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At least 1,405 records · Page 78Linked to original sources
PubMed1981

Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates.

Homogenates of perfused rat brain generated oxidized glutathione from reduced glutathione during incubation with dopamine or serotonin. This activity was blocked by pargyline, a monoamine oxidase inhibitor, or by catalase, a scavenger of hydrogen peroxide. These results demonstrate formation of hydrogen peroxide by monoamine oxidase and the coupling of the peroxide to glutathione peroxidase activity. Oxidized glutathione was measured fluorometrically via the oxidation of NADPH by glutathione reductase. In the absence of added dopamine or serotonin, a much smaller amount of reduced glutathione was oxidized; this activity was blocked by catalase, but not by pargyline. Therefore, endogenous production of hydrogen peroxide, not linked to monoamine oxidase activity, was present. These results indicate that glutathione peroxidase (linked to hexose monophosphate shunt activity) can function to eliminate hydrogen peroxide generated by monoamine oxidase and other endogenous sources in aminergic neurons.

Animals↗
PubMed2005

Degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil.

Phanerochaete chrysosporium NRRL 6361 and Pleurotus pulmonarius CBS 664.97 were tested for their ability to grow under nonsterile conditions and to degrade various aromatic hydrocarbons in an aged contaminated soil that also contained high concentrations of heavy metals. After 24 days fungal incubation, carbon-CO2 liberated, an indicator of microbial activity, reached a plateau. At the end of the incubation time (30 days), fungal colonization was clearly visible and was confirmed by ergosterol and cell organic carbon determinations. In spite of unfavorable pH (around 7.4) and the presence of heavy metals, both fungi produced Mn-peroxidase activity. In contrast, laccase and aryl-alcohol oxidase were detected only in the soil treated with P. pulmonarius CBS 664.97 and lignin-peroxidase in that with P. chrysosporium NRRL 6361. No lignin-modifying enzyme activities were present in non-inoculated soil incubated for 30 days (control microcosm). Regardless of the fungus employed, a total removal of naphtalene, tetrachlorobenzene, and dichloroaniline isomers, diphenylether and N-phenyl-1-naphtalenamine, was observed. Significant release of chloride ions was also observed in fungal-treated soil, in comparison with that recorded in the control microcosm. Both fungi led to a significant decrease in soil toxicity, as assessed using two different soil contact assays, including the Lepidium sativum L. germination test and the Collembola mortality test.

Biodegradation, Environmental↗
PubMedDate not supplied

[Optimization of the conditions of immobilization of enzymes in a photopolymeric membrane].

The residual activity of enzymes immobilized in the membrane on the basis on 1-vinyl-2-pyrrolidinone as photopolymerizable composition is studied. It is established, that under conditions of the immobilization at 20 degrees C the residual activity glucoseoxidase is about 35% from a initial level, horseredish peroxidase and urease from Jeack beans--42% and 20%, respectively. In case of an immobilization of beta-glucoseoxidase -50 degrees C it reaches almost 50% from a initial level. It was investigated the influence of different sources of UV-radiation and different substances on stability of the enzymes in the composition and in the immobilization matrix at storage. Dynamic of changes of enzyme activity at the photoimmobilization was characterized, and also the requirements for providing of its maximal storage was selected.

Drug Storage↗
PubMed2002

Complexities in ETS-domain transcription factor function and regulation: lessons from the TCF (ternary complex factor) subfamily. The Colworth Medal Lecture.

The ETS-domain transcription factor family can be divided into a series of subfamilies. Elk-1 represents the founding member of the ternary complex factor (TCF) subfamily. By focusing on the TCF subfamily, we can demonstrate the complexities that exist in the function and regulation of ETS-domain transcription factors. This article focuses on Elk-1 in detail and summarizes the functions of other TCFs. The key themes covered include the domain structure of the TCFs, the mechanisms of complex formation with serum response factor, regulation of TCFs by mitogen-activated protein kinase cascades, and transcriptional regulatory properties of the TCFs. Finally, the emerging role of the TCFs in vivo is discussed. A picture is developing indicating that, while these proteins exhibit significant sequence and functional conservation, key differences in their structure and regulation are being identified which may relate to unique functions of these proteins in vivo.

Amino Acid Sequence↗
PubMed1976

The effect of oxygen on the enzymes concerned in the metabolism of 5-hydroxytryptamine by rat brain and liver preparations.

1. The effect of oxygen concentration at 1 atm on rat enzyme systems concerned in the synthesis and degradation of 5-hydroxytryptamine was studied in vitro. 2. Oxygen activated tryptophan hydroxylase and the deamination of both 5-hydroxytryptamine and tyramine by monoamine oxidase. 3. Oxygen did not affect the activities of 5-hydroxytryptophan decarboxylase or peroxidase.

Air↗
PubMed2007

Larval feeding induced defensive responses in tobacco: comparison of two sibling species of Helicoverpa with different diet breadths.

Plants respond differently to damage by different herbivorous insects. We speculated that sibling herbivorous species with different host ranges might also influence plant responses differently. Such differences may be associated with the diet breadth (specialization) of herbivores within a feeding guild, and the specialist may cause less intensive plant responses than the generalist. The tobacco Nicotinana tabacum L. is the common host plant of a generalist Helicoverpa armigera (Hübner) and a specialist H. assulta Guenée (Lepidoptera, Noctuidae). The induced responses of tobacco to feeding of these two noctuid herbivores and mechanical wounding were compared. The results showed that the feeding of the specialist H. assulta and the generalist H. armigera resulted in the same inducible defensive system, but response intensity of plants was different to these two species. Inductions of jasmonic acid (JA), lipoxygenase (LOX), and proteinase inhibitors (PIs) were not significantly different concerning these two species, but H. assulta caused the less intensive foliar polyphenol oxidase (PPO) increase, more intensive nicotine and peroxidase (POD) increases in tobacco than H. armigera. The defensive response of plant to herbivores with different diet breadth seems to be more complicated than we expected, and the specialist does not necessarily cause less intensive plant responses than the generalist.

Animals↗
PubMed1980

Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase.

Euglena gracilis was found to contain a peroxidase that specifically require L-ascorbic acid as the natural electron donor in the cytosol. The presence of an oxidation-reduction system metabolizing L-ascorbic acid was demonstrated in Euglena cells. Oxidation of L-ascorbic acid by the peroxidase, and the absence of ascorbic acid oxidase activity, suggests that the system functions to remove H2O2 in E. gracilis, which lacks catalase.

Ascorbate Peroxidases↗
PubMed2001

Mechanisms of survival of necrotrophic fungal plant pathogens in hosts expressing the hypersensitive response.

The hypersensitive response (HR), elicited when resistant hosts are infected by incompatible races of biotrophic fungi, has been researched extensively. New studies on host responses to necrotrophic fungi are beginning to show that when the HR occurs in hosts colonized by necrotrophs, fungal growth is accelerated rather than retarded. We review current knowledge about how necrotrophs survive in host plants in which the HR is expressed. We discuss how necrotrophs cope with the environmental factors formed as a result of the HR. Necrotrophs contain an array of enzymes, which can help in exploiting the hostile environment in order to colonize the host and to remove or inactivate active oxygen species (AOS). Among this array of enzymes are superoxide dismutase (SOD), peroxidases, catalase, and perhaps laccases and polyphenol oxidases. Of these, only SOD and catalase have been studied in any detail. The precise significance of SOD and catalase in host invasion and fungal resistance is still not adequately known. The importance of different peroxidases is also still far from clear. We speculate that AOS species may trigger the response of necrotrophs to the host environment.

Fungi↗
PubMed1991

Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase.

Tobacco (Nicotiana tabacum) plants transformed with a chimeric tobacco anionic peroxidase gene have previously been shown to synthesize high levels of peroxidase in all tissues throughout the plant. One of several distinguishable phenotypes of transformed plants is the rapid browning of pith tissue upon wounding. Pith tissue from plants expressing high levels of peroxidase browned within 24 hours of wounding, while tissue from control plants did not brown as late as 7 days after wounding. A correlation between peroxidase activity and wound-induced browning was observed, whereas no relationship between polyphenol oxidase activity and browning was found. The purified tobacco anionic peroxidase was subjected to kinetic analysis with substrates which resemble the precursors of lignin or polyphenolic acid. The purified enzyme was found to readily polymerize phenolic acids in the presence of H(2)O(2) via a modified ping-pong mechanism. The percentage of lignin and lignin-related polymers in cell walls was nearly twofold greater in pith tissue isolated from peroxidase-overproducer plants compared to control plants. Lignin deposition in wounded pith tissue from control plants closely followed the induction of peroxidase activity. However, wound-induced lignification occurred 24 to 48 hours sooner in plants overexpressing the anionic peroxidase. This suggests that the availability of peroxidase rather than substrate may delay polyphenol deposition in wounded tissue.

Journal Article↗
PubMed1990

Kinetics of the inhibition of hog kidney D-amino acid oxidase by short-, medium- and long-chain fatty acids.

Various fatty acids were studied in vitro as inhibitors of pure hog kidney D-amino acid oxidase by means of a spectrophotometric peroxidase-coupling method using D-methionine as a substrate. All the fatty acids tested behaved as substrate-competitive inhibitors of the enzyme. The affinity of the saturated aliphatic acids for D-amino acid oxidase decreased from pentanoate (5:0; Ki = 220 microM) to laurate (12:0; Ki = 675 microM), then rose to a maximum with stearate (18:0; Ki = 36 microM), suggesting the presence of a site in the active center of the enzyme that accepts long-chain fatty acid alkyl groups. Unsaturation did not further increase the affinity of the fatty acid for this binding site.

Animals↗
PubMed1980

Endocytosis of asialoglycoprotein-enzyme conjugates by hepatocytes.

Desialylated glycoproteins were covalently linked to two cytochemically detectable enzymes, horseradish peroxidase or tyrosinase, and injected intravenously in amounts of approximately 0.5 per cent of total plasma glycoproteins into rats. Comparative studies of the rates of disappearance and distribution of free enzyme and conjugates established that recognition of the conjugates by the plasma membranes of hepatocytes was due to the exposure of the terminal galactose residue of the desialylated glycoproteins. At 1 minute after injection, reaction products of the enzyme markers were seen in coated pits and vesicles, elongated pinocytic channels and pleomorphic vesicles, at or close to the sinusoidal surface of hepatocytes. Vesicles containing reaction products were also observed along the lateral surfaces of hepatocytes. By 10 minutes, reaction products were seen in residual bodies near the biliary poles of hepatocytes. These studies confirm the existence of hepatocellular channels previously seen only with large excess of hemoglobin or following partial hepatectomy. They also indicate that the specific receptor for asialoglycoproteins is not restricted to the sinusoidal surfaces of hepatocytes and that transport to the catabolic sites proceeds via cytoplasmic channels and vesicles.

Animals↗
PubMed2006

Restricted expression of NADPH oxidase/peroxidase gene (Duox) in zone VII of the ascidian endostyle.

The ascidian Ciona intestinalis, a marine invertebrate chordate, is an emerging model system for developmental and evolutionary studies. The endostyle, one of the characteristic organs of ascidians, is a pharyngeal structure with iodine-concentrating and peroxidase activities and is therefore considered to be homologous to the follicular thyroid of higher vertebrates. We have previously reported that a limited part of the endostyle (zone VII) is marked by the expression of orthologs of the thyroid peroxidase (TPO) and thyroid transcription factor-2 (TTF-2/FoxE) genes. In this study, we have identified the Ciona homolog of NADPH oxidase/peroxidase (Duox), which provides hydrogen peroxide (H(2)O(2)) for iodine metabolism by TPO in the vertebrate thyroid. Expression patterns assessed by in situ hybridization have revealed that Ciona Duox (Ci-Duox) is predominantly expressed in the dorsal part of zone VII of the endostyle. Furthermore, two-color fluorescent in situ hybridization with Ci-Duox and Ciona TPO (CiTPO) has revealed that the ventral boundary of the Ci-Duox domain of expression is more dorsal than that of CiTPO. We have also characterized several genes, such as Ci-Fgf8/17/18, 5HT7, and Ci-NK4, which are predominantly expressed in the ventral part of zone VII, in a region complementary to the Ci-Duox expression domain. These observations suggest that, at the molecular level, zone VII has a complex organization that might have some impact on the specification of cell types and functions in this thyroid-equivalent element of the ascidian endostyle.

Animals↗
PubMedDate not supplied

Cytotoxicity of some potential DNA intercalators (carbazole, acridine and anthracene derivatives) evaluated through neutrophil chemiluminescence.

A modifying effect of potential DNA intercalators, belonging to a group of carbazole, acridine and anthracene derivatives, on the course of luminol-dependent chemiluminescence of neutrophils (polymorphonuclear leucocytes; PMNL) in the process of phagocytosis was studied. This effect was also examined in reactive-oxygen-species-generating non-cellular reaction systems consisted of myeloperoxidase or xanthine oxidase. Adriamycin (Doxorubicin), which is widely applied to neoplasm therapy, was used as a reference intercalator in the conducted experiments. It was demonstrated that some structurally different derivatives of carbazole inhibited the light emission from N-formyl-methionyl-leucyl-phenylalanine (fMLP)-induced neutrophils to the same degree as adriamycin. It can be suggested that the same inhibitory effect was caused by either a different cellular distribution of the derivatives or different interactions of the derivatives with reactive oxygen species in the investigated systems. Measurements of chemiluminescence suggested that the thiol group in one of the carbazole derivatives could strongly interfere with oxidative cell metabolism. In contrast to the analogous derivative of carbazole, both anthracene and acridine derivatives, possessing an N-1'-hydroxyethyl-ethylenodiamino group, induced different increases in chemiluminescence accompanying the process of neutrophil phagocytosis. Cytotoxicity of the investigated derivatives, being tested previously in cancer cells with a sulphorhodamine B assay, was found to possess a specific representation in the complex picture of the derivative-caused modification both of neutrophil and enzymatic non-cellular chemiluminescence. We suggest that chemiluminescence assays may serve as a helpful tool in the primary screening of drug cytotoxicity.

Acetaldehyde↗
PubMed2006

Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium.

The white rot basidiomycete Phanerochaete chrysosporium produces an array of nonspecific extracellular enzymes thought to be involved in lignin degradation, including lignin peroxidases, manganese peroxidases, and the H2O2-generating copper radical oxidase, glyoxal oxidase (GLX). Preliminary analysis of the P. chrysosporium draft genome had identified six sequences with significant similarity to GLX and designated cro1 through cro6. The predicted mature protein sequences diverge substantially from one another, but the residues coordinating copper and constituting the radical redox site are conserved. Transcript profiles, microscopic examination, and lignin analysis of inoculated thin wood sections are consistent with differential regulation as decay advances. The cro2-encoded protein was detected by liquid chromatography-tandem mass spectrometry in defined medium. The cro2 cDNA was successfully expressed in Aspergillus nidulans under the control of the A. niger glucoamylase promoter and secretion signal. The recombinant CRO2 protein had a substantially different substrate preference than GLX. The role of structurally and functionally diverse cro genes in lignocellulose degradation remains to be established.

Alcohol Oxidoreductases↗
PubMed1987

Susceptibility of Trichophyton quinckeanum and Trichophyton rubrum to products of oxidative metabolism.

Two dermatophyte strains, Trichophyton quinckeanum and Trichophyton rubrum, were highly susceptible to in vitro killing by components of the H2O2-peroxidase-halide system. Both strains were, however, resistant to relatively high concentrations of reagent H2O2 or H2O2 enzymatically generated by glucose and glucose oxidase, KI, or lactoperoxidase (LPO) alone. Resistance to hydrogen peroxidase killing was found to be in part due to the presence of endogenous catalase in the fungi; susceptibility was increased by pretreatment of the fungi with a catalase inhibitor. Kinetic studies using small quantities of reagent or enzymatically generated H2O2 and LPO-KI showed that the system was lethal for both fungal strains within 1 min. Furthermore, using the glucose-glucose oxidase-LPO-KI system, it was shown that catalase, superoxide dismutase and histidine scavengers of H2O2, superoxide anion and singlet oxygen, respectively, prevented the killing of fungus, whereas scavengers of hydroxyl radicals such as benzoate and mannitol had no effect. T. quinckeanum was found to contain large quantities of superoxide anion, as judged by the nitroblue-tetrazolium test. Consequently, the xanthine (or hypoxanthine) and xanthine oxidase system in which the main product is superoxide anion had no toxic effect on the fungus. The high sensitivity of dermatophytes to killing by the H2O2-peroxidase-halide system active in polymorphonuclear neutrophils and macrophages may account in part for fungal toxicity in vivo.

Dose-Response Relationship, Drug↗
PubMed2002

Kinetic parameters for the thermal inactivation of quality-related enzymes in carrots and potatoes.

Kinetic parameters for the thermal inactivation of several enzymes in carrot and potato homogenates have been determined. In carrots the most heat-resistant activity was polygalacturonase, followed by peroxidase and pectinmethylesterase. In potatoes peroxidase was the most resistant, followed by pectin methylesterase, polyphenol oxidase, and lipoxygenase. There were several notable similarities between the inactivation kinetics in the two vegetables. In both cases peroxidase activity gave simple first-order inactivation kinetics but yielded a curved Arrhenius plot for the temperature dependence. Pectin methylesterase in both commodities consisted of a labile and a resistant form. The relative amounts of the two forms and the temperature dependences for their inactivation were also similar.

Carboxylic Ester Hydrolases↗
PubMed1997

Nasotemporal asymmetries in V1: ocular dominance columns of infant, adult, and strabismic macaque monkeys.

To quantify asymmetries of input from the two eyes into each cerebral hemisphere, we measured ocular dominance column (ODC) widths and areas in the striate visual cortex (area V1) of macaque monkeys. Ocular dominance stripes in layer 4C were labeled by using transneuronal transport of intraocularly injected wheat germ agglutinin-horseradish peroxidase (WGA-HRP) or cytochrome oxidase (CO) histochemistry, after deafferentation of one eye or even by leaving afferent input intact. In infant monkey aged 4 and 8 weeks, ocular dominance stripes labeled by WGA-HRP appeared adultlike with smooth, sharply defined borders. In normal infant and normal adult macaque, ocular dominance stripes driven by the nasal retina (i.e., contralateral eye) were consistently wider than stripes driven by the temporal retina (i.e., ipsilateral eye). Asymmetries in the percentage of area V1 driven by nasal vs. temporal ODCs showed a similar "nasal bias": in infant macaque, approximately 58% of ODCs in V1 were driven by nasal retina, and in adult macaque approximately 57%. The asymmetries tended to be slightly smaller in opercular V1 and greater in calcarine V1. "Spontaneous" ocular dominance stripes were revealed by CO staining of V1 in a naturally strabismic monkey and in a monkey made strabismic by early postnatal alternating monocular occlusion. In these animals, ocular dominance stripes and CO blobs corresponding to the nasal retina stained more intensely for CO in both the right and left V1. ODC spacing and the nasotemporal asymmetry in ODC width and area were similar in strabismic and normal monkeys. Our results in normal monkeys extend the observations of previous investigators and verify that nasotemporal inputs to opercular and calcarine V1 are unequal, with a consistent bias favoring inputs from the nasal retina. The CO results in strabismic macaque suggest that the nasal ODC bias promotes interocular suppression when activity in neighboring ODCs is decorrelated by abnormal binocular experience in infancy.

Aging↗