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Information on EC 4.1.1.17 - ornithine decarboxylase and Organism(s) Rattus norvegicus and UniProt Accession P09057
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4.1.1.17 ornithine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
Specify your search results
Word Map
- 4.1.1.17
- polyamine
- spermidine
- alpha-difluoromethylornithine
- carcinogenesis
- antizyme
-
chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
-
phorbol
- mucosa
- difluoromethylornithine
-
diamine
- decarboxylases
-
n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
-
antiproliferative
-
tpa-induced
- prostaglandin
- testosterone
-
3hthymidine
- tumorigenesis
-
mitogen
- cycloheximide
- c-fos
- methylglyoxal
-
tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
-
hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
-
protooncogene
- papilloma
-
7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
-
tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
-
crypt
- trypanothione
-
12-o-tetradecanoylphorbol
-
ester-induced
- actinomycin
- mezerein
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
odc, ornithine decarboxylase, ldodc, lysine/ornithine decarboxylase, s-adenosylmethionine decarboxylase/ornithine decarboxylase, ldc/odc, odc-paralogue, xodc2, adometdc/odc, ddodc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bODC
-
-
-
-
Decarboxylase, ornithine
-
-
-
-
ODC
ODC-paralogue
-
-
-
-
XODC1
-
-
-
-
XODC2
-
-
-
-
ODC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-60-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5alpha-dihydrotestosterone
?
-
administration of 0.1 mM to the heart elicits a significant increase in ornithine decarboxylase activity in the left atrium of control male rats, that tends to decrease in gonadectomized rats, the effect is significant for female rats. Testosterone plasma levels positively correlate with the gradient of modifications of ornithine decarboxylase activity elicited by 5alpha-dihydrotestosterone exposure
-
-
?
L-Orn
?
-
induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation regulation occurs at the levels of transcription, translation and protein degradation, mechanisms and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects with vindesine or doxorubicin, overview
-
-
?
L-ornithine
putrescine + CO2
-
key enzyme of polyamine biosynthesis, essential role of the polyamines in cancer cell adaptation to hypoxic stress, effects of hypoxia on the polyamine system in cancer cells, overview. Compensatory up-regulation of polyamine transport on inhibition of ODC
-
-
?
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
?
additional information
?
-
-
during liver regeneration from 70% partial hepatectomy, ODC produces newly synthesized spermidine, the inhibition of Gln-Lys bond production by the preferential formation of protein-spermidine bonds leads to an increase in DNA synthesis. Gln-Lys bond formation is catalyzed by transglutaminase 2 as a post-translational modification of proteins
-
-
?
additional information
?
-
-
ODC is the first and rate limiting enzyme in the synthesis of polyamines, which are essential for normal cell growth, the induction of the enzyme by interleukines 4 and 13 is involved in upregulation of kinases ERK, PI3K, and PKA, and in cell proliferation, overview. Dexamethasone, ERK, MEK, and PI3K pathways are involved in the regulation of ODC, overview
-
-
?
additional information
?
-
-
ornithine decarboxylase is a cancer related protein. ODC is the key enzyme in polyamine synthesis and a regulator of cell proliferation. In gastric mucosal inflammation, induced by NaHCO3 feeding, ODC expression and activity is increased correlated to enhanced cell proliferation, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5alpha-dihydrotestosterone
?
-
administration of 0.1 mM to the heart elicits a significant increase in ornithine decarboxylase activity in the left atrium of control male rats, that tends to decrease in gonadectomized rats, the effect is significant for female rats. Testosterone plasma levels positively correlate with the gradient of modifications of ornithine decarboxylase activity elicited by 5alpha-dihydrotestosterone exposure
-
-
?
L-Orn
?
-
induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation regulation occurs at the levels of transcription, translation and protein degradation, mechanisms and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects with vindesine or doxorubicin, overview
-
-
?
L-ornithine
putrescine + CO2
-
key enzyme of polyamine biosynthesis, essential role of the polyamines in cancer cell adaptation to hypoxic stress, effects of hypoxia on the polyamine system in cancer cells, overview. Compensatory up-regulation of polyamine transport on inhibition of ODC
-
-
?
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
?
additional information
?
-
-
during liver regeneration from 70% partial hepatectomy, ODC produces newly synthesized spermidine, the inhibition of Gln-Lys bond production by the preferential formation of protein-spermidine bonds leads to an increase in DNA synthesis. Gln-Lys bond formation is catalyzed by transglutaminase 2 as a post-translational modification of proteins
-
-
?
additional information
?
-
-
ODC is the first and rate limiting enzyme in the synthesis of polyamines, which are essential for normal cell growth, the induction of the enzyme by interleukines 4 and 13 is involved in upregulation of kinases ERK, PI3K, and PKA, and in cell proliferation, overview. Dexamethasone, ERK, MEK, and PI3K pathways are involved in the regulation of ODC, overview
-
-
?
additional information
?
-
-
ornithine decarboxylase is a cancer related protein. ODC is the key enzyme in polyamine synthesis and a regulator of cell proliferation. In gastric mucosal inflammation, induced by NaHCO3 feeding, ODC expression and activity is increased correlated to enhanced cell proliferation, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-Dimethylputrescine
-
none of the three isomers, meso, +, and - inhibits in vitro, but strongly inhibits in vivo in rats or in H-35 hepatoma cells
1-diethyl-2-hydroxy-2-nitroso-hydrazine
-
nitric oxide donor, inhibition via S-nitrosylation of Cys360 in the active site of ODC
antizyme
-
an important endogenous regulator of ODC and polyamine homeostasis, overview, the wild type form of ODC has an extremely short half life of 20-30 min, and its degradation is mediated by antizyme, which binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
-
Ornithine decarboxylase antizyme
-
noncompetitive with respect to Orn, plays a role in the regulation of ornithine decarboxylase in mammary gland under physiological conditions
-
peroxynitrite
-
0.1 mM, 50% inhibition, almost complete inhibition above 1 mM, nitration of tyrosine residues
alpha-difluoromethylornithine
-
i.e. DFMO, irreversible inactivator, antitumor action of ODC inhibition using DFMO, chemopreventive effects, DFMO provides significant protection against 7,12-dimethylbenz[a]-anthracene-induced mammary carcinogenesis, overview
alpha-difluoromethylornithine
-
specific and irreversible ODC inhibitor, complete inhibition at 0.1 mM
additional information
-
subcutaneous injection of 10 mg of dexamethasone/kg body weight decreases significantly the basal levels of lung ODC activity
-
additional information
-
inhibition of ODC activity reverts the transformation of cells in vitro and reduces tumor growth
-
additional information
-
serum deprivation reduces enzyme activity by 97.2% and by 87.0% in C6 cells, overview, enzyme activity is affected in primary astrocytes but not in secondary cell lines exposed to 872 MHz RF radiation, overview
-
additional information
-
ODC is inhibited by MAPK kinase, PKA, and PI3K inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ODC induction, e.g. in response to the tumor promoter 12-O-tetradecanoylphorbol-13-acetate, is a necessary step in MEK-induced tumorigenesis, ODC is induced during carcinogenesis by a variety of oncogenic stimuli, overview
-
additional information
-
carbonate ions increase the ODC enzyme expression
-
additional information
-
the enzyme is induced by interleukines 4 and 13, the induction is decreased by MAPK kinase PKA and P3IK inhibitors
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
assay for enzyme activity based on atmospheric pressure chemical ionization-mass spectrometry of dansylated putrescine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
relationship between expression level of the enzyme and mucosal proliferation, overview
analysis of expression of the cancer-related protein ornithine decarboxylase (ODC) in nontransformed gastric mucosa, relationship between expression level of the enzyme and mucosal proliferation, overview
-
AR4-2J pancreatic tumor cells, which show increased phosphorylation of the eIF4E regulatory protein 4E-BP1 and high levels of eIF4E compared to normal cells, also exhibit increased translational initiation of ODC mRNA
additional information
-
basal ornithine decarboxylase activity in isolated left atria shows differences in the four groups of animals studied, being higher in males than estrogenized females, and increased in both sexes by castration, though not significantly changed in females
additional information
immunohistochemic expression analysis of gene ODC, the ODC protein is detected mainly in the cytoplasm of the epithelial cells in all 3 groups of animals, i.e. unoperated rats, operated rats fed a normal diet, and operated rats given a carbonate-supplemented diet, also some stromal and inflammatory cells are positively stained, overview
additional information
-
immunohistochemic expression analysis of gene ODC, the ODC protein is detected mainly in the cytoplasm of the epithelial cells in all 3 groups of animals, i.e. unoperated rats, operated rats fed a normal diet, and operated rats given a carbonate-supplemented diet, also some stromal and inflammatory cells are positively stained, overview
additional information
-
immunocytochemical localization of ornithine decarboxylase
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
ornithine decarboxylase regulates the activity and localization of rhoA via polyamination, ODC activity is needed for the maintenance of rhoA at the plasma membrane
physiological function
ODC catalyzes the synthesis of putrescine from ornithine and is a rate-limiting enzyme in polyamine biosynthesis. The enzyme is involved in cell growth and its activity increases rapidly and markedly in regenerating liver after partial hepatectomy. Ornithine, which is a substrate of ODC, is a key metabolite in the urea cycle and the first precursor of the polyamine pathway, it increases progressively in the liver of partially hepatectomized rats, as a consequence of the increased flow of metabolites through the urea cycle. Polyamines, ODC-catalyzed products, play important roles in cell growth and differentiation due to the modification of proteins and are good substrates of transglutaminase 2 (TG2). TG2 and ornithine decarboxylase conversely regulate cell growth and differentiation, overview
physiological function
Ornithine decarboxylase (ODC) is the key enzyme in polyamine synthesis and a regulator of cell proliferation. ODC enhances cell proliferation in the gastric mucosa
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DCOR_RAT
461
0
51047
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
150000
-
gel filtration in presence of 10 mM sodium phosphate buffer, trimeric enzyme form
250000
-
gel filtration in presence of 1 mM sodium phosphate buffer, polymeric enzyme form
55000
-
gel filtration in presence of 0.25 M NaCl, 10 mM sodium phosphate buffer, pH 7.0, monomeric form
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
antizyme binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the wild type form of ODC has an extremely short half life of 20-30 min, and its degradation is mediated by antizyme, which binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, in presence of dithiothreitol, pyridoxal phosphate, and Tween 80 unless very dilute, stable for 2 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
carbonate ions lead to increased expression of ODC with cancer-inducing effect
partial hepatectomy/liver regeneration induces ODC enzyme expression. In retinoic acid-untreated rat, ODC activity significantly increases with a peak at 1 day after partial hepatectomy, and declines thereafter. In retinoic acid-treated rats, the peak of its activity shifts to 2 days after partial hepatectomy and the amount of its peak activity is only two-thirds of that in retinoic acid-untreated rat at 1 day after partial hepatectomy
retinoic acid suppresses ODC enzyme expression. In retinoic acid-untreated rat, ODC activity significantly increases with a peak at 1 day after partial hepatectomy, and declines thereafter. In retinoic acid-treated rats, the peak of its activity shifts to 2 days after partial hepatectomy and the amount of its peak activity is only two-thirds of that in retinoic acid-untreated rat at 1 day after partial hepatectomy
no decrease in the ODC activity is detected after treatment with 0.2 mM monodansylcadaverine or cystamine
-
ODC activity in H9c2 cells increases more than 2fold after 2 h of insulin treatment (200 nM)
-
protein kinase C stimulates polyamine biosynthesis through the induction of ornithine decarboxylase. Hearts preconditioned with three cycles of 5-min ischemia and 5-min reflow show an increase of ODC expression
-
the association of heterogenous nuclear ribonuclear protein U with c-Myc-Max complex is essential for ODC gene induction by growth stimulation
-
the state of artificial hypobiosis in rats on decrease in the body temperature to 14.4-18.0°C during 3.0-3.5 h is accompanied by an increase in the ODC activity in kidney to 200% of the control level
-
the state of artificial hypobiosis in rats on decrease in the body temperature to 14.4-18.0°C during 3.0-3.5 h is accompanied by drops in the ODC activities in the neocortex and liver by 50-60% and in rapidly proliferating tissues (thymus, spleen, and small intestine mucosa) by 80% of the control value
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Tween 80, Triton X-100 or bovine serum albumin are effective in renaturation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kitani, T.; Fujisawa, H.
Molecular properties of ornithine decarboxylase from mouse kidney. Detailed comparison with those of the enzyme from rat liver
J. Biochem.
103
547-553
1988
Mus musculus, Rattus norvegicus
Seely, J.E.; Persson, L.; Sertich, G.J.; Pegg, A.E.
Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney
Biochem. J.
226
577-586
1985
Mus musculus, Rattus norvegicus
Flamigni, F.; Guarnieri, C.; Caldarera, C.M.
Characterization of highly purified ornithine decarboxylase from rat heart
Biochim. Biophys. Acta
802
245-252
1984
Rattus norvegicus
Kitani, T.; Fujisawa, H.
Influence of salts on the activity and the subunit structure of ornithine decarboxylase from rat liver
Biochim. Biophys. Acta
784
164-167
1984
Rattus norvegicus
Hayashi, S.I.; Fujita, K.
Antizyme and antizyme inhibitor of ornithine decarboxylase (rat liver)
Methods Enzymol.
94
185-193
1983
Rattus norvegicus
Hayashi, S.I.; Kameji, T.
Ornithine decarboxylase (rat liver)
Methods Enzymol.
94
154-158
1983
Rattus norvegicus
Kitani, T.; Fujisawa, H.
Effects of detergent on ornithine decarboxylase from rat liver. Stabilization and renaturation
Eur. J. Biochem.
119
177-181
1981
Rattus norvegicus
Ono, M.; Inoue, H.; Suzuki, F.; Takeda, Y.
Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats
Biochim. Biophys. Acta
284
285-297
1972
Rattus norvegicus
Hu, Y.W.; Brosnan, M.E.
Properties of ornithine decarboxylase-antizyme from mammary gland of lactating rats
Arch. Biochem. Biophys.
254
637-641
1987
Rattus norvegicus
Kuehn, G.D.; Atmar, V.; Daniels, G.R.
Polyamine-dependent protein kinase from the slime mold Physarum polycephalum
Methods Enzymol.
94
147-154
1983
Physarum polycephalum, Rattus norvegicus
Miyamoto, K.; Oka, T.; Fujii, T.; Yamaji, M.; Minami, H.; Nakabou, Y.; Hagihira, H.
Purification and some properties of rat intestinal ornithine decarboxylase
J. Biochem.
106
167-171
1989
Rattus norvegicus
Moyano, N.; Frydman, J.; Buldain, G.; Ruiz, O.; Frydman, R.B.
Inhibition of ornithine decarboxylase by the isomers of 1,4-dimethylputrescine
J. Med. Chem.
33
1969-1974
1990
Rattus norvegicus
Persson, L.; Rosengren, E.; Sundler, F.; Uddman, R.
Immunocytochemical localization of ornithine decarboxylase
Methods Enzymol.
94
166-169
1983
Mus musculus, Rattus norvegicus
Lee, Y.S.; Cho, Y.D.
Comparison of biochemical and immunological properties between rat and Nicotiana glutinosa ornithine decarboxylase
J. Biochem. Mol. Biol.
34
408-414
2001
Rattus norvegicus (P09057), Nicotiana glutinosa (Q9FPK5)
-
Bauer, P.M.; Buga, G.M.; Fukuto, J.M.; Pegg, A.E.; Ignarro, L.J.
Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme
J. Biol. Chem.
276
34458-34464
2001
Rattus norvegicus
Bartolome, J.V.; Wang, S.; Greer, N.L.; Schanberg, S.M.
Glucocorticoid regulation of ornithine decarboxylase in the postnatal rat lung
Life Sci.
64
895-904
1999
Rattus norvegicus
Seidel, E.R.; Ragan, V.; Liu, L.
Peroxynitrite inhibits the activity of ornithine decarboxylase
Life Sci.
68
1477-1483
2001
Rattus norvegicus
Babu, G.N.; Sailor, K.A.; Beck, J.; Sun, D.; Dempsey, R.J.
Ornithine decarboxylase activity in in vivo and in vitro models of cerebral ischemia
Neurochem. Res.
28
1851-1857
2003
Rattus norvegicus
Gaboriau, F.; Havouis, R.; Groussard, K.; Moulinoux, J.P.; Lescoat, G.
Measurement of ornithine decarboxylase activity in cell extracts using mass spectrometry detection of dansylated putrescine
Anal. Biochem.
341
385-387
2005
Rattus norvegicus
Shantz, L.M.; Levin, V.A.
Regulation of ornithine decarboxylase during oncogenic transformation: mechanisms and therapeutic potential
Amino Acids
33
213-223
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Hoeytoe, A.; Juutilainen, J.; Naarala, J.
Ornithine decarboxylase activity is affected in primary astrocytes but not in secondary cell lines exposed to 872 MHz RF radiation
Int. J. Radiat. Biol.
83
367-374
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Ohtake, Y.; Maruko, A.; Ohishi, N.; Kawaguchi, M.; Satoh, T.; Ohkubo, Y.
Effect of retinoic acid on transglutaminase and ornithine decarboxylase activities during liver regeneration
Cell Biochem. Funct.
26
359-365
2008
Rattus norvegicus
Wei, L.H.; Yang, Y.; Wu, G.; Ignarro, L.J.
IL-4 and IL-13 upregulate ornithine decarboxylase expression by PI3K and MAP kinase pathways in vascular smooth muscle cells
Am. J. Physiol. Cell Physiol.
294
C1198-C1205
2008
Rattus norvegicus
Svensson, K.J.; Welch, J.E.; Kucharzewska, P.; Bengtson, P.; Bjurberg, M.; Pahlman, S.; Ten Dam, G.B.; Persson, L.; Belting, M.
Hypoxia-mediated induction of the polyamine system provides opportunities for tumor growth inhibition by combined targeting of vascular endothelial growth factor and ornithine decarboxylase
Cancer Res.
68
9291-9301
2008
Homo sapiens, Rattus norvegicus
Bordallo, J.; Secades, L.; Bordallo, C.; Cantabrana, B.; Sanchez, M.
Influence of gender and sex hormones on 5alpha-dihydrotestosterone elicited effect in isolated left atria of rats: role of beta-adrenoceptors and ornithine decarboxylase activity
Eur. J. Pharmacol.
604
103-110
2008
Rattus norvegicus
Ehrnstroem, R.A.; Bjursten, L.M.; Ljungberg, O.; Veress, B.; Haglund, M.E.; Lindstroem, C.G.; Andersson, T.
Dietary supplementation with carbonate increases expression of ornithine decarboxylase and proliferation in gastric mucosa in a rat model of gastric cancer
Int. J. Cancer
122
727-733
2008
Rattus norvegicus
Govoni, M.; Bonavita, F.; Shantz, L.M.; Guarnieri, C.; Giordano, E.
Overexpression of ornithine decarboxylase increases myogenic potential of H9c2 rat myoblasts
Amino Acids
38
541-547
2010
Rattus norvegicus
Maekitie, L.T.; Kanerva, K.; Andersson, L.C.
Ornithine decarboxylase regulates the activity and localization of rhoA via polyamination
Exp. Cell Res.
315
1008-1014
2009
Rattus norvegicus
Ivanov, I.P.; Firth, A.E.; Atkins, J.F.
Recurrent emergence of catalytically inactive ornithine decarboxylase homologous forms that likely have regulatory function
J. Mol. Evol.
70
289-302
2010
Aedes aegypti, Ancylostoma ceylanicum, Anopheles gambiae, Aspergillus clavatus, Aspergillus fischeri, Aspergillus fumigatus, Aspergillus terreus, Bos taurus, Botrytis cinerea, Branchiostoma floridae, Caenorhabditis briggsae, Caenorhabditis elegans, Meyerozyma guilliermondii, Canis lupus familiaris, Gallus gallus, Ciona intestinalis, Coccidioides immitis, Culex pipiens, Dictyostelium discoideum, Drosophila melanogaster, Fusarium oxysporum, Fusarium verticillioides, Homo sapiens, Hydra vulgaris, Mus musculus, Neurospora crassa, Rattus norvegicus, Takifugu rubripes, Trypanosoma brucei, Xenopus laevis, Petromyzon marinus, Parastagonospora nodorum, Uncinocarpus reesii, Tetraodon nigroviridis, Dugesia japonica, Gasterosteus aculeatus, Anolis carolinensis, Schmidtea mediterranea, Nasonia vitripennis
Correa-Basurto, J.; Rodrguez-Paez, L.; Aguiar-Moreno, E.; Lopez-Sanchez, P.; Espinoza-Fonseca, L.; Wong, C.; Trujillo-Ferrara, J.
Computational and experimental evaluation of ornithine derivatives as ornithine decarboxylase inhibitors
Med. Chem. Res.
18
20-30
2009
Rattus norvegicus
-
Zhao, Y.J.; Zhang, W.H.; Xu, C.Q.; Li, H.Z.; Wang, L.N.; Li, H.; Sun, Y.H.; Lin, Y.; Han, L.P.; Zhang, L.; Tian, Y.; Wang, R.; Yang, B.F.; Li, W.M.
Involvement of the ornithine decarboxylase/polyamine system in precondition-induced cardioprotection through an interaction with PKC in rat hearts
Mol. Cell. Biochem.
332
135-144
2009
Rattus norvegicus
Matsuoka, Y.; Uehara, N.; Tsubura, A.
hnRNP U interacts with the c-Myc-Max complex on the E-box promoter region inducing the ornithine decarboxylase gene
Oncol. Rep.
22
249-255
2009
Rattus norvegicus
Aksyonova, G.E.; Logvinovich, O.S.; Fialkovskaya, L.A.; Afanasyev, V.N.; Ignatev, D.A.; Kolomiytseva, I.K.
Ornithine decarboxylase activity in rat organs and tissues under artificial hypobiosis
Biochemistry
75
1126-1131
2010
Rattus norvegicus
Ohtake, Y.; Maruko, A.; Ohishi, N.; Kawaguchi, M.; Satoh, T.; Ohkubo, Y.
Effect of retinoic acid on transglutaminase and ornithine decarboxylase activities during liver regeneration
Cell Biochem. Funct.
26
359-365
2008
Rattus norvegicus (P09057), Rattus norvegicus Wistar (P09057)
Ehrnstroem, R.A.; Bjursten, L.M.; Ljungberg, O.; Veress, B.; Haglund, M.E.; Lindstroem, C.G.; Andersson, T.
Dietary supplementation with carbonate increases expression of ornithine decarboxylase and proliferation in gastric mucosa in a rat model of gastric cancer
Int. J. Cancer
122
727-733
2008
Rattus norvegicus (P09057), Rattus norvegicus, Rattus norvegicus Wistar (P09057)
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