid sequence requirements for ornithine decarboxylase activity." Thesis, The University of Arizona, 1988. http://hdl.handle.net/10150/276838.

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ODC activity of the altered proteins was measured and compared to that of the full length 461 amino acid containing ODC. Mouse ODC cDNA sequences were deleted from either 5' or 3' ends using exonuclease III and Mung Bean nuclease treatments. An internal deletion was obtained by Hinc II and Bcl I restriction endonuclease digestion of the full length ODC cDNA. Capped mRNAs were synthesized in vitro using the resulting deleted DNA as templates, and the protein was translated in vitro. The results indicate that the protein in which translation initiates at internal AUG start codons does not have a

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Tome, Margaret Ellen. "Cellular and biochemical consequences of ornithine decarboxylase regulation." Diss., The University of Arizona, 1996. http://hdl.handle.net/10150/282137.

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The polyamines are abundant polycations necessary for eucaryotic cell growth. Ornithine decarboxylase (ODC), the first and often rate-limiting enzyme in polyamine biosynthesis, is responsible for the formation of putrescine, the precursor for polyamine synthesis. ODC is normally very tightly regulated by a complex interaction of control of both synthesis and degradation. Regulation of ODC synthesis allows cells to increase ODC in response to various stimuli; however, the importance of the rapid degradation of ODC in cellular metabolism is less well understood. The studies presented here have c

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De, Villiers Jandre. "Attempted routes towards the synthesis of fluorinated analogues of ornithine as potential inhibitors of ornithine decarboxylase." Thesis, Stellenbosch : University of Stellenbosch, 2007. http://hdl.handle.net/10019.1/3096.

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Thesis (MSc (Chemistry and Polymer Science))--University of Stellenbosch, 2007.<br>Human African Trypanosomiasis (HAT) is a disease that threatens more then 60 million men, woman and children in Africa. It is known that the inhibition of the enzyme, ornithine decarboxylase (ODC) leads to cell arrest and subsequent death of Trypanosoma brucei, the parasite that causes the disease. The fluorinated ornithine analogue, DFMO (difluoromethylornithine or eflornithine) is a known inhibitor of ODC. Although various syntheses for DFMO exist they have some practical drawbacks which prevent the cost

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Nancarrow, Michelle Jane. "The role of polyamines in cellular and molecular events in the wool follicle." Title page, contents and abstract only, 1995. http://web4.library.adelaide.edu.au/theses/09PH/09phn1756.pdf.

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Bibliography: leaves 255-280. In vivo and in vitro investigations of the hypothesis that polyamines and their synthetic enzymes have a role in regulation of cellular and molecular processes in the follicle. The activity of ornithine decarboxylase (ODC), the rate limiting polyamine biosynthetic enzyme, is demonstrated in wool follicle homogenates.

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9

Laitinen, Päivi. "Antizyme in the regulation of mouse brain ornithine decarboxylase." Oulu : University of Oulu, 1986. http://catalog.hathitrust.org/api/volumes/oclc/16882622.html.

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10

Zhang, Ling 1962. "Molecular cloning and characterization of the chicken ornithine decarboxylase gene." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=22831.

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Ornithine decarboxylase (ODC) is the rate determining enzyme in the biosynthesis of polyamines which are essential for cell growth. In chickens, significantly higher bioactivity is reported in broiler than in egg layer strains of chickens (Bulfield et al., 1988). To characterize the genetic differences in growth rates and ODC levels in chickens, an ODC cDNA and genomic gene were cloned and sequenced. Sequencing of ODC cDNA revealed that this clone (pODZ3: 2,052 bp) was not a full length of ODC cDNA and contained 2 putative introns. The open reading frame (introns deleted) coded for a protein o

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Books on the topic "Ornithine Ornithine decarboxylase"

1

Hoskin, Nathan. Polyamines and ornithine decarboxylase in carcinogenesis and neoplasia. U.S. Dept. of Health and Human Services, Public Health Service, National Institutes of Health, National Cancer Institute, International Cancer Research Data Bank, 1988.

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2

Wensing, Enrico J. Ribonucleotide reductase and ornithine decarboxylase mRNA expression in hydroxyurea resistant and cell cycle synchronized mammalian cells. National Library of Canada = Bibliothèque nationale du Canada, 1993.

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3

Hermon, Dowling R., Fölsch U. R, and Löser C, eds. Polyamines in the gastrointestinal tract: Proceedings of the 62nd Falk Symposium held in Titisee/Black Forest, Germany, October 6-8, 1991. Kluwer Academic Publishers, 1992.

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Ornithine decarboxylase: Biology, enzymology, and molecular genetics. Pergamon, 1989.

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Shin-ichi, Hayashi, ed. Ornithine decarboxylase: Biology, enzymology, and molecular genetics. Pergamon Press, 1989.

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Hayashi, Shin-Ichi. Ornithine Decarboxylase: Biology, Enzymology, and Molecular Genetics (International Encyclopedia of Pharmacology and Therapeutics, Section 129). Pergamon, 1989.

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Hayashi, Shin-Ichi. Ornithine Decarboxylase: Biology, Enzymology, and Molecular Genetics (International Encyclopedia of Pharmacology and Therapeutics, Section 129). Pergamon, 1989.

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Polyamines in the Gastrointestinal Tract (Falk Symposium). Springer, 1992.

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Book chapters on the topic "Ornithine Ornithine decarboxylase"

1

Schomburg, Dietmar, and Margit Salzmann. "Ornithine decarboxylase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_15.

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2

Coffino, Philip. "Degradation of Ornithine Decarboxylase." In Ubiquitin and the Biology of the Cell. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1922-9_14.

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3

Persson, Lo. "Regulation of Ornithine Decarboxylase Expression." In Polyamine Cell Signaling. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-145-1_23.

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Nowotarski, Shannon L., Sofia Origanti, and Lisa M. Shantz. "Posttranscriptional Regulation of Ornithine Decarboxylase." In Methods in Molecular Biology. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-034-8_17.

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Hayashi, S., Y. Murakami, S. Matsufuji, M. Nishiyama, R. Kanamoto, and T. Kameji. "Studies on Ornithine Decarboxylase Antizyme." In Progress in Polyamine Research. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5637-0_3.

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Brosnan, Margaret E., and Yu-Wan Hu. "Ornithine Decarboxylase Antizyme in Mammalian Tissues." In Progress in Polyamine Research. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5637-0_4.

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Persson, Lo, and Koichi Takao. "Translational Initiation of Ornithine Decarboxylase mRNA." In Endocrine Updates. Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-6446-8_5.

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Bello-Fernandez, C., and J. L. Cleveland. "c-myc Transactivates the Ornithine Decarboxylase Gene." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-77633-5_56.

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Mitchell, J. L. A., M. F. Hicks, H. J. Chen, and J. A. Hoff. "Modifications of Ornithine Decarboxylase Induced by Phosphatases." In Progress in Polyamine Research. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5637-0_6.

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Terashima, Sinya, Yasushi Teranishi, Yutaka Hoshino, Mitumasa Ogata, Hitoshi Inoue, and Ryoichi Motoki. "Ornithine Decarboxylase Activity in Human Stomach Cancer." In Recent Advances in Management of Digestive Cancers. Springer Japan, 1993. http://dx.doi.org/10.1007/978-4-431-68252-3_45.

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Conference papers on the topic "Ornithine Ornithine decarboxylase"

1

Keough, Martin P., Karen DeFeo, Candace S. Hayes, and Susan K. Gilmour. "Abstract 2471: Immunosuppressive effect of elevated epidermal ornithine decarboxylase activity." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2471.

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Barry, Elizabeth L., Leila A. Mott, Robert S. Sandler, Dennis J. Ahnen, and John A. Baron. "Abstract 2831: Ornithine decarboxylase polymorphisms and risk of colorectal adenoma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2831.

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North, ML, N. Khanna, H. Grasemann, and JA Scott. "Ornithine Decarboxylase Inhibition in an Acute Murine Model of Allergic Inflammation." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4231.

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Schultz, Chad R., Martin C. Gruhlke, Alan J. Slusarenko, and Andre S. Bachmann. "Abstract 464: Allicin, a potent new ornithine decarboxylase inhibitor in neuroblastoma." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-464.

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Kim, Hong Im, Chad R. Schultz, Andrea L. Buras, et al. "Abstract 1242: Ornithine decarboxylase as a therapeutic target in endometrial cancer." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1242.

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Lange, Ingo, Dana-Lynn T. Koomoa, and Andre S. Bachmann. "Abstract 2495: Sepiapterin reductase interacts with Ornithine Decarboxylase and regulates neuroblastoma proliferation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2495.

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Kendzicky, Ann M., Ping Zhao, Katherine Samal, et al. "Abstract 2765: Targeting both ornithine decarboxylase and polyamine transport inhibits tumor growth in neuroblastoma." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2765.

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Lin, Bruce S., Jason A. Zell, Argyrios Ziogas, and Hoda Anton-Culver. "Abstract 3759: Meat consumption, ornithine decarboxylase gene polymorphism, and outcomes after colorectal cancer diagnosis." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3759.

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Koomoa, Dana-Lynn T., and Ingo Lange. "Abstract LB-68: MYCN-induced TRPM7 expression and channel activity occurs through a mechanism that involves ornithine decarboxylase." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-lb-68.

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Nowotarski, Shannon L., and Lisa M. Shantz. "Abstract 3161: The RNA binding protein HuR stabilizes the ornithine decarboxylase (ODC) transcript in non-melanoma skin cancer." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3161.

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Reports on the topic "Ornithine Ornithine decarboxylase"

1

Manni, Andrea. Relative Contribution of Ornithine Decarboxylase (ODC) Versus S-adenosylmethionine Decarboxylase (SAMDC) to Human Breast Cancer Progression and Development. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada408110.

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