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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 3777-3783 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 4250-4255 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 197 (1999), S. 71-78 
    ISSN: 1573-4919
    Keywords: ornithine decarboxylase ; polyamine ; translational control ; untranslated region ; CHO cells ; transfection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The polyamines are ubiquitous in nature and appear to fulfil several important functions, mostly related to growth, in the cell. The first, and often rate-limiting, step in the biosynthesis of the polyamines is catalysed by ornithine decarboxylase (ODC), which is subject to a variety of control mechanisms. The polyamines exert a strong feedback regulation of the expression - as well as the degradation of the enzyme. The regulation of ODC expression appears to occur at the translational level. The ODC mRNA contains a long GC-rich 5′ untranslated region (UTR), which has been demonstrated to hamper the translation of the mRNA. However, it has not yet been conclusively established whether this part of the mRNA fulfils any function in relation to the polyamine-mediated control of ODC synthesis. In the present study, we have used stable transgenic CHO cells, expressing either full-length ODC mRNA or 5′ UTR-truncated ODC mRNA, to elucidate the role, if any, of the 5′ UTR in the translational regulation of the enzyme by polyamines. No differences in regulatory properties were observed between the cells expressing the full-length ODC mRNA and those expressing the ODC mRNA devoid of most the 5′ UTR. The cell lines down-regulated ODC (synthesis as well as activity) to the same extent upon exposure to an excess of polyamines, demonstrating that the feedback control of ODC mRNA translation occurs by a mechanism independent of the major part of the 5′ UTR of the ODC mRNA.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4919
    Keywords: Ehrlich ascites tumor cells ; ornithine decarboxylase ; mRNA half-life ; protein turnover ; superinduction ; actinomycin D
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract When Ehrlich ascites tumor cells were stimulated to grow, their ornithine decarboxylase (ODC) activity increased 20- to 30-fold. The increase in ODC mRNA content was one order of magnitude less during the corresponding period. Likewise, the subsequent changes in ODC activity failed to show proportionality to those of the ODC mRNA content. The changes in ODC activity were not attributable to changes in ODC turnover, even though the half-life of the enzyme decreased from 56 min during the period of increasing, to 36 min during the period of decreasing ODC activity. There was no evidence of an activation-inactivation-cycle for the enzyme. In view of these findings it appears that ODC mRNA alterations are amplified mainly at the translational level. The biphasic change in ODC mRNA content was partly attributable to a change in turnover of the message, as determined after inhibition of transcription with actinomycin D. Thus, the ODC mRNA half-life was estimated to decrease from 8.7 h during the period of increasing ODC activity to 4.0 h during the period of decreasing ODC activity. Despite the inhibition of transcription by actinomycin D, there was a marked superinduction of ODC activity. Our data demonstrate that the regulation of ODC expression is a complex phenomenon, involving controls at many levels.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4919
    Keywords: diethylglyoxal bis(guanylhydrazone) ; S-adenosylmethionine decarboxylase ; polyamines ; L1210 cells ; antiproliferative effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The polyamines are cell constituents essential for growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) catalyzes a key step in the polyamine biosynthetic pathway. Methylglyoxal bis(guanylhydrazone) (MGBG) is an anti-leukemic agent with a strong inhibitory effect against AdoMetDC. However, the lack of specificity limits the usefulness of MGBG. In the present report we have used an analog of MGBG, diethylglyoxal bis(guanylhydrazone) (DEGBG), with a much greater specificity and potency against AdoMetDC, to investigate the effects of AdoMetDC inhibition on cell proliferation and polyamine metabolism in mouse L1210 leukemia cells. DEGBG was shown to effectively inhibit AdoMetDC activity in exponentially growing L1210 cells. The inhibition of AdoMetDC was reflected in a marked decrease in the cellular concentrations of spermidine and spermine. The concentration of putrescine, on the other hand, was greatly increased. Treatment with DEGBG resulted in a compensatory increase in the synthesis of AdoMetDC demonstrating an efficient feedback control. Cells seeded in the presece of DEGBG ceased to grow after a lag period of 1–2 days, indicating that the cells contained an excess of polyamines which were sufficient for one or two cell cycles in the absence of polyamine synthesis. The present results indicate that analogs of MGBG, having a greater specificity against AdoMetDC, might be valuable for studies concerning polyamines and cell proliferation.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 162 (1996), S. 113-119 
    ISSN: 1573-4919
    Keywords: polyamines ; ornithine decarboxylase ; S-adenosylmethionine decarboxylase ; Chinese hamster ovary cells ; translational regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract In the present study we have examined the regulation of the polyamine biosynthetic pathway in a cell line deficient in ornithine decarboxylase (ODC) activity. These cells were unable to grow unless polyamines were provided in their growth medium. Seeding the cells in the absence of polyamines rapidly resulted in a cellular depletion of putrescine and spermidine. Although the cells were devoid of ODC activity they were demonstrated to express an inactive ODC which was feedback regulated by polyamines in a normal manner. Cells seeded in the absence of polyamines exhibited a marked increase in ODC synthesis rate which was not correlated with an equal change in the ODC mRNA level. The synthesis of S-adenosylmethionine decarboxylase (AdoMetDC) was also increased in the cells seeded in the absence of polyamines. However, this increase was essentially explained by a change in the amount of AdoMetDC mRNA. The addition of putrescine to the growth medium appeared to stimulate the conversion of AdoMetDC proenzyme into its two subunits, indicating a physiological role of putrescine in the regulation of AdoMetDC expression.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 31 (1999), S. 507-514 
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Histamine is involved in many important biological processes such as allergic reactions, gastric acid secretion and neurotransmission. The formation of histamine is catalysed by the enzyme histidine decarboxylase. In order to understand the role of histamine in different tissues, information about the cellular localisation of the decarboxylase is important. However, the availability of antisera against the enzyme, which can be used in immunocytochemical techniques, has so far been limited, mainly due to the difficulties in purifying sufficient amounts of histidine decarboxylase from various tissues. In the present study we describe the use of antisera raised against rat recombinant histidine decarboxylase to localise the enzyme immunocytochemically in the gastric mucosa of different mammals and submammalian vertebrates. The antisera specifically stained histidine decarboxylase-immunoreactive cells in the gastric mucosa of not only rat, but also of species like frog, chicken, mouse and dog. This is the first report describing the immunocytochemical distribution of the decarboxylase in the gastric mucosa of species other than rat. These antisera are likely to become valuable tools for further studies of the immunocytochemical localisation of histidine decarboxylase.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-0878
    Keywords: Ornithine decarboxylase ; Chick embryo ; Organogenesis A ; Autoradiography ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization of ornithine decarboxylase (ODC), a key enzyme in polyamine biosynthesis and thus in cell growth, was determined in the 4.5-day-old chick embryo, using two independent methods of analysis. ODC protein was identified by indirect immunofluorescence with a monospecific ODC antibody, and catalytically active ODC was identified by autoradiography with α-(5-3H) difluoromethylornithine. Both methods revealed a basically similar distribution of ODC within the embryo. Among the organs, the brain exhibited the highest ODC levels. ODC levels were also high in spinal cord, mesonephric tubules and heart. Similar levels, but confined to limited areas, were found in liver tissue, head mesenchyme, and the oral and pharyngeal regions. Organs that exhibited high ODC levels are all engaged in rapid growth, as well as in extensive tissue remodeling and differentiation.
    Type of Medium: Electronic Resource
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  • 9
    Publication Date: 1988-12-01
    Print ISSN: 0005-2728
    Electronic ISSN: 1879-2650
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Published by Elsevier
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  • 10
    Publication Date: 2009-11-06
    Print ISSN: 1535-3893
    Electronic ISSN: 1535-3907
    Topics: Chemistry and Pharmacology
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