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Inhibition of indoleamine 2,3-dioxygenase in mixed lymphocyte reaction affects glucose influx and enzymes involved in aerobic glycolysis and glutaminolysis in alloreactive T-cells
dc.creator | Eleftheriadis, T. | en |
dc.creator | Pissas, G. | en |
dc.creator | Yiannaki, E. | en |
dc.creator | Markala, D. | en |
dc.creator | Arampatzis, S. | en |
dc.creator | Antoniadi, G. | en |
dc.creator | Liakopoulos, V. | en |
dc.creator | Stefanidis, I. | en |
dc.date.accessioned | 2015-11-23T10:26:14Z | |
dc.date.available | 2015-11-23T10:26:14Z | |
dc.date.issued | 2013 | |
dc.identifier | 10.1016/j.humimm.2013.08.268 | |
dc.identifier.issn | 0198-8859 | |
dc.identifier.uri | http://hdl.handle.net/11615/27344 | |
dc.description.abstract | Indoleamine 2,3-dioxygenase (IDO) suppresses adaptive immunity. T-cell proliferation and differentiation to effector cells require increased glucose consumption, aerobic glycolysis and glutaminolysis. The effect of IDO on the above metabolic pathways was evaluated in alloreactive T-cells. Mixed lymphocyte reaction (MLR) in the presence or not of the IDO inhibitor, 1-methyl-DL-tryptophan (1-MT), was used. In MLRs, 1-MT decreased tryptophan consumption, increased cell proliferation, glucose influx and lactate production, whereas it decreased tricarboxylic acid cycle activity. In T-cells, from the two pathways that could sense tryptophan depletion, i.e. general control nonrepressed 2 (GCN2) kinase and mammalian target of rapamycin complex 1, 1-MT reduced only the activity of the GCN2 kinase. Additionally 1-MT treatment of MLRs altered the expression and/or the phosphorylation state of glucose transporter-1 and of key enzymes involved in glucose metabolism and glutaminolysis in alloreactive T-cells in a way that favors glucose influx, aerobic glycolysis and glutaminolysis. Thus in alloreactive T-cells, IDO through activation of the GCN2 kinase, decreases glucose influx and alters key enzymes involved in metabolism, decreasing aerobic glycolysis and glutaminolysis. Acting in such a way, IDO could be considered as a constraining factor for alloreactive T-cell proliferation and differentiation to effector T-cell subtypes. (C) 2013 American Society for Histocompatibility and Immunogenetics. Published by Elsevier Inc. All rights reserved. | en |
dc.source | Human Immunology | en |
dc.source.uri | <Go to ISI>://WOS:000328014800002 | |
dc.subject | TRYPTOPHAN CATABOLISM | en |
dc.subject | CANCER-CELLS | en |
dc.subject | TYROSINE PHOSPHORYLATION | en |
dc.subject | DENDRITIC | en |
dc.subject | CELLS | en |
dc.subject | TUMOR-GROWTH | en |
dc.subject | METABOLISM | en |
dc.subject | EXPRESSION | en |
dc.subject | TOLERANCE | en |
dc.subject | SURVIVAL | en |
dc.subject | DEHYDROGENASE | en |
dc.subject | Immunology | en |
dc.title | Inhibition of indoleamine 2,3-dioxygenase in mixed lymphocyte reaction affects glucose influx and enzymes involved in aerobic glycolysis and glutaminolysis in alloreactive T-cells | en |
dc.type | journalArticle | en |
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