scholarly journals A Tear Metabolomic Profile Showing Increased Ornithine Decarboxylase Activity and Spermine Synthesis in Thyroid-Associated Orbitopathy

2022 ◽  
Vol 11 (2) ◽  
pp. 404
Author(s):  
Benjamin Billiet ◽  
Juan Manuel Chao de la Barca ◽  
Marc Ferré ◽  
Jeanne Muller ◽  
Anaïs Vautier ◽  
...  
Keyword(s):  
Ornithine Decarboxylase ◽  
Eye Disease ◽  
Control Group ◽  
Graves Disease ◽  
Decarboxylase Activity ◽  
Metabolomic Profile ◽  
Orbital Fibroblasts ◽  
Increased Activity ◽  
Metabolomic Approach ◽  
Stimulation Of

About half of patients with Graves’ disease develop an orbitopathy related to an inflammatory expansion of the periorbital adipose tissue and muscles. We used a targeted metabolomic approach measuring 188 metabolites by mass spectrometry to compare the metabolic composition of tears in patients with active (n = 21) versus inactive (n = 24) thyroid-associated orbitopathy. Among the 44 metabolites accurately measured, 8 showed a significant alteration of their concentrations between the two groups. Two short-chain acylcarnitines, propionylcarnitine and butyrylcarnitine, and spermine showed increased concentrations in the tears of patients with active orbitopathy, whereas ornithine, glycine, serine, citrulline and histidine showed decreased concentrations in this group. In addition, the ratio putrescine/ornithine, representing the activity of ornithine decarboxylase, was significantly increased in patients with active compared to inactive orbitopathy (p = 0.0011, fold change 3.75). The specificity of this candidate biomarker was maintained when compared to a control group with unclassified dry eye disease. Our results suggest that the stimulation of ornithine decarboxylase by TSH receptor autoantibodies in orbital fibroblasts could lead to increased synthesis of spermine, through the increased activity of ornithine decarboxylase, that may contribute to periorbital expansion in Graves’ ophthalmopathy.

scholarly journals Response of enzymes involved in the metabolism of polyamines to phytohaemagglutinin-induced activation of human lymphocytes

1981 ◽  
Vol 196 (3) ◽  
pp. 733-738 ◽  
Author(s):  
H Korpela ◽  
E Hölttä ◽  
T Hovi ◽  
J Jänne
Keyword(s):  
Ornithine Decarboxylase ◽  
Human Lymphocytes ◽  
Lymphocyte Activation ◽  
Decarboxylase Activity ◽  
Spermidine Synthase ◽  
Irreversible Inhibitor ◽  
Adenosylmethionine Decarboxylase ◽  
Spermine Synthase ◽  
Diamine Oxidase Activity ◽  
Stimulation Of

The stimulation of lymphocyte ornithine decarboxylase and adenosylmethionine decarboxylase produced by phytohaemagglutinin was accompanied by an equally marked, but delayed, stimulation of spermidine synthase, which is not commonly considered as an inducible enzyme. In contrast with the marked stimulation of these biosynthetic enzymes, less marked changes were observed in the biodegradative enzymes of polyamines in response to phytohaemagglutinin. Diamine oxidase activity was undetectable during all stages of the transformation. The activity of polyamine oxidase remained either constant or was slightly decreased several days after addition of the mitogen. The activity of polyamine acetylase (employing all the natural polyamines as substrates) distinctly increased both in the cytosolic and crude nuclear preparations of the cells during later stages of mitogen activation. Difluoromethylornithine, an irreversible inhibitor of ornithine decarboxylase, although powerfully inhibiting ornithine decarboxylase, produced a gradual enhancement of adenosylmethionine decarboxylase activity during lymphocyte activation, without influencing the activities of the two propylamine transferases (spermidine synthase and spermine synthase).

Estrogen-like stimulation of uterine ornithine decarboxylase by cholera toxin

1984 ◽  
Vol 246 (3) ◽  
pp. E288-E291
Author(s):  
R. A. Webster ◽  
C. J. Zaloudek ◽  
B. C. Inman ◽  
P. J. Stewart
Keyword(s):  
Estrogen Receptor ◽  
Protein Synthesis ◽  
Vascular Permeability ◽  
Cholera Toxin ◽  
Nuclear Receptor ◽  
Ornithine Decarboxylase ◽  
Ovariectomized Rats ◽  
Decarboxylase Activity ◽  
Nuclear Estrogen Receptor ◽  
Stimulation Of

Cholera toxin administered by intrauterine injection to ovariectomized rats increased uterine ornithine decarboxylase activity as much as systemic estradiol at 4 h after treatment. At 45-60 min after treatment, however, cholera toxin did not increase nuclear estrogen receptor or stimulate synthesis of the uterine "induced protein," which is closely correlated with nuclear receptor, whereas estradiol caused substantial increases in both nuclear receptor and induced protein synthesis. Intrauterine injection of cholera toxin also produced an estrogen-like elevation of the uterine protein/DNA ratio at 24 h. Because both cholera toxin and estradiol are known to increase vascular permeability, our results support the hypothesis that some uterine effects of estradiol are not mediated by receptor-genome interaction but involve another mechanism that is associated with increased vascular permeability.

Puromycin Stimulation of Rat Liver Ornithine Decarboxylase Activity

Nature ◽  
1973 ◽  
Vol 241 (5387) ◽  
pp. 275-277 ◽  
Author(s):  
WILLIAM T. BECK ◽  
RILL ANN BELLANTONE ◽  
E. S. CANELLAKIS
Keyword(s):  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Decarboxylase Activity ◽  
Ornithine Decarboxylase Activity ◽  
Stimulation Of

scholarly journals Inhibition of ornithine decarboxylase of HeLa cells by diamines and polyamines. Effect on cell proliferation

1980 ◽  
Vol 186 (3) ◽  
pp. 925-931 ◽  
Author(s):  
Andrew A. Branca ◽  
Edward J. Herbst
Keyword(s):  
Hela Cell ◽  
Ornithine Decarboxylase ◽  
Cell Cultures ◽  
Hela Cells ◽  
Horse Serum ◽  
Fresh Medium ◽  
Decarboxylase Activity ◽  
Inhibitory Protein ◽  
Ornithine Decarboxylase Activity ◽  
Stimulation Of

1. Ornithine decarboxylase activity is stimulated in high-density HeLa-cell cultures by dilution of or replacement of spent culture medium with fresh medium containing 10% (v/v) horse serum. 2. After stimulation, ornithine decarboxylase activity reaches a peak at 4–6h, then rapidly declines to the low enzyme activity characteristic of quiescent cultures, where it remains during the remainder of the cell cycle. 3. The stimulation of ornithine decarboxylase is eliminated by the addition of 0.5μm-spermine or -spermidine or 10μm-putrescine to the HeLa-cell cultures at the time of re-feeding with fresh medium. Much higher concentrations (1mm) of the non-physiological diamines, 1,3-diamino-propane or 1,3-diamino-2-hydroxypropane, are required to eliminate the stimulation of ornithine decarboxylase in re-fed HeLa-cell cultures. 4. A heat-labile, non-diffusible inhibitor, comparable with the inhibitory protein ornithine decarboxylase antizyme, is induced in HeLa cells by the addition of exogenous diamines or polyamines. 5. Intracellular putrescine is eliminated, intracellular spermidine and spermine are severely decreased and proliferation of HeLa cells is inhibited when cultures are maintained for 48h in the presence of the non-physiological inducer of ornithine decarboxylase antizyme, 1,3-diamino-2-hydroxypropane. Exogenous putrescine, a physiological inducer of the antizyme, does not decrease intracellular polyamines or interfere with proliferation of HeLa cells.

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