Добірка наукової літератури з теми "IDO/TDO"
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Статті в журналах з теми "IDO/TDO":
Oweira, Hani, Imad Lahdou, Stefan Mehrle, Elias Khajeh, Rajan Nikbakhsh, Omid Ghamarnejad, Peter Terness, Christoph Reißfelder, Mahmoud Sadeghi, and Ali Ramouz. "Kynurenine Is the Main Metabolite of Tryptophan Degradation by Tryptophan 2,3-Dioxygenase in HepG2 Tumor Cells." Journal of Clinical Medicine 11, no. 16 (August 16, 2022): 4794. http://dx.doi.org/10.3390/jcm11164794.
Terai, Londin, Rochani, Link, Lam, Kaushal, Bhushan, Orloff, and Sato. "Expression of Tryptophan 2,3-Dioxygenase in Metastatic Uveal Melanoma." Cancers 12, no. 2 (February 10, 2020): 405. http://dx.doi.org/10.3390/cancers12020405.
Kim, Chan, Joo Hoon Kim, Jin Sung Kim, Hong Jae Chon, and Joo-Hang Kim. "A novel dual inhibitor of IDO and TDO, CMG017, potently suppresses the kynurenine pathway and overcomes resistance to immune checkpoint inhibitors." Journal of Clinical Oncology 37, no. 15_suppl (May 20, 2019): e14228-e14228. http://dx.doi.org/10.1200/jco.2019.37.15_suppl.e14228.
Campesato, Luis Felipe, Sadna Budhu, Jeremy Tchaicha, Abhinav Jaiswal, Mathieu Gigoux, Stephane Pourpe, Cailian Liu, et al. "Blockade of IDO/TDO downstream effectors restricts cancer immune suppression." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 137.3. http://dx.doi.org/10.4049/jimmunol.202.supp.137.3.
Thackray, Sarah J., Christopher G. Mowat, and Stephen K. Chapman. "Exploring the mechanism of tryptophan 2,3-dioxygenase." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1120–23. http://dx.doi.org/10.1042/bst0361120.
Oxenkrug, G. "Genetic and Environmental Impacts in Major Depressive Disorder are Mediated Via Kynurenine Pathway of Tryptophan Metabolism." European Psychiatry 24, S1 (January 2009): 1. http://dx.doi.org/10.1016/s0924-9338(09)70899-5.
SUZUKI, Sachiko, Shigenobu TONÉ, Osamu TAKIKAWA, Toshikazu KUBO, Ichiro KOHNO, and Yohsuke MINATOGAWA. "Expression of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase in early concepti." Biochemical Journal 355, no. 2 (April 6, 2001): 425–29. http://dx.doi.org/10.1042/bj3550425.
Nienhaus, Karin, and G. Ulrich Nienhaus. "Co Recombination in Human IDO and TDO - A Comparison." Biophysical Journal 106, no. 2 (January 2014): 676a. http://dx.doi.org/10.1016/j.bpj.2013.11.3744.
Sacramento, Jireh Joy D., and David P. Goldberg. "Oxidation of an indole substrate by porphyrin iron(iii) superoxide: relevance to indoleamine and tryptophan 2,3-dioxygenases." Chemical Communications 56, no. 20 (2020): 3089–92. http://dx.doi.org/10.1039/c9cc10019a.
Paccosi, Sara, Marta Cecchi, Angela Silvano, Sergio Fabbri, and Astrid Parenti. "Different effects of tryptophan 2,3-dioxygenase inhibition on SK-Mel-28 and HCT-8 cancer cell lines." Journal of Cancer Research and Clinical Oncology 146, no. 12 (August 10, 2020): 3155–63. http://dx.doi.org/10.1007/s00432-020-03351-2.
Дисертації з теми "IDO/TDO":
Julio, Ariane Rivellis. "Desenvolvimento e validação de métodos bioanalíticos para o monitoramento dos produtos das vias metabólicas do triptofano em linhagem celular de glioma humano." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-28042016-105250/.
The tryptophan metabolism (Trp) takes place by means of kynurenine (QUIN), by the serotonin pathway (SER) and by the pathway of trace amines synthesis. The first generates QUIN and a variety of other secondary metabolites. When driven by the enzyme indoleamine 2,3 dioxygenase (IDO) contributes to the phenomena of tolerance and immune escape of tumor cells; and when conducted by tryptophan 2,3 -dioxygenase (TDO) in the liver, participates in the niacin synthesis NAD. The SER pathway leads to the serotonin neurotransmitter (SER) formation, which can generate the hormone melatonin (MEL), respectively and other biologically active metabolites. Another less studied amines trace synthesis pathway produces neuroactive products. Given the scope and importance of Trp metabolic pathways,we developed and validated a robust, sensitive and selective bioanalytical method by high performance liquid chromatography (HPLC) coupled mass spectrometry (MS) for simultaneous determination of TRP and its 16 metabolites. Therefore, we chose to evaluate the three routes, glioma cell lines. The initial choice of this type of cell was due to the great interest in Trp metabolism studies in tumor cells, which glioma cells has been a model. In assays with glioma cells, we followed the effects of an inductor and inhibitors of the first stage of Trp metabolism, via the kynurenine pathway, or IFN -γ (IDO inducer) 1- methyltryptophane (1- MT; competitive IDO inhibitor) and 680C91 (selective TDO inhibitor). We could observe the first step induction or inhibition impact had over the further metabolites and the metabolism differences between the two studied strains, A172 and T98G. The T98G glioma cell has only IDO activity, while the A172 has both IDO and TDO activity as well. The IFN-γ indution showed that this cytokine not only acts in the formation of QUIN route, but has a modest impact on the others routes. Inhibition of IDO showed that the competitive inhibitor has activity in itself than a simple Trp-QUIN relationship. However, our results allow us to show the first time the complete description of these pathways, in particular, in these cell lines that can assume therapeutic strategies in these routes that are related or not with tumor progression.
Pantouris, Georgios. "Insights into inhibition of heme-dependent dioxygenases." Thesis, University of Edinburgh, 2012. http://hdl.handle.net/1842/7714.
Branquinho, Maryana Stephany Ferreira. "Efeitos dos inibidores de IDO e TDO na proliferação, migração e invasão de melanomas humanos e na atividade tumoricida de células mononucleares." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-11112015-142104/.
In cancer, the increased expression of the enzymes indolamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO), that convert tryptophan (Trp) to kynurenine (KYN), has been associated with the mechanism of immune escape of tumoral cells and inhibitors of these enzymes have been considered as immuno-adjuvants in antitumor therapy. The most known is the 1-methyl-tryptophan (1-MT), a competitive inhibitor of IDO and a target in clinical trials. 1-MT is found in the enantiomeric forms D- and L- and although 1-L-MT is more efficient to inhibit IDO1 (the isoform more active in tumors), 1-D-MT is more efficient in experimental models. This fact suggests that 1-MT may have additional actions beyond IDO inhibition. In this study, we evaluated the direct effects of 1-D-MT, 1-L-MT and 1-DL-MT on human melanomas. We also tested the effects of the compound 680C91 (an inhibitor of TDO). Proliferation, migration and invasion are the usual in vitro tests to evaluate how a specific compound affects tumor progression. We observed that all of the tested compounds have some direct effect on at least one of these parameters depending on the cell lineage. Therefore, direct effects on proliferation, migration and invasion must compose the antineoplastic activity of these compounds. In co-cultures, we observed that 1-MT was able to potentiate the tumoricidal activity of peripheral blood mononuclear cells (PBMC) and led to a decreased production of IFN-γ and TNF-α, and an increase in IL-10. These changes were not linked with the inhibition of KYN production, and led us to consider that the effect of 1-MT on cytokine production occurs independently of the enzyme IDO and is part of its antitumor effects. 1-MT also led to changes in the concentration of other Trp metabolites. Finally, the co-culture by itself led to an increased consumption of xanthurenic acid (XA) and increased production of kynurenic acid (KA). This result seems significant to the immunology of tumors given the biological effects of these compounds.
Venancio, Paloma Almeida. "Expressão de indoleamina 2,3-dioxigenase (IDO) e triptofano 2,3-dioxigenase(TDO) no ambiente cervicovaginal normal, na vaginose bacteriana e nas lesões cervicais associadas ao HPV." Universidade de São Paulo, 2018. http://www.teses.usp.br/teses/disponiveis/9/9142/tde-12112018-124550/.
In this study we evaluated the role of tryptophan (Trp) metabolism in cervix homeostasis, bacterial vaginosis and HPV-associated lesions. The importance of Trp metabolism is due to its action on microorganisms and immune cells. Tryptophan consumption has been identified as a way to controlling bacterial growth limiting infection. On the other hand, the oxidation of Trp produces kynurenine (Kyn) which plays a key role in immunological tolerance. The formation of Kyn occurs through the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO). IDO is the most studied of them within the context of infections / immune escape. More recently, TDO has also been considered in studies of cancer progression. In this thesis, we were interested in cervicovaginal epithelium IDO expression in women with bacterial vaginosis and of IDO and TDO in cervical samples of women with different degrees of cervical lesion associated with HPV. A total of 165 women attended at CAISM/UNICAMP were divided into two groups: a case group composed of women with low or high grade lesions and invasive carcinoma (n = 42) and a control group composed of women with normal cytology, independent to present genital infection (n =123). IDO was evaluated by immunocytochemistry in liquid-based cytology and IDO and TDO in cervical biopsies. Women with bacterial vaginosis had increased IDO expression in squamous cells compared to women without bacterial vaginosis (OR = 7.41, 95% CI = 2.50- 21.74; p<0.0001). In normal vaginal epithelium with or without HPV infection there was a mild IDO expression in squamous cells. In the presence of cervical intraepithelial lesions or squamous cell carcinoma, there was an increase in the number of IDO-positive dysplastic squamous cells and leukocytes; increase in IDO can also be observed in organotypic skin cultures transduced with HPV-16 E6/E7 oncoproteins. In cervical lesions, as observed for IDO, TDO was expressed in leukocytes, especially infiltrates in the stromal region and in the wall of blood vessels. The basal expression of IDO in the normal cervical epithelium and its positive regulation in HPV infection and associated lesions suggests the participation of Trp metabolism in the immunosuppressive mechanisms involved in the disease. Although some previous data have already considered the role of IDO, as far as we know this is the first evidence of the participation of TDO in the vaginal epithelium, cervical intraepithelial neoplasia and squamous cell carcinoma. In addition, in leukocytes, especially those with a typical polymorphonuclear morphology, appear to be important sources of IDO in the uterine cervix.
Parigiani, Mattia. "Accorgimenti nutrizionali volti all'ottimizzazione del metabolismo del triptofano in condizioni fisiologiche e patologiche." Bachelor's thesis, Alma Mater Studiorum - Università di Bologna, 2020. http://amslaurea.unibo.it/22079/.
Michel, Marion. "Conception, synthèse et validation de molécules hétérocycliques fluorées ciblant IDO et/ou TDO pour le traitement de la neuroinflammation et son diagnostic par imagerie 18F-TEP." Electronic Thesis or Diss., Orléans, 2023. http://www.theses.fr/2023ORLE1051.
The ageing of the global population has led to an increase in the number of people suffering from neurodegenerative diseases, with the concomitant lack of curative treatments. Consequently, the development of new diagnostic and therapeutic tools to improve care for these patients has become a major research challenge.Many of these diseases, including Alzheimer's, Parkinson's and Lou Gehrig's disease, follow the same pathophysiological process known as neuroinflammation. This mechanism of cerebral immunity, which emerges at the earliest stages of the disease, has recently become the focus of scientific interest. Indoleamine 2,3-dioxygenase (IDO) and Tryptophan 2,3-dioxygenase (TDO) enzymes, involved in the catabolism of tryptophan, have been identified as being over-expressed in the context of neuroinflammation and appear to play a key role in it.Positron emission tomography (PET) is a precision imaging-technique giving access to the functional study of organs such as the brain. This non-invasive technique can thus be used for the diagnosis, monitoring and quantification of CNS diseases by the administration of specific radiotracers targeting this area.In order to design powerful fluorinated radioligands specific to the IDO and TDO enzymes, we began this research project by transposing IDO ligands form the literature into new 18F-labelled radioligands. We then developed original chemical series with a [6-5] or [6-5-5] scaffold to obtain mixed or selective TDO ligands. Finally, the exploration of the chemical space in the heterocyclic domain led us to the novel design of fluorinated TDO-selective ligands with a high potential for development
Частини книг з теми "IDO/TDO":
Prendergast, George C., William J. Malachowski, Arpita Mondal, Peggy Scherle, and Alexander J. Muller. "IDO/TDO Inhibition in Cancer." In Oncoimmunology, 289–307. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-62431-0_17.
Тези доповідей конференцій з теми "IDO/TDO":
Coma, Silvia, Jill Cavanaugh, James Nolan, Jeremy Tchaicha, Karen McGovern, Everett Stone, Candice Lamb, et al. "Abstract 3757: Targeting the IDO/TDO pathway through degradation of the immunosuppressive metabolite kynurenine." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3757.
Tchaicha, Jeremy, Karen McGovern, Luis Felipe Campesato, Silvia Coma, Xiaoyan Michelle Zhang, Meghan Walsh, Jill Cavanaugh, Taha Merghoub, Jedd Wolchok, and Mark Manfredi. "Abstract 4723: Targeting the IDO and TDO pathway through inhibition of the aryl hydrocarbon receptor." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4723.
Campesato, Luis F., Sadna Budhu, Mathieu Gigoux, Jeremy Tchaicha, Stephane Pourpe, Cailian Liu, Dmitriy Zamarin, et al. "Abstract PR05: Blockade of AHR activation by IDO/TDO-derived kynurenine restricts cancer immune suppression." In Abstracts: AACR Special Conference on Tumor Immunology and Immunotherapy; November 27-30, 2018; Miami Beach, FL. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/2326-6074.tumimm18-pr05.
Zhang, Michelle, Everett Stone, Todd A. Triplett, Kendra Triplett, Candice Lamb, Christos S. Karamitros, John Blazek, George Georgiou, and Mark G. Manfredi. "Abstract 5570: A novel approach to targeting the IDO/TDO pathway through degradation of the immunosuppressive metabolite kynurenine." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-5570.
Mautino, Mario R., Richard A. Metz, Firoz Jaipuri, Jesse Waldo, Sanjeev Kumar, Agnieszka Marcinowicz-Flick, Hima Potturi, et al. "Abstract 1633: Novel specific- and dual- tryptophan-2,3-dioxygenase (TDO) and indoleamine-2,3-dioxygenase (IDO) inhibitors for tumor immunotherapy." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-1633.
Noubade, Rajkumar, Holbrook Kohrt, Lisa Marshall, Idit Sagiv-Barfi, Jonathan Hebb, Cariad Chester, Amanda Rajapaksa, et al. "Abstract 3648: Expression of tolerogenic enzymes IDO-1, IDO-2 and TDO in commonly used mouse tumor models and impact on model selection for evaluation of immunosuppression reversal by novel therapeutics." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3648.
Wise, Alan, Barry E. McGuinness, Sarah C. Trewick, Phillip M. Cowley, Nicola Bevan, Clare Szybut, and Thomas J. Brown. "Abstract 4292: In vitro kynurenine modulation by novel dual-acting and selective tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) inhibitors." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4292.
Sordillo, Laura A., Lin Zhang, Peter Sordillo, and Robert R. Alfano. "Alzheimer’s disease: label-free fluorescence shows increases in indoleamine 2,3-dioxygenase (IDO) or tryptophan 2,3-dioxygenase (TDO) activity in affected areas of the brain." In Optical Biopsy XVII: Toward Real-Time Spectroscopic Imaging and Diagnosis, edited by Robert R. Alfano, Stavros G. Demos, and Angela B. Seddon. SPIE, 2019. http://dx.doi.org/10.1117/12.2513384.