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detectable immunohistochemically from day 6
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marrow stromal cell or mesenchymal stem cells (MSC)
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from humans suffering from inflammatory neurological disorders exhibit increased IDO activity
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very irregular activity
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consistently expresses the enzyme at low levels. Exposure to UV-light leads to a dose-responding upregulation. Overexpression of indoleamine-pyrrole 2,3-dioxygenase could reduce apoptosis significantly following UV-B irradiation
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IDO-competent cells exhibit attributes of B cells as well as dendritic cells
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cells grown in a medium containing L-tryptophan as the sole carbon, nitrogen, and energy source
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extravillous
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epithelium
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despite suppression by progesterone, indoleamine 2,3-dioxygenase expression in endometrial stromal cells may increase during decidualization due to stimulation by interferon-gamma secreted by infiltrating leukocytes
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of uterine endometrium and cervix
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mature granule cells of the adult mouse dentate gyrus
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primary hepatocyte
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i.e. human umbilical vein endothelial cell, express little indoleamine 2,3-dioxygenase, which is poorly upregulated upon activation (except by mycoplasma)
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in HUVEC cells the enzyme is upregulated by incubation with cytokines or in mycoplasma-infected cells. Inhibition of indoleamine 2,3-dioxygenase improves ability of HUVEC cells to stimulate T-cell proliferation
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Langerhans cells possess an immunoregulatory function in promoting T cell tolerance by production of IDO
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enzyme activity is detected in all lenses ranging from 26 to 80 years and there are no clear relationship of IDO activity with age
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anterior and bow region
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IFNgamma-primed
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IDO-competent cells are present in spleens of B-cell-deficient mice
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peritumoral infiltrate
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premetamorphic stage
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low level expression
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highest expression in liver and trunk kidney
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epithelium
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epithelium
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microvascular endothelial cell, HBMEC
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IDO-1 is associated with senile plaques in Alzheimer's disease brains and is specifically localized in conjunction with neurofibrillary tangles
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Alzheimer's disease brain
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IDO2
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expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
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indoleamine 2,3-dioxygenase
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enzyme activity in triple transgenic Alzheimer's disease mice. Expression of TDO mRNA is significantly increased in the cerebellum of Alzheimer's disease mouse brain
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IDO2
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expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
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activity with D-Trp and L-Trp
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in the group of rats aged 12 months, the highest specific activity is found in the small intestine
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in glandular epithelium in first trimester pregnancy
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strong expression in stromal and glandular epithelial cells of the first trimester decidua
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CD123+/CCR6+ dendritic cells do not constitutively express indoleamine 2,3-dioxygenase, and, even if they express the enzyme after interferon-gamma treatment, they possess only limited T-cell regulatory function
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tumor-associated dendritic cell, indoleamine 2,3-dioxygenase is up-regulated after maturation of dendritic cells in presence of prostaglandin E2
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expressed in antigen-presenting dendritic cells where tryptophan catabolism drives immune tolerance
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mature, but not immature dendritic cells metabolize tryptophan
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the expression of the enzyme is selectively induced in specific splenic dendritic cell subsets when mice are exposed to the synthetic immunomodulatory reagent CTLA4-Ig
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derived from bone marrow
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BAOEC cell
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arterially derived, express little indoleamine 2,3-dioxygenase, which is poorly upregulated upon activation (except by mycoplasma)
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IDO1 is constitutively expressed in the epididymis
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diploid fibroblast cells FS-4
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expression of TDO mRNA is significantly increased in the hippocampus of Alzheimer's disease patient brain. TDO co-localizes with quinolinic acid, neurofibrillary tangles-tau and amyloid deposits in the hippocampus of Alzheimer's disease patient brain
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neurons, level of activity is lower than in monocytic cells in lymph nodes
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the enzyme is upregulated by interferon-gamma in neurons of the hippocampus
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IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
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IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
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intestinal biopsies from patients with coeliac disease show an increased expression of indoleamine 2,3-dioxygenase
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IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
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IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
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intestinal mucosa of rat exhibits lower activity than in rabbit
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IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
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IDO is highly expressed throughout the intestine with a marked presence in the jejunum and ileum both at the RNA and protein level
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IDO2
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predominantly expressed
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tubular cells in the kidney
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tubular epithelial cell. Expression of indoleamine 2,3-dioxygenase may be deleterious during renal inflammation, because it enhances TEC self-injury through Fas/FasL interactions. Attenuation of indoleamine 2,3-dioxygenase may represent a novel strategy to promote kidney function following ischemia and renal allograft rejection
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IDO2
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low activity in rats aged 2-3 months or 12 months
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highest expression in liver and trunk kidney
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upregulation of IDO in the livers of patients with chronic hepatitis C
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low level expression
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IDO2
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IDO2
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liver enzyme is specific for L-Trp
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upregulation of IDO in the livers of chimpanzees with chronic hepatitis C
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395456, 395464, 395470, 395476, 395477, 395479, 395481, 395486, 395488, 395489, 395497, 658924, 663910, 666138, 688601, 699980 brenda
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tryptophan 2,3-dioxygenase
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activity is low in newborn rats, increases up to the age of 2-3 months and decreases from 3 months of age to 18 months
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cancer bearing lung exhibits 20fold increase in IDO activity
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endothelial cell expression in lung
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indoleamine 2,3-dioxygenase
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activity with L-Trp and D-5-hydroxytryptophan
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low activity, activity is not age-related
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enzyme is induced in monocyte-derived macrophages treated with human recombinant interferon-beta or interferon gamma
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in the villous stroma and in the fetal membrane
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induced by alpha-, beta- and gamma-interferon
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monocytes are a major source of active IDO in normal peripheral blood
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the enzyme is upregulated by interferon-gamma in neurons of the hippocampus. The enzyme could contribute to the vulnerability of neurons to inflammatory conditions
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K562 from human erythroleukemia, human hepatocellular carcinoma cell line HepG2
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term placenta
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brush border microvillous plasma membranes of placental syncytiotrophoblast
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in the first and second trimester placenta the enzyme is localized to the syncytiotrophoblast, stroma and macrophages. In term placenta confined mainly to vascular endothelial cells of villous blood vessels, and to macrophages within the fetal villus
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endothelial cell expression in placenta
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indoleamine 2,3-dioxygenase
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in newborn rats IDO activity is present only in small intestine. In the group of rats aged 2-3 months, the highest specific activity is found in the small intestine, decrease of enzyme activity in relation to age
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dentritic cells
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dentritic cells
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brush border microvillous plasma membranes of placental syncytiotrophoblast
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low level expression
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additional information
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placental enzyme is not expressed in the maternal facing brush border membrane of syncytiotrophoblast
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additional information
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cell in the peritumoral infiltrate of the stroma
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additional information
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endometrial glandular and surface epithelial cells exhibit strong activity during the secretory phase
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additional information
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T-lymphocyte
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additional information
IDO is found ubiquitously in all tissues
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additional information
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IDO is found ubiquitously in all tissues
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additional information
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IDO is not detected in CD103- gut dendritic cells and in spleen
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additional information
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IDO1 expression is found in most tissues and is regulated by immunological signals, including interferon-gamma, lipopolysaccharide and tumor necrosis factor
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additional information
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quantitative real-time RT PCR enzyme expression analysis in brain sectiions
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additional information
in human tumors IDO-2 is expressed, but it is produced in a functionally inactive form
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additional information
in human tumors IDO-2 is expressed, but it is produced in a functionally inactive form
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additional information
indoleamine 2,3-dioxygenase (IDO) is expressed in antigen-presenting cells
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additional information
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indoleamine 2,3-dioxygenase (IDO) is expressed in antigen-presenting cells
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additional information
indoleamine 2,3-dioxygenase is expressed in antigen-presenting cells and exerts immunosuppressive effects on CD4+ T cells through the inhibition of aerobic glycolysis or through downregulation of key enzymes that directly or indirectly promote fatty acid synthesis, a prerequisite for CD4+ T-cell proliferation and differentiation into effector cell lineages
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additional information
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indoleamine 2,3-dioxygenase is expressed in antigen-presenting cells and exerts immunosuppressive effects on CD4+ T cells through the inhibition of aerobic glycolysis or through downregulation of key enzymes that directly or indirectly promote fatty acid synthesis, a prerequisite for CD4+ T-cell proliferation and differentiation into effector cell lineages
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additional information
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entorhinal cortex
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additional information
analysis of various tissues
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additional information
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analysis of various tissues
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additional information
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IDO is not detected in CD103- gut dendritic cells and in spleen
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additional information
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IDO1 expression is found in most tissues and is regulated by immunological signals, including interferon-gamma, lipopolysaccharide and tumor necrosis factor. Expression of IDO2 protein in the liver and kidney in these IDO1-/- mice is unaffected, although the IDO2 transcript is downregulated. It is possible that the deletion of the IDO1 gene affects the expression of the IDO2 protein in other cell types, and 1DMT's effects might be mediated through either or both IDO isoforms
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additional information
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quantitative real-time RT PCR enzyme expression analysis in brain sectiions
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