Indoleamine 2,3-dioxygenase (IDO) expression in lung cancer

Karanikas, Vaios; Ζαμανάκου, Μαρία; Kerenidi, Theodora; Dahabreh, Jubrail; Hevas, Athanasios; Νάκου, Μαρία; Gourgoulianis, Konstantinos; Germenis, Anastasios E.

doi:10.4161/cbt.6.8.4446

Cited by 66 publications

(50 citation statements)

References 17 publications

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“…KTR is considered an indirect marker of IDO activity and was in the current study associated with increased risk of lung cancer. Although no previous prospective studies have investigated KTR in relation to lung cancer, our data would seem consistent with studies conducted in case series in which tryptophan depletion was associated with worse clinical outcome (17,18). However, the association of KTR with lung cancer risk was primarily driven by an inverse association of tryptophan, to a large extent explained by its strong correlation with methionine, which was previously found associated with lung cancer risk in the same study population (20).…”

Section: Discussionsupporting

confidence: 77%

“…The key enzymes in degradation of tryptophan through the kynurenine pathway, IDO and TDO, as well as downstream catabolites may influence the immune system (11,24), and thus affect cancer development and progression (7,8,10,12,17,18,25). KTR is considered an indirect marker of IDO activity and was in the current study associated with increased risk of lung cancer.…”

Section: Discussionmentioning

confidence: 99%

“…It is methodologically complex to measure cellular IDO and TDO activity directly in an epidemiologic setting, but the ratio between circulating kynurenine and tryptophan (KTR) is widely accepted as an indirect measure of IDO activity (11,13). Circulating tryptophan and kynurenine concentrations have been associated with poor outcome among patients with lung cancer (17,18), but have not yet been evaluated in relation to lung cancer incidence in a prospective setting.…”

Section: Introductionmentioning

confidence: 99%

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Circulating Biomarkers of Tryptophan and the Kynurenine Pathway and Lung Cancer Risk

Chuang

Fanidi

Ueland

et al. 2014

Cancer Epidemiology, Biomarkers &Amp; Prevention

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Background: Imbalances in tryptophan metabolism have been linked to cancer-related immune escape and implicated in several cancers, including lung cancer.Methods: We conducted a nested case-control study within the European Prospective Investigation into Cancer and Nutrition (EPIC) that included 893 incident lung cancer cases and 1,748 matched controls. Circulating levels of tryptophan and six of its metabolites were measured and evaluated in relation to lung cancer risk.Results: Tryptophan (P trend ¼ 2 Â 10

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Section: Discussionsupporting

confidence: 77%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Circulating Biomarkers of Tryptophan and the Kynurenine Pathway and Lung Cancer Risk

Chuang

Fanidi

Ueland

et al. 2014

Cancer Epidemiology, Biomarkers &Amp; Prevention

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“…Indeed, a growing body of evidence has suggested that a variety of immunosuppressive factors derived from the tumor cells and surrounding cells contribute to the establishment of regional immunosuppressive networks in patients with ESCC [6][7][8][9]. Recently, indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that catalyzes the initial and rate-limiting steps in the metabolism of the essential amino acid tryptophan along the kynurenine pathway, is found to be increased and functions as a critical immunosuppressive factor in many types of human cancers [10][11][12][13][14][15][16][17][18]. However, little information is available concerning the expression of IDO in ESCC.…”

Section: Introductionmentioning

confidence: 99%

Localization of indoleamine 2,3-dioxygenase in human esophageal squamous cell carcinomas

Liu

Fuai

et al. 2009

Virchows Arch

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Immunosuppressive factors derived from the tumor and nontumor cells present in the tumor microenvironment contribute to tumor escape from host immune attack. Recently, the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) derived from both the tumor cells and surrounding nontumor cells was found to function as a critical immunosuppressive factor. While the expression of IDO is intensively under investigation in many types of cancers, little information is available in esophageal squamous cell carcinomas (ESCC) thus far. In this study, we have therefore investigated the cellular localization of IDO in 45 ESSCs and ten morphologically normal esophageal tissues; the correlation of IDO with clinicopathological parameters was also analyzed. Immunohistochemistry (IHC) analysis revealed that the density of IDO-positive cells was increased in ESCCs relative to controls (P < 0.01). These cells were distributed as clusters and formed a patchy pattern in both the cancerous epithelium and the surrounding noncancerous cells. Double IHC further confirmed that many IDO-positive cells in the tumor stroma were smooth-muscle-actin-alpha-positive myofibroblasts, CD68-positive macrophages, and S100-positive dendritic cells. Statistical analysis showed that the densities of IDO-positive cells were not significantly correlated with tumor clinical parameters (tumor invasion depth, node metastasis, and TNM stages) and lymphocytic infiltration. Our current findings suggested that the increased IDO expression in ESCCs is from a mixed cellular source (both cancer cells and noncancerous cells). Further studies on immune cell functional analysis are required in the future.

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“…IDO has been investigated in pulmonary, hepatocellular, renal, endometrial and nasopharyngeal carcinomas (7)(8)(9)(10). The inhibition of IDO expression could significantly suppress tumor growth and promote the anti-tumor activities of various immunotherapeutic agents in relevant animal models (11,12).…”

Section: Introductionmentioning

confidence: 99%

SAHA down-regulates the expression of indoleamine 2,3-dioxygenase via inhibition of the JAK/STAT1 signaling pathway in gallbladder carcinoma cells

et al. 2012

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Abstract. The aim of the present study was to investigate the role of the JAK/STAT1 signaling pathway in suberoylanilide hydroxamic acid (SAHA)-mediated down-regulation of indoleamine 2,3-dioxygenase (IDO) in gallbladder carcinoma cells. We treated SGC-996 gallbladder carcinoma cells with IFN-γ and SAHA. Western blotting was used to detect the expression of IDO, signal transducer and activator of transcription 1 (STAT1) phosphorylation and interferon regulatory factor genes-1 (IRF-1). Confocal microscopy analysis was used to detect STAT1 translocation. Transient transfection and reporter gene assay was used for detecting the activation of γ-activated sites (GAS) and interferon-stimulated response elements (ISRE). The results revealed that IDO was expressed in SGC-996 cells in a dose-and time-dependent manner when stimulated with IFN-γ and SAHA down-regulated the expression of IDO induced by IFN-γ in a dose-dependent manner.SAHA blocked the expression of IRF-1 induced by IFN-γ and SAHA inhibited IFN-γ-induced STAT1 phosphorylation and nuclear translocation. In addition, SAHA down-regulated IFN-γ-induced activation of GAS and ISRE. In conclusion, SAHA down-regulated IDO expression via inhibition of the activation of members of the JAK/STAT1 signaling pathway. Therefore, regulation of the JAK/STAT1 signaling pathway may provide a new gallbladder carcinoma immunotherapeutic strategy to break tumor immune tolerance.

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Indoleamine 2,3-dioxygenase (IDO) expression in lung cancer

Cited by 66 publications

References 17 publications

Circulating Biomarkers of Tryptophan and the Kynurenine Pathway and Lung Cancer Risk

Circulating Biomarkers of Tryptophan and the Kynurenine Pathway and Lung Cancer Risk

Localization of indoleamine 2,3-dioxygenase in human esophageal squamous cell carcinomas

SAHA down-regulates the expression of indoleamine 2,3-dioxygenase via inhibition of the JAK/STAT1 signaling pathway in gallbladder carcinoma cells

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