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Indoleamine 2,3-dioxygenase increases p53 levels in alloreactive human T cells, and both indoleamine 2,3-dioxygenase and p53 suppress glucose uptake, glycolysis and proliferation.
Int Immunol. 2014 Dec; 26(12):673-84.II

Abstract

Indoleamine 2,3-dioxygenase (IDO) suppresses adaptive immunity by inhibiting T-cell proliferation and altering glucose metabolism. The tumor suppressor p53 also alters these cellular processes with similar results. The effect of IDO on p53 and on glucose metabolism was evaluated in alloreactive T cells. Mixed-lymphocyte reactions (MLRs) were performed in the presence or not of the IDO inhibitor, 1-dl-methyl-tryptophan (1-MT) and/or the p53 inhibitor, pifithrin-α (PFT). Cell proliferation, glucose consumption and lactate production were assessed. 1-MT increased cell proliferation, glucose influx and lactate production, whereas PFT enhanced cell proliferation and glucose influx, leaving lactate production unaffected. In MLR-derived T cells, protein analysis revealed that IDO activated general control non-derepressible 2 kinase and induced p53, p-p53 (p53 phosphorylated at serine 15) and p21. In addition, both IDO and p53 decreased glucose transporter 1 and TP53-induced glycolysis and apoptosis regulator and increased synthesis of cytochrome c oxidase 2. IDO also reduced lactate dehydrogenase-A and glutaminase 2 levels, whereas p53 left them unaffected. Neither 1-MT nor PFT affected glucose-6-phosphate dehydrogenase. In conclusion, in alloreactive T cells, IDO increases p53 levels, and both IDO and p53 inhibit cell proliferation, glucose consumption and glycolysis. Lactate production and glutaminolysis are also suppressed by IDO, but not by p53.

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Eleftheriadis T

Department of Nephrology, Medical School, University of Thessaly, Neo Ktirio, Mezourlo Hill, 41110 Larissa, Greece teleftheriadis@yahoo.com.

Department of Nephrology, Medical School, University of Thessaly, Neo Ktirio, Mezourlo Hill, 41110 Larissa, Greece.

Department of Nephrology, Medical School, University of Thessaly, Neo Ktirio, Mezourlo Hill, 41110 Larissa, Greece.

Department of Nephrology, Medical School, University of Thessaly, Neo Ktirio, Mezourlo Hill, 41110 Larissa, Greece.

Department of Nephrology, Medical School, University of Thessaly, Neo Ktirio, Mezourlo Hill, 41110 Larissa, Greece.

Department of Nephrology, Medical School, University of Thessaly, Neo Ktirio, Mezourlo Hill, 41110 Larissa, Greece.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

25064493

Citation

Eleftheriadis, Theodoros, et al. "Indoleamine 2,3-dioxygenase Increases P53 Levels in Alloreactive Human T Cells, and Both Indoleamine 2,3-dioxygenase and P53 Suppress Glucose Uptake, Glycolysis and Proliferation." International Immunology, vol. 26, no. 12, 2014, pp. 673-84.

Eleftheriadis T, Pissas G, Antoniadi G, et al. Indoleamine 2,3-dioxygenase increases p53 levels in alloreactive human T cells, and both indoleamine 2,3-dioxygenase and p53 suppress glucose uptake, glycolysis and proliferation. Int Immunol. 2014;26(12):673-84.

Eleftheriadis, T., Pissas, G., Antoniadi, G., Spanoulis, A., Liakopoulos, V., & Stefanidis, I. (2014). Indoleamine 2,3-dioxygenase increases p53 levels in alloreactive human T cells, and both indoleamine 2,3-dioxygenase and p53 suppress glucose uptake, glycolysis and proliferation. International Immunology, 26(12), 673-84. https://doi.org/10.1093/intimm/dxu077

Eleftheriadis T, et al. Indoleamine 2,3-dioxygenase Increases P53 Levels in Alloreactive Human T Cells, and Both Indoleamine 2,3-dioxygenase and P53 Suppress Glucose Uptake, Glycolysis and Proliferation. Int Immunol. 2014;26(12):673-84. PubMed PMID: 25064493.

* Article titles in AMA citation format should be in sentence-case

TY - JOUR T1 - Indoleamine 2,3-dioxygenase increases p53 levels in alloreactive human T cells, and both indoleamine 2,3-dioxygenase and p53 suppress glucose uptake, glycolysis and proliferation. AU - Eleftheriadis,Theodoros, AU - Pissas,Georgios, AU - Antoniadi,Georgia, AU - Spanoulis,Aginor, AU - Liakopoulos,Vassilios, AU - Stefanidis,Ioannis, Y1 - 2014/07/26/ PY - 2014/7/28/entrez PY - 2014/7/30/pubmed PY - 2015/7/15/medline KW - 3-dioxygenase KW - GCN2 kinase KW - T cells KW - aerobic glycolysis KW - glutaminolysis KW - indoleamine 2 KW - p53 KW - proliferation SP - 673 EP - 84 JF - International immunology JO - Int Immunol VL - 26 IS - 12 N2 - Indoleamine 2,3-dioxygenase (IDO) suppresses adaptive immunity by inhibiting T-cell proliferation and altering glucose metabolism. The tumor suppressor p53 also alters these cellular processes with similar results. The effect of IDO on p53 and on glucose metabolism was evaluated in alloreactive T cells. Mixed-lymphocyte reactions (MLRs) were performed in the presence or not of the IDO inhibitor, 1-dl-methyl-tryptophan (1-MT) and/or the p53 inhibitor, pifithrin-α (PFT). Cell proliferation, glucose consumption and lactate production were assessed. 1-MT increased cell proliferation, glucose influx and lactate production, whereas PFT enhanced cell proliferation and glucose influx, leaving lactate production unaffected. In MLR-derived T cells, protein analysis revealed that IDO activated general control non-derepressible 2 kinase and induced p53, p-p53 (p53 phosphorylated at serine 15) and p21. In addition, both IDO and p53 decreased glucose transporter 1 and TP53-induced glycolysis and apoptosis regulator and increased synthesis of cytochrome c oxidase 2. IDO also reduced lactate dehydrogenase-A and glutaminase 2 levels, whereas p53 left them unaffected. Neither 1-MT nor PFT affected glucose-6-phosphate dehydrogenase. In conclusion, in alloreactive T cells, IDO increases p53 levels, and both IDO and p53 inhibit cell proliferation, glucose consumption and glycolysis. Lactate production and glutaminolysis are also suppressed by IDO, but not by p53. SN - 1460-2377 UR - https://www.unboundmedicine.com/medline/citation/25064493/Indoleamine_23_dioxygenase_increases_p53_levels_in_alloreactive_human_T_cells_and_both_indoleamine_23_dioxygenase_and_p53_suppress_glucose_uptake_glycolysis_and_proliferation_ L2 - https://academic.oup.com/intimm/article-lookup/doi/10.1093/intimm/dxu077 DB - PRIME DP - Unbound Medicine ER -