Regulation of indoleamine 2,3-dioxygenase activity in the small intestine and the epididymis of mice☆
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Cited by (87)
Circadian control of kynurenine pathway enzymes in the rat pineal gland, liver, and heart and tissue- and enzyme-specific responses to lipopolysaccharide
2022, Archives of Biochemistry and BiophysicsCitation Excerpt :More importantly, the circadian oscillation in rat liver TDO activity was measured, with a peak around sunset [26,27], which roughly corresponds with the Tdo expression peak at CT10.5 observed in this study. To complete the list of previous observations, the rhythmic activity of IDO2 was reported in mice intestines and epididymides [30]. Omic circadian data are available for mice and rat liver transcriptomes and support the circadian rhythmicity of Kynu and Ido2 [54,55].
Immutol regulates CD4<sup>+</sup>Tregs, CD8<sup>+</sup>Tregs and pDCs via IDO signaling pathway to induce immune tolerance in rat heart allograft transplant
2021, Transplant ImmunologyCitation Excerpt :In recent years, scientists have found that IDO is the rate-limiting enzyme of the kynurenine pathway of tryptophan metabolism, catalyzing the oxidation of tryptophan to N′-formyl L-type guanidine ammonia acid (N′-formyl L-kynurenine) [1–3].
Kynurenine pathway and human systems
2020, Experimental GerontologyCitation Excerpt :Agents that increase the hepatic concentrations of these two reduced dinucleotides, such as glucose, nicotinamide (Badawy and Evans, 1976a) and chronic ethanol administration (Punjani et al., 1979) inhibit TDO activity. By contrast, IDO is not induced by glucocorticoids or activated by haem and is only activated moderately by a large Trp dose (Yoshida et al., 1980; Cook et al., 1980). This limited activation could, as stated above, be due to enzyme inhibition by [Trp] of ≥50 μM.
The Epididymis
2015, Knobil and Neill's Physiology of Reproduction: Two-Volume SetApicomplexan parasite, Eimeria falciformis, co-opts host tryptophan catabolism for life cycle progression in mouse
2012, Journal of Biological ChemistryCitation Excerpt :Three enzymes can initiate the kynurenine pathway, degrading most of the cellular tryptophan into various metabolites collectively termed as kynurenines. IDO1 is constitutively expressed (4, 29, 30) and induced in a variety of cell types, e.g. dendritic cells, macrophages, endothelial cells, and fibroblasts (1, 5, 31, 32). The second enzyme, tryptophan 2,3-dioxygenase, is expressed mainly in the liver, induced by the amino acid itself and regulates tryptophan homeostasis (33).
Deficient tryptophan catabolism along the kynurenine pathway reveals that the epididymis is in a unique tolerogenic state
2011, Journal of Biological ChemistryCitation Excerpt :There is ample evidence that IDO mediates potent immunosuppression in classical immune responses as well as in fetal tolerance, tumor immune resistance, and regulation of autoimmune responses (1–3, 6–8). Thirty years ago, Yoshida et al. (9) reported that rodent epididymal protein extracts exhibited a high IDO activity. Later, Takikawa et al. (10) demonstrated that unlike the classical cytokine-mediated expression of IDO encountered in nearly all mammalian tissues, the epididymal expression of IDO was constitutive and independent of IFN-γ.
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This work was supported in part by research grants from the Naito Foundation, the Matsunaga Science Foundation, the Sakamoto Foundation, Iyakushigen Kenkyu Shinkohkai, the Mitsubishi Foundation, Nippon Shinyaku Co., Ltd., and the Intractable Diseases Division, Public Health Bureau, Ministry of Health and Welfare, Japan and by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture, Japan.
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Present address: First Department of Internal Medicine, Tokyo University Hospital.
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Present address: Department of Pharmacology, Kyoto University Faculty of Medicine.