Localization of Nitric-oxide Synthase in Plant Peroxisomes

Barroso, Juan B.; Corpas, Francisco J.; Carreras, Alfonso; Sandalio, Luisa M.; Valderrama, Raquel; Palma, José M.; Lupiáñez, José A.; Rı́o, Luis A. del

doi:10.1074/jbc.274.51.36729

Cited by 330 publications

(220 citation statements)

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“…5 Subcellular compartmentalization of iNOS within peroxisomes has been shown to occur in plants, although it was not associated with any physiologic consequence distinct from that of cytosolic iNOS. 37 Here we show that peroxisomal localization of iNOS can be associated with reduced expression of catalase. Previous studies have indicated that NO can inactivate catalase reversibly in hepatocytes 38 and reduce catalase expression in C6 glioma cells.…”

Section: Discussionmentioning

confidence: 94%

“…Although iNOS has been shown to localize to plant peroxisomes, 37 this is the first report of iNOS expression within animal cell peroxisomes in response to septic stress and, more specifically, in an organ that is one of the body's initial defenses against infections. 44 Kupffer cells, the resident macrophages of the liver, also express iNOS (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

et al. 2002

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Shock states induce the expression of inducible nitric oxide synthase (iNOS) in both Kupffer cells and hepatocytes in the liver, but little is known about its subcellular localization in these cells. Studies were undertaken to characterize the subcellular location of iNOS in hepatocytes in response to sepsis. By immunofluorescence analysis, intraperitoneal challenge with bacterial lipopolysaccharide induced cytosolic iNOS in Kupffer cells but punctate labeling in hepatocytes. Cultured rat hepatocytes exposed to interferon gamma, interleukin 1, and tumor necrosis factor ␣ showed iNOS protein expression within peroxisomes as early as 4 hours after stimulation, as determined by colabeling for catalase or PMP70. To a lesser extent, iNOS was also observed associated with the plasma membrane and in undefined intracellular aggregates. S tudies in the past decade have shown that all nitric oxide synthases (NOS), whether constitutive or inducible, are regulated at transcriptional, posttranscriptional, translational, and posttranslational levels. 1 One important aspect of NOS regulation is its subcellular localization. For example, endothelial NOS is localized to the caveolae of endothelial cells, where direct association with caveolin I regulates enzyme activity. 2 Such localization may enhance NO function by concentrating NO release close to the cell surface. The inducible NOS (iNOS; NOS2) isoform, which contributes to inflammatory processes through high NO output, is regulated positively and negatively by cytokines but can also be controlled posttranslationally by NO and/or its reaction products. 1,3,4 Furthermore, this enzyme is found in both particulate and cytosolic cellular pools. 5 Our interest has focused on the regulation and function of iNOS in the liver. This enzyme is readily upregulated in hepatocytes, 6 and human iNOS expression was first detected in hepatocytes. 7 In vivo studies have shown that the consequences of iNOS up-regulation in liver are dependent on the physiologic or pathologic circumstances. Following conditions associated with severe redox stress, iNOS contributes to hepatocellular damage during hemorrhagic shock or hepatic ischemia/reperfusion. 8,9 In contrast, iNOS-generated NO suppresses hepatocyte apoptosis in endotoxemia 10 and following cytokine exposure. 11 To better understand how iNOS functions within hepatocytes as well as factors that might determine the fate of NO in the liver, we undertook a study to characterize its subcellular localization. We show that iNOS localizes to the peroxisome, plasma membrane, and cytoplasm. Interestingly, increased expression of iNOS is associated with decreased catalase expression.

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

et al. 2002

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“…Initial evidence was based on the production of NO and L-citrulline from L-Arg by plant extracts and/or its inhibition by specific inhibitors, typically inactive substrate analogs (Cueto et al, 1996;Ninnemann and Maier, 1996;Delledonne et al, 1998;Durner et al, 1998). In a different approach, the use of antibodies against mammalian NOS enzymes detected immunoreactive proteins in different plant cell compartments (Barroso et al, 1999;Ribeiro et al, 1999). However, subsequent identification of the cross-reacting polypeptides using matrix-assisted laser desorption/ionization-time of flight mass spectrometry demonstrated that the mammalian antibodies recognized plant proteins unrelated to NOS (Butt et al, 2003), making this strategy inappropriate to infer the presence of plant NOS.…”

Section: First Leads In the Hunt For Plant Nos Enzymesmentioning

confidence: 99%

Hunting for Plant Nitric Oxide Synthase Provides New Evidence of a Central Role for Plastids in Nitric Oxide Metabolism

et al. 2009

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Nitric oxide (NO) has emerged as a central signaling molecule in plants and animals. However, the long search for a plant NO synthase (NOS) enzyme has only encountered false leads. The first works describing a pathogen-induced NOS-like plant protein were soon retracted. New hope came from the identification of NOS1, an Arabidopsis thaliana protein with an atypical NOS activity that was found to be targeted to mitochondria in roots. Although concerns about the NO-producing activity of this protein were raised (causing the renaming of the protein to NO-associated 1), compelling data on its biological role were missing until recently. Strong evidence is now available that this protein functions as a GTPase that is actually targeted to plastids, where it might be required for ribosome function. These and other results support the argument that the defective NO production in loss-of-function mutants is an indirect effect of interfering with normal plastid functions and that plastids play an important role in regulating NO levels in plant cells.

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“…NO stimulates seed germination in different species, and a decrease in NO levels has been associated with fruit maturation and senescence of flowers (Beligni and Lamattina, 2001). NO production has been observed in response to several biotic and abiotic stimuli, such as pathogen infection, bacterial elicitors, high temperature, osmotic stress, and UV-B light (Durner et al, 1998;Barroso et al, 1999;Krause and Durner, 2004;Zeidler et al, 2004;Shapiro, 2005;Corpas et al, 2008;Kolbert et al, 2008;Zhao et al, 2009).…”

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confidence: 99%

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

et al. 2010

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Mitochondria play an essential role in nitric oxide (NO) signal transduction in plants. Using the biotin-switch method in conjunction with nano-liquid chromatography and mass spectrometry, we identified 11 candidate proteins that were S-nitrosylated and/or glutathionylated in mitochondria of Arabidopsis (Arabidopsis thaliana) leaves. These included glycine decarboxylase complex (GDC), a key enzyme of the photorespiratory C 2 cycle in C3 plants. GDC activity was inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues. Gas-exchange measurements demonstrated that the bacterial elicitor harpin, a strong inducer of reactive oxygen species and NO, inhibits GDC activity. Furthermore, an inhibitor of GDC, aminoacetonitrile, was able to mimic mitochondrial depolarization, hydrogen peroxide production, and cell death in response to stress or harpin treatment of cultured Arabidopsis cells. These findings indicate that the mitochondrial photorespiratory system is involved in the regulation of NO signal transduction in Arabidopsis.

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Localization of Nitric-oxide Synthase in Plant Peroxisomes

Abstract: The presence of nitric-oxide synthase (NOS) in peroxisomes from leaves of pea plants (Pisum sativum L.) was studied. Plant organelles were purified by differential and sucrose density gradient centrifugation. In purified intact peroxisomes a Ca

Cited by 330 publications

References 42 publications

Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

Hunting for Plant Nitric Oxide Synthase Provides New Evidence of a Central Role for Plastids in Nitric Oxide Metabolism

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

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