caa a22 4500 463186672 CHVBK 20180406164855.0 cr unu---uuuuu 170326e20070801xx s 000 0 eng 10.1007/s00726-007-0531-2 doi (NATIONALLICENCE)springer-10.1007/s00726-007-0531-2 Regulation of ornithine decarboxylase during oncogenic transformation: mechanisms and therapeutic potential [Elektronische Daten] [L. M. Shantz, V. A. Levin] Summary.: The activity of ornithine decarboxylase (ODC1), the first enzyme in polyamine biosynthesis, is induced during carcinogenesis by a variety of oncogenic stimuli. Intracellular levels of ODC and the polyamines are tightly controlled during normal cell growth, and regulation occurs at the levels of transcription, translation and protein degradation. Several known proto-oncogenic pathways appear to control ODC transcription and translation, and dysregulation of pathways downstream of ras and myc result in the constitutive elevation of ODC activity that occurs with oncogenesis. Inhibition of ODC activity reverts the transformation of cells in vitro and reduces tumor growth in several animal models, suggesting high levels of ODC are necessary for the maintenance of the transformed phenotype. The ODC irreversible inactivator DFMO has proven to be not only a valuable tool in the study of ODC in cancer, but also shows promise as a chemopreventive and chemotherapeutic agent in certain types of malignancies. Springer-Verlag, 2007 Keywords: Ornithine decarboxylase - DFMO - Oncogenic transformation - Polyamines nationallicence AdoMetDC : S-adenosylmethionine decarboxylase nationallicence AZ : antizyme nationallicence BCNU : 1,3-bis(2-chloroethyl)-1-nitrosourea nationallicence DFMO : α-difluoromethylornithine nationallicence DMBA : 7,12-dimethylbenz[a]anthracene nationallicence eIF4E : eukaryotic initiation factor 4E nationallicence ERK : extracellular-signal-regulated kinase nationallicence 5-FU : 5-fluorouracil nationallicence IFN : interferon nationallicence IRES : internal ribosome entry site nationallicence K14 : keratin 14 nationallicence MEK : mitogen-activated protein kinase kinase nationallicence mTOR : mammalian target of rapamycin nationallicence NMBA : N-nitrosomethylbenzylamine nationallicence ODC : ornithine decarboxylase nationallicence OH-BBN : N-butyl-N(4-hydroxybutyl)nitrosamine nationallicence SSAT : spermidine/spermine N1-acetyltransferase nationallicence TPA : 12-O-tetradecanoylphorbol-13-acetate nationallicence Shantz L. M. Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, PA, USA aut Levin V. A. The Department of Neuro-Oncology, University of Texas M.D. Anderson Cancer Center, Houston, TX, USA aut Amino Acids Springer-Verlag 33/2(2007-08-01), 213-223 0939-4451 33:2<213 2007 33 726 https://doi.org/10.1007/s00726-007-0531-2 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-007-0531-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shantz L. M. Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, PA, USA aut NATIONALLICENCE 700 1- Levin V. A. The Department of Neuro-Oncology, University of Texas M.D. Anderson Cancer Center, Houston, TX, USA aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 33/2(2007-08-01), 213-223 0939-4451 33:2<213 2007 33 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer