Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes

Maia, Luísa B.; Moura, José J. G.

doi:10.1016/j.redox.2018.08.020

Cited by 44 publications

(32 citation statements)

References 195 publications

(314 reference statements)

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“…Two main pathways, reductive and oxidative, appear to explain NO synthesis in plants. One is based on the reduction of nitrite, and the other involves the oxidation of aminated molecules, such as the amino acid arginine [15].…”

Section: Introductionmentioning

confidence: 99%

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Tejada‐Jiménez

Llamas

Galván

et al. 2019

Plants

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Nitric oxide is a gaseous secondary messenger that is critical for proper cell signaling and plant survival when exposed to stress. Nitric oxide (NO) synthesis in plants, under standard phototrophic oxygenic conditions, has long been a very controversial issue. A few algal strains contain NO synthase (NOS), which appears to be absent in all other algae and land plants. The experimental data have led to the hypothesis that molybdoenzyme nitrate reductase (NR) is the main enzyme responsible for NO production in most plants. Recently, NR was found to be a necessary partner in a dual system that also includes another molybdoenzyme, which was renamed NO-forming nitrite reductase (NOFNiR). This enzyme produces NO independently of the molybdenum center of NR and depends on the NR electron transport chain from NAD(P)H to heme. Under the circumstances in which NR is not present or active, the existence of another NO-forming system that is similar to the NOS system would account for NO production and NO effects. PII protein, which senses and integrates the signals of the C–N balance in the cell, likely has an important role in organizing cell responses. Here, we critically analyze these topics.

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Section: Introductionmentioning

confidence: 99%

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Tejada‐Jiménez

Llamas

Galván

et al. 2019

Plants

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Section: Discussionmentioning

confidence: 99%

Effect of Individual, Simultaneous and Sequential Inoculation of Pseudomonas fluorescens and Meloidogyne incognita on Growth, Biochemical, Enzymatic and Nonenzymatic Antioxidants of Tomato (Solanum lycopersicum L.)

Noureldeen

Asif

Ansari

et al. 2021

Plants

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This study was conducted on tomato (Solanum lycopersicum cv. K-21) to investigate the bioprotective nature of Pseudomonas fluorescens and its interactive effects with Meloidogyne incognita in terms of growth biomarkers, changes in biochemical attributes and modulation in antioxidant enzymes of the tomato plant. In this study, we grew tomato plants with M. incognita and P. fluorescens in separate pots, simultaneously and sequentially (15 days prior or post) after 15 days of seed sowing. The sequential inoculation of Mi15→Pf maximally increased the root-knot index and decreased the nematode population. It was also noted that inoculation suppressed the plant growth biomarkers in comparison to control. However, maximum suppression in nematode reproduction and increment in growth and physiological attributes were observed when P. fluorescens was applied 15 days prior to the nematode (Pf15→Mi) as compared to control. All the treatments showed an increase in antioxidant enzymes. Expression of phenol content and defensive enzymes such as peroxidase (POX) and superoxide dismutase (SOD) increased, in contrast to a significant reduction in malondialdehyde (MDA) and hydrogen peroxide (H2O2) contents when compared with the untreated inoculated plants. However, the highest levels of POX and SOD, and a lowest of phenol, MDA and H2O2 were displayed in the treatment Pf15→Mi, followed by Mi+Pf and Mi15→Pf.

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“…Humans are characterized by a single AOX enzyme, while rodents express four isoenzymes (AOX1-4). Both enzymes AOX and XOR are able to generate besides ROS also nitric oxide (NO) (see Maia and Moura 2018;Bender and Schwarz 2018). Under normal culturing conditions of adipocytes, AOX localizes in the cytoplasm of cells ( Fig.…”

Section: Aox Is Expressed In Adipocytes and Links Lds And Mitochondrimentioning

confidence: 99%

Formation and degradation of lipid droplets in human adipocytes and the expression of aldehyde oxidase (AOX)

et al. 2019

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Lipid droplet (LD) binding proteins in mammary glands and in adipocytes were previously compared and striking similar sets of these specific proteins demonstrated. Xanthine oxidoreductase (XOR) together with perilipins and the lactating mammary gland protein butyrophilin play an important role in the secretion process of LDs into milk ducts. In contrast, in adipose tissue and in adipocytes, mainly perilipins have been described. Moreover, XOR was reported in mouse adipose tissue and adipocyte culture cells as "novel regulator of adipogenesis". This obvious coincidence of protein sets prompted us to revisit the formation of LDs in human-cultured adipocytes in more detail with special emphasis on the possibility of a LD association of XOR. We demonstrate by electron and immunoelectron microscopy new structural details on LD formation in adipocytes. Surprisingly, by immunological and proteomic analysis, we identify in contrast to previous data showing the enzyme XOR, predominantly the expression of aldehyde oxidase (AOX). AOX could be detected tightly linked to LDs when adipocytes were treated with starvation medium. In addition, the majority of cells show an enormous interconnected, tubulated mitochondria network. Here, we discuss that (1) XOR is involved-together with perilipins-in the secretion of LDs in alveolar epithelial cells of the lactating mammary gland and is important in the transcytosis pathway of capillary endothelial cells. (2) In cells, where LDs are not secreted, XOR cannot be detected at the protein level, whereas in contrast in these cases, AOX is often present. We detect AOX in adipocytes together with perilipins and find evidence that these proteins might direct LDs to mitochondria. Finally, we here report for the first time the exclusive and complementary localization of XOR and AOX in diverse cell types.

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Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes

Cited by 44 publications

References 195 publications

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes

Effect of Individual, Simultaneous and Sequential Inoculation of Pseudomonas fluorescens and Meloidogyne incognita on Growth, Biochemical, Enzymatic and Nonenzymatic Antioxidants of Tomato (Solanum lycopersicum L.)

Formation and degradation of lipid droplets in human adipocytes and the expression of aldehyde oxidase (AOX)

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