Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30044 (antioxidant enzyme)
 8,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mesorhizobium ciceri, Mesorhizobium mediterraneum and Sinorhizobium medicae strains showed different symbiotic performances when inoculated to chickpea (Cicer arietinum L., cv. chetoui) at unstressed conditions and under salt stress. The analysis of nodular proteic composition and antioxidant enzyme activities revealed a polymorphism of patterns on SDS and native PAGE suggesting a potential dependence on the bacterial partner. Salt effect was analysed on plant growth, nitrogen fixation and antioxidant enzymes. M. ciceri, the most efficient strain, seemed to allow a best tolerance to chickpea plants under salt stress. This constraint did not affect the nodular superoxide dismutase (SOD, E.C. 1.15.1.1) activity of the symbiosis implicating the latter strain. This symbiosis showed the least decrease for the nodule protein level and the catalase (CAT, E.C. 1.11.1.6) activity, and the highest increase of peroxidase (POX, E.C. 1.11.1.7) activity that seemed to be related with the tolerance to salt.
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PMID:Rhizobial strain involvement in plant growth, nodule protein composition and antioxidant enzyme activities of chickpea-rhizobia symbioses: modulation by salt stress. 1547 77

All members of R. glutinosa show the unique characteristic of intrinsic tolerance to paraquat (PQ). Antioxidant enzymes have been proposed to be the primary mechanism of PQ resistance in several plant species. Therefore, the antioxidant enzyme systems of R. glutinosa were evaluated by comparatively analyzing cellular antioxidant enzyme levels, and their responses of oxidative stresses and hormones. The levels of ascorbate peroxidase (APX), glutathione reductase (GR), non-specific peroxidase (POX), and superoxide dismutase (SOD) were 7.3-, 4.9-, 2.7- and 1.6-fold higher in PQ-tolerant R. glutinosa than in PQ-susceptible soybeans. However, the activity of catalase (CAT) was about 12-fold higher in the soybeans. The activities of antioxidant enzymes reduced after PQ treatment in the two species, with the exception of POX and SOD in R. glutinosa, which increased by about 40 %. Interestingly, the activities of APX, SOD and POX in R. glutinosa, relative to those in soybeans, were further increased by 49, 67 and 93 % after PQ treatment. The considerably higher intrinsic levels, and increases in the relative activities of antioxidant enzymes in R. glutinosa under oxidative stress support the possible role of these enzymes in the PQ tolerance of R. glutinosa. However, the relatively lower levels of SOD versus PQ tolerance, and the mixed responses of antioxidant enzymes to stresses and hormones, suggest a possible alternative mechanism(s) for PQ tolerance in R. glutinosa.
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PMID:The activities of antioxidant enzymes in response to oxidative stresses and hormones in paraquat-tolerant Rehmannia glutinosa plants. 1547 27

The present work examined the hypothesis that brain ischemic tolerance induced by ischemic preconditioning (IPC) is triggered by an initial oxidative stress and is associated with an increase in antioxidant enzyme activities as one end-effector of the neuroprotection. Wistar rats were preconditioned by a single 3-min occlusion of the middle cerebral artery. After a various duration of reperfusion (30 min, 24, 72 or 168 h), rats were subjected to a 60-min focal ischemia and sacrificed 24 h later. Cerebral infarcts were significantly reduced when performed during the 24- to 72-h time window after IPC. The pretreatment with the protein synthesis inhibitor, cycloheximide (1 mg/kg, i.p., 30 min prior to IPC), completely suppressed the neuroprotection. The free radical scavenger, dimethylthiourea (DMTU; 300 mg/kg, i.p., 30 min prior to IPC) and the antioxidant ebselen (10 mg/kg, oral cramming, 2 h before and 12 h after IPC) also abolished the IPC-induced protection of the brain. Nevertheless, IPC did not induce any delayed changes in antioxidant enzyme (superoxide dismutase, glutathion peroxidase) activities nor in the neuronal expression of Mn and Cu/Zn superoxide dismutase. These results indicate that an initial oxidative stress could be involved as a trigger of IPC, while antioxidant enzymes do not play a key role as end-effectors in such a neuroprotection.
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PMID:Brain ischemic preconditioning is abolished by antioxidant drugs but does not up-regulate superoxide dismutase and glutathion peroxidase. 1549 54

Oral streptococci such as Streptococcus gordonii are facultative anaerobes that initiate biofilm formation on tooth surfaces. An isolated S. gordonii::Tn917-lac biofilm-defective mutant contained a transposon insertion in an open reading frame (ORF) encoding a homolog of NosX of Ralstonia eutropha, a putative maturation factor of nitrous oxide reductase. Located downstream are two genes, qor1 and qor2, predicted to encode two putative NADPH quinone oxidoreductases. These three genes are cotranscribed, forming a putative oxidative stress response (osr) operon in S. gordonii. Inactivation of nosX, qor1, or qor2 resulted in biofilm-defective phenotypes. Expression of nosX, measured by the beta-galactosidase activity of the nosX::Tn917-lac mutant, was growth-phase dependent and enhanced when grown under aerobic conditions or in the presence of paraquat. Real-time reverse transcription-PCR revealed that nosX-specific mRNA levels were increased approximately 8.4 and 3.5 fold in biofilm-derived cells grown on plastic and glass, respectively, when compared to planktonic cells. Expression of nosX increased 19.9 fold in cells grown under aerated aerobic conditions and 4.7 fold in cells grown under static aerobic conditions. Two ORFs immediately adjacent to the osr operon encode a putative NADH oxidase (Nox) and a putative thiol-specific antioxidant enzyme (AhpC, for alkyl hydroperoxide peroxidase C). Expression of nox and ahpC was also significantly increased in cells grown under aerated and static aerobic conditions when compared to anaerobic conditions. In addition, nox expression was increased in biofilm cells compared to planktonic cells. These genes may be part of an island that deals with oxidoreductive response, some of which may be important in S. gordonii biofilm formation.
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PMID:Role of a nosX homolog in Streptococcus gordonii in aerobic growth and biofilm formation. 1557 67

The influence of the intestine cestode Botriocephalus gregarius on the antioxidant enzyme system in the liver and muscle of its host, the Black Sea flounder Psetta maxima maeotica, was studied. The significant increase of superoxidedismutase activity in examined tissues and changes of catalase and peroxidase activities were detected. High correlation (r > or = 0.6) between enzyme activities and the parasite number was noted. The possibility to use antioxidant enzyme activity as biomarkers of the parasite invasion in fish is discussed.
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PMID:[The influence of the parasite invasion on antioxidant enzyme activity in the liver and muscles of a host, the Black Sea flounder Psetta maxima maeotica]. 1565

The effects of soil and foliar phosphorus supplementation on the activities and levels of superoxide dismutase (SOD), guaiacol peroxidase (POX), and ascorbate peroxidase (APX) in tomato fruits were evaluated by determining enzyme activities and isoenzyme analysis. Both protein levels and enzyme activities varied depending on the variety and season. In general, phosphorus supplementation did not alter SOD, POX, and APX activities significantly;however, some treatments showed season- and stage-specific enhancement in activities as noticed with hydrophos and seniphos supplementation. Three different SOD isozymes were observed, and these isozymes showed very similar staining intensities in response to P application and during the three developmental stages studied. Two major isozymes of POX and two different APX isozymes were observed at all the developmental stages. The results suggest that antioxidant enzyme activities may be influenced by the availability of phosphorus, but are subject to considerable variation depending on the developmental stage and the season.
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PMID:Effects of phosphorus fertilizer supplementation on antioxidant enzyme activities in tomato fruits. 1574 37

In preliminary experiments it was found that Escherichia coli strains AB1157 and KS400 are different in their abilities to grow under various oxygen levels in cultivation medium: the first strain does not grow under high oxygen conditions, unlike the second one. To investigate whether the damage to cellular components due to production of reactive oxygen species (ROS) was responsible for this difference, the intensity of free radical oxidation of proteins and lipids as well as the activities of selected antioxidant and associated enzymes (superoxide dismutase, catalase, peroxidase, glutathione reductase, glucose-6-phosphate dehydrogenase) were compared in the two strains. The level of thiobarbituric acid-reactive substances was 1.8-2.5-fold higher in AB1157 than in KS400, but the concentration of carbonyl proteins was lower in the AB1157 strain. In both strains growth under higher oxygen levels resulted in higher superoxide dismutase and peroxidase activities in both exponential and stationary phases. Overall, the activities of antioxidant enzymes were always higher in the KS400 strain than in AB1157. The results for both lipid and protein oxidative damage and antioxidant enzyme activities suggest that the differences in oxygen tolerance between these two strains may be due to their different abilities to cope with ROS.
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PMID:Possible reasons for difference in sensitivity to oxygen of two Escherichia coli strains. 1589 8

A rice pse(t) (premature senescence, tentatively) mutant line, was isolated from 4,500 independent T-DNA inserted transgenic lines. The symptoms of premature senescence appeared more severely than those of the control plants (Zhonghua 11, japonica) at the last development stage. To characterize the mutant and provide basic information on the candidate genes by mapping to a physical region of 220-kb, experiments were carried out in two phytotrons under controlled temperature of 24 degrees C and 28 degrees C, respectively. The content of chlorophyll, soluble protein and MDA (malondialdehyde), net photosynthesis, the antioxidant enzyme activities of SOD (superoxide dismuase) (EC 1.15.1.1) and POD (peroxidase) (EC 1.11.1.7) and the peptidase activities of leaves were measured from top to bottom according to the leaf positions at the flowering stage. Compared with the control plant, the mutant showed the following characteristics: (1) Higher net photosynthesis rate (P(n)) appeared in the 1st and 2nd leaves, contents of chlorophyll and soluble protein were also higher in the 1st leaf; (2) The activities of SOD, POD and peptidase were higher according to the leaf position from top to bottom; (3) The symptom of premature senescence was accelerated in the mutant at 28 degrees C treatment. The MDA content and the SOD and POD activities between the 24 degrees C and 28 degrees C treatment mutants were not significantly different. Content of chlorophyll and soluble protein of leaves mutant decreased rapidly at 28 degrees C treatment. The results show that pse(t) is sensitive to high temperature. The probable function of PSE(T) is discussed.
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PMID:Isolation and physiological characteristics of a premature senescence mutant in rice (Oryza sativa L.). 1605 15

Catalase is a highly conserved heme-containing antioxidant enzyme known for its ability to degrade hydrogen peroxide into water and oxygen. In low concentrations of hydrogen peroxide, the enzyme also exhibits peroxidase activity. We report that mammalian catalase also possesses oxidase activity. This activity, which is detected in purified catalases, cell lysates, and intact cells, requires oxygen and utilizes electron donor substrates in the absence of hydrogen peroxide or any added cofactors. Using purified bovine catalase and 10-acetyl-3,7-dihydroxyphenoxazine as the substrate, the oxidase activity was found to be temperature-dependent and displays a pH optimum of 7-9. The Km for the substrate is 2.4 x 10(-4) m, and Vmax is 4.7 x 10(-5) m/s. Endogenous substrates, including the tryptophan precursor indole, the neurotransmitter precursor beta-phenylethylamine, and a variety of peroxidase and laccase substrates, as well as carcinogenic benzidines, were found to be oxidized by catalase or to inhibit this activity. Several dietary plant micronutrients that inhibit carcinogenesis, including indole-3-carbinol, indole-3-carboxaldehyde, ferulic acid, vanillic acid, and epigallocatechin-3-gallate, were effective inhibitors of the activity of catalase oxidase. Difference spectroscopy revealed that catalase oxidase/substrate interactions involve the heme-iron; the resulting spectra show time-dependent decreases in the ferric heme of the enzyme with corresponding increases in the formation of an oxyferryl intermediate, potentially reflecting a compound II-like intermediate. These data suggest a mechanism of oxidase activity involving the formation of an oxygen-bound, substrate-facilitated reductive intermediate. Our results describe a novel function for catalase potentially important in metabolism of endogenous substrates and in the action of carcinogens and chemopreventative agents.
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PMID:Characterization of the oxidase activity in mammalian catalase. 1607 30

Living conditions for plants in the mountains become increasingly less favorable with increasing altitude. In the alpine region, the plants are commonly exposed to daily rather than seasonal temperature fluctuations and by frequent freezing temperature. To elucidate the freezing tolerance mechanism of alpine plants, Saussurea laniceps Hand.-Mazz. was used as a model plant. It is a perennial herbal plant distributed in alpine regions of Yunnan and Tibet of China. It can survive on mountains with elevations over 4000 m. Wild S. laniceps plants are propagated only by seeds in the alpine areas. Micropropagation of S. laniceps through seed was a desirable method to get enough seedlings for freezing research. Micropropagation through plantlets derived from germinated S. laniceps seeds collected from Tibet was achieved successfully. Activities of antioxidant enzyme and solute contents were investigated in plantlets of S. laniceps. Freezing tolerance in plantlets increased after 7 or 15 d of cold-hardening (Table 1). Cold-hardening (2 degrees C) increased the activities of SOD, peroxidase, and catalase (Fig.1) in plantlets. A similar increase was also observed in the protein and proline content (Fig.1), whereas soluble carbohydrates changed little (Fig.1). These results obtained suggest that the higher activities of SOD, peroxidase, and catalase, as well as the higher protein and proline content may be biochemical adaptation for freezing toleranc in cold-hardened S. laniceps plantlets. Interestingly, deacclimation was slow; even after the plants were placed again under a temperature of 21-23 degrees C for 5 d, the higher freezing hardiness, enzyme activities, protein and proline content acquired after cold acclimation remained. In conclusion, our plantlet cultures have proved to be good materials for experimentation on freezing resistance in study of freezing-resistance mechanism in the alpine plant S. laniceps.
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PMID:[Effects of cold-hardening on freezing tolerance and antioxidant enzyme activities in plantlets of Saussurea laniceps Hand.-Mazz]. 1612 Oct 17


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