Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.3.1 (NADPH oxidase)
 11,281 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Our previous results have shown that oxidative stress may reduce the regeneration potential of protoplasts, but only protoplasts that are able to supply extracellularly H(2)O(2) can actually divide (C.I. Siminis, A.K. Kanellis, K.A. Roubelakis-Angelakis [1993] Physiol Plant 87: 263-270; C.I. Siminis, A.K. Kanellis, K.A. Roubelakis-Angelakis [1994] Plant Physiol 1105: 1375-1383; A. de Marco, K.A. Roubelakis-Angelakis [1996a] Plant Physiol 110: 137-145; A. de Marco, K.A. Roubelakis-Angelakis [1996b] J Plant Physiol 149: 109-114). In the present study we have attempted to break down the oxidative burst response into the individual active oxygen species (AOS) superoxide (O(2)(*-)) and H(2)O(2), and into individual AOS-generating systems during the isolation of regenerating tobacco (Nicotiana tabacum L.) and non-regenerating grape (Vitis vinifera L. ) mesophyll protoplasts. Wounding leaf tissue or applying purified cellulase did not elicit AOS production. However, the application of non-purified cellulase during maceration induced a burst of O(2)(*-) and H(2)O(2) accumulation in tobacco leaf, while in grape significantly lower levels of both AOS accumulated. AOS were also generated when protoplasts isolated with purified cellulase were treated with non-purified cellulase. The response was rapid: after 5 min, AOS began to accumulate in the culture medium, with significant quantitative differences between the two species. In tobacco protoplasts and plasma membrane vesicles, two different AOS synthase activities were revealed, one that showed specificity to NADPH and sensitivity to diphenyleneiodonium (DPI) and was responsible for O(2)(*-) production, and a second NAD(P)H activity that was sensitive to KCN and NaN(3), contributing to the production of both AOS. The first activity probably corresponds to a mammalian-like NADPH oxidase and the second to a NAD(P)H oxidase-peroxidase. In grape, only one AOS-generating activity was detected, which corresponded to a NAD(P)H oxidase-peroxidase responsible for the generation of both AOS.
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PMID:The generation of active oxygen species differs in tobacco and grapevine mesophyll protoplasts. 1048 75

In maize (Zea mays L.) cells, the sources of apoplast hydrogen peroxide (H(2)O(2)) induced by abscisic acid (ABA) has been proposed. Histochemical and cytochemical localization of ABA-induced H(2)O(2) production in leaves of maize was examined, using 3, 3-diaminobenzidine (DAB) and cerium chloride (CeCl(3)) staining respectively. Pretreatment with two different inhibitors for each enzymes, with diphenylene iodonium (DPI) and imidazole against NADPH oxidase, NaCN and NaN(3) against peroxidases (POD), and quinacrine and guazatine against polyamine oxidases (PAO), reduced H(2)O(2) accumulation induced by ABA. Among them, NADPH oxidase inhibitors arrested the production of apoplastic H(2)O(2) most strongly (Figs.1,2). Further studies showed that exogenous ABA treatment could enhance the activities of plasma membrane (PM) NADPH oxidase, cell wall POD and apoplast PAO significantly. Moreover, the activity of PM NADPH oxidase kept increasing before 1.5 h, while the other two enzymes began to decrease at 0.5 h within 2 h by ABA treatment (Fig.3). The results suggest that exogenous ABA treatment can lead to significant increases in H(2)O(2) accumulation in apoplast through up-regulating the activities of the PM NADPH oxidases, cell wall POD and apoplast PAO, of which the first one plays a central role in ABA-induced apoplastic H(2)O(2) accumulation.
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PMID:[The mechanism of ABA-induced apoplastic H2O2 accumulation in maize leaves]. 1707 74

The effects of cadmium (Cd) on the accumulation of hydrogen peroxide (H(2)O(2)) and superoxide anion (O(2)(-)) in leaves of Phaseolus aureus and Vicia sativa were investigated. Cadmium at 100 microM significantly increased the production of O(2)(-) and H(2)O(2), as well as the activities of plasma membrane-bound nicotinamide adenine dinucleotide phosphate (NADPH) oxidases and the symplastic and apoplastic activities of superoxide dismutase and ascorbate peroxidase in the leaves of both species. Apoplastic guaiacol peroxidase activity was significantly induced in the leaves of both species, particularly in P. aureus exposed to 100 microM Cd. Experiments with diphenylene iodonium as an inhibitor of NADPH oxidase and NaN(3) as an inhibitor of peroxidase showed that the majority of Cd-induced reactive oxygen species production in the leaves of both species may involve plasma membrane-bound NADPH oxidase and apoplastic peroxidase. Compared to V. sativa, increases in Cd-induced production of O(2)(-) and H(2)O(2) and activities of NADPH oxidase and apoplastic peroxidase were more pronounced in P. aureus. In contrast, V. sativa had higher leaf symplastic superoxide dismutase and ascorbate peroxidase activities than P. aureus. The results indicated that V. sativa was more tolerant to Cd than P. aureus.
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PMID:Cadmium-induced accumulation of hydrogen peroxide in the leaf apoplast of Phaseolus aureus and Vicia sativa and the roles of different antioxidant enzymes. 1926 80

Although glial cells play a major role in the pathogenesis of many neurological diseases by exacerbating neuronal and non-neuronal cell death, the mechanisms involved are unclear. We examined the effects of microglia-(MCM) or astrocyte-(ACM) conditioned media obtained by chemical ischemia on the neuronal injury in SH-SY5Y cells. Chemical ischemia was induced by the treatment with NaN(3) and 2-deoxy-d-glucose for 2h. MCM-treated SH-SY5Y cells showed reduced the viability, increased caspase-3 activity, decreased Bcl-2/Bax ratio, and increased cytochrome c release, increased inflammatory cytokines, and increased reactive oxygen species (ROS) generation. MCM also increased gp91phox nicotinamide adenine dinucleotide phosphate (NADPH) oxidase, which was inhibited by NADPH oxidase inhibitor, apocynin, and gp91phox siRNA. However, ACM did not show any significant changes. The results suggest that microglia activated by ischemic insult may increase reactive oxygen species generation via activation of gp91phox NADPH oxidase, resulting in neuronal injury.
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PMID:Ischemia-activated microglia induces neuronal injury via activation of gp91phox NADPH oxidase. 2003 16

The effects of cadmium (Cd) on the accumulation of hydrogen peroxide (H(2)O(2)) and antioxidant enzyme activities in roots of Solanum nigrum L. and the role of N-acetyl-l-cysteine (NAC) as a cysteine (Cys) donor against Cd toxicity were investigated. Cd at 50 and 200 microM significantly increased the contents of thiobarbituric acid-reactive substances (TBARS), the production of H(2)O(2) and superoxide anion (O(2)(-)), and the activities of catalase, guaiacol peroxidase, ascorbate peroxidase, glutathione peroxidase (GSH-Px), glutathione reductase, and superoxide dismutase. Experiments with diphenylene iodonium as an inhibitor of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and NaN(3) as an inhibitor of peroxidase showed that the major source of Cd-induced reactive oxygen species in the roots may include plasma membrane-bound NADPH oxidase and peroxidase. In addition, the effects of NAC on plant growth, antioxidant enzyme activity, and non-protein thiol content were analyzed. Under Cd stress, the addition of 500 microM NAC decreased the contents of TBARS and production of H(2)O(2) and O(2)(-), but increased levels of Cys and reduced glutathione (GSH), phytochelatins, and activity of GSH-Px in roots. These results suggest that NAC could protect plants from oxidative stress damage, and this protection seems to be performed via increased GSH biosynthesis. Furthermore, NAC treatment also increased the contents of protein thiols in S. nigrum roots. By using size-exclusion chromatography, we found involvement of NAC in the Cd tolerance mechanism through increased biosynthesis of Cd-binding proteins.
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PMID:Cadmium-induced oxidative damage and protective effects of N-acetyl-L-cysteine against cadmium toxicity in Solanum nigrum L. 2048 18