Impact of indoleamine 2,3-dioxygenase on the antioxidant system in the placentas of severely pre-eclamptic patients

Nishizawa, Haruki; Suzuki, Manami; Pryor-Koishi, Kanako; Sekiya, Takao; Tada, Shin; Kurahashi, Hiroki; Udagawa, Yasuhiro

doi:10.3109/19396368.2011.587590

Cited by 20 publications

(10 citation statements)

References 26 publications

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“…This is a fairly local effect, as ROS cannot cross the cell membrane. In this issue of SBiRM, Nishizawa et al [2011], demonstrate cellular co-localization of IDO and DNA oxidative damage, supporting the hypothesis that these two findings may be related. IDO can utilize either oxygen (O 2 ) or superoxide (O 2 .-) for its activity and superoxide may serve as both substrate and co-factor for IDO [Thomas and Stocker 1999].…”

supporting

confidence: 64%

Placental IDO and oxidative damage in pre-eclampsia: fresh chicken or fresh eggs?

Pennington

Schulz

Schust

2011

Systems Biology in Reproductive Medicine

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supporting

confidence: 64%

Placental IDO and oxidative damage in pre-eclampsia: fresh chicken or fresh eggs?

Pennington

Schulz

Schust

2011

Systems Biology in Reproductive Medicine

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“…In humans, IDO1 is induced within the vascular endothelium of disease states such as pre-eclampsia [571], as well as in resistance vessels and cardiac tissue during septic shock in response to various infections including S. aureus, E. coli, Enterobacter cloacae, Serratia marcescens, Legionella pneumophila, Enterococcus spp., Streptococcus spp., and coagulase-negative Staphylcoccus and Klebsiella [479]. In human sepsis, IDO1 expression and activity positively correlates with the degree of hypotension [479].…”

Section: Vascular Tone and Blood Pressurementioning

confidence: 99%

Role of indoleamine 2,3-dioxygenase in health and disease

et al. 2015

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IDO1 (indoleamine 2,3-dioxygenase 1) is a member of a unique class of mammalian haem dioxygenases that catalyse the oxidative catabolism of the least-abundant essential amino acid, L-Trp (L-tryptophan), along the kynurenine pathway. Significant increases in knowledge have been recently gained with respect to understanding the fundamental biochemistry of IDO1 including its catalytic reaction mechanism, the scope of enzyme reactions it catalyses, the biochemical mechanisms controlling IDO1 expression and enzyme activity, and the discovery of enzyme inhibitors. Major advances in understanding the roles of IDO1 in physiology and disease have also been realised. IDO1 is recognised as a prominent immune regulatory enzyme capable of modulating immune cell activation status and phenotype via several molecular mechanisms including enzyme-dependent deprivation of L-Trp and its conversion into the aryl hydrocarbon receptor ligand kynurenine and other bioactive kynurenine pathway metabolites, or non-enzymatic cell signalling actions involving tyrosine phosphorylation of IDO1. Through these different modes of biochemical signalling, IDO1 regulates certain physiological functions (e.g. pregnancy) and modulates the pathogenesis and severity of diverse conditions including chronic inflammation, infectious disease, allergic and autoimmune disorders, transplantation, neuropathology and cancer. In the present review, we detail the current understanding of IDO1's catalytic actions and the biochemical mechanisms regulating IDO1 expression and activity. We also discuss the biological functions of IDO1 with a focus on the enzyme's immune-modulatory function, its medical implications in diverse pathological settings and its utility as a therapeutic target.

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“…In this model, 8-hydroxy-2′-deoxy-guanosine (8-OHdG, a marker for oxidative damage to DNA) was found to be higher in preeclamptic than normotensive pregnancies. Moreover, immunohistochemical signals of 8-OHdG inversely correlated with Trp-degrading activity, suggesting that a decrease in the antioxidant activity of IDO1 contributed to the pathogenesis of this disorder (122). …”

Section: Altered Trp Degradation In Pregnancy Pathologymentioning

confidence: 99%

The Role of Placental Tryptophan Catabolism

2014

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This review discusses the mechanisms and consequences of degradation of tryptophan (Trp) in the placenta, focusing mainly on the role of indoleamine 2,3-dioxygenase-1 (IDO1), one of three enzymes catalyzing the first step of the kynurenine pathway of Trp degradation. IDO1 has been implicated in regulation of feto-maternal tolerance in the mouse. Local depletion of Trp and/or the presence of metabolites of the kynurenine pathway mediate immunoregulation and exert antimicrobial functions. In addition to the decidual glandular epithelium, IDO1 is localized in the vascular endothelium of the villous chorion and also in the endothelium of spiral arteries of the decidua. Possible consequences of IDO1-mediated catabolism of Trp in the endothelium encompass antimicrobial activity and immunosuppression, as well as relaxation of the placental vasotonus, thereby contributing to placental perfusion and growth of both placenta and fetus. It remains to be evaluated whether other enzymes mediating Trp oxidation, such as indoleamine 2,3-dioxygenase-2, Trp 2,3-dioxygenase, and Trp hydroxylase-1 are of relevance to the biology of the placenta.

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Impact of indoleamine 2,3-dioxygenase on the antioxidant system in the placentas of severely pre-eclamptic patients

Cited by 20 publications

References 26 publications

Placental IDO and oxidative damage in pre-eclampsia: fresh chicken or fresh eggs?

Placental IDO and oxidative damage in pre-eclampsia: fresh chicken or fresh eggs?

Role of indoleamine 2,3-dioxygenase in health and disease

The Role of Placental Tryptophan Catabolism

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