Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00080 (Leaf)
 21,685 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The subcellular location of superoxide dismutase in the leaves of spinach and other C3 plants has been investigated. 2. Most activity appeared to be located within chloroplasts. These organelles contain a cyanide-sensitive (copper-zinc) superoxide dismutase, most of which is located in the stroma although some is bound to the thylakoids. 3. Intact chloroplast fractions also contain a cyanide-insensitive (manganese) superoxide dismutase, but this activity is located on the outside of the chloroplasts and may be adsorbed onto them during isolation. 4. Leaf mitochondrial fractions contain only a small percentage of total leaf superoxide dismutase activity, but there is more than can be accounted for by contamination with chloroplasts. 5. Mitochondria contain both a cyanide-sensitive dismutase, apparently located in the intermembrane space, and a cyanide-insensitive activity, apparently located in the matrix. 6. The microsomal fraction contains no superoxide dismutase activity.
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PMID:Subcellular localisation and identification of superoxide dismutase in the leaves of higher plants. 72 73

Neutrophil-induced alterations in feline erythrocytes were studied to better understand the pathogenesis of erythrocyte destruction associated with inflammatory diseases. As in previous studies, addition of superoxide dismutase/catalase to a coculture of erythrocytes and activated neutrophils attenuated neutrophil-induced immunoglobulin G (IgG) binding. However, incubation of erythrocytes with hydrogen peroxide or neutrophil-derived anuclear cytoplasts (neutroplasts) failed to induce IgG binding. Addition of phenylmethylsulfonyl fluoride, a serine protease inhibitor, to the erythrocyte-neutrophil coculture attenuated IgG binding. These observations suggest that neutrophil-derived serine protease activity is involved in IgG binding to erythrocytes. Further, incubation of erythrocytes with serine proteases, but not metalloproteases or sulfhydryl proteases, induced immunoglobulin binding. Freeze-fracture replicas of the erythrocyte membrane failed to demonstrate clustering of band 3 protein, suggesting that spatial rearrangement of band 3 protein was not the cause of the IgG binding. Neutrophil-induced IgG binding due to the combined action of proteases and oxidants may explain the accelerated destruction of erythrocytes in inflammatory diseases.
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PMID:Neutrophil-induced immunoglobulin binding to erythrocytes involves proteolytic and oxidative injury. 174 Jun 41

In plants, environmental adversity often leads to the formation of highly reactive oxygen radicals. Since resistance to such conditions may be correlated with the activity of enzymes involved in oxygen detoxification, we have generated transgenic tobacco plants which express elevated levels of manganese superoxide dismutase (MnSOD) within their chloroplasts or mitochondria. Leaf discs of these plants have been analyzed in conditions in which oxidative stress was generated preferentially within one or the other organelle. It was found that high level overproduction of MnSOD in the corresponding subcellular location could significantly reduce the amount of cellular damage which would normally occur. In contrast, small increases in MnSOD activity were deleterious under some conditions. A generally applicable model correlating the consequences of SOD with the magnitude of its expression is presented.
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PMID:Manganese superoxide dismutase can reduce cellular damage mediated by oxygen radicals in transgenic plants. 205 Jan 9

Free radicals produced in the fluid of jaw cysts were directly measured at room temperature using ESR. With these samples, SOD activity of the cyst fluid was measured by the ESR spin trapping method with DMPO as a trapping agent. Freeze-dried samples of cyst fluid showed a broad ESR signal at g = 2.005. Relative signal intensity of samples from jaw cysts with inflammation was higher than jaw cysts without inflammation. SOD activity of cyst fluid with high viscosity showed higher values than that of cyst fluid with low viscosity. We suggest that free radicals produced in jaw cyst damage tissues while higher SOD activity of cyst fluid play a role in a self-defense mechanism against free radicals.
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PMID:Free radicals and SOD activity of jaw cyst. Direct measurement and spin trapping studies by ESR. 216 66

To study the effect of protein flexibility on electrostatic recognition, we have devised two novel computer graphic representations of the changes in the electrostatic field of a protein resulting from its internal motions. The atomic structure of Cu, Zn superoxide dismutase was minimized, and the 200 lowest frequency normal modes of the enzyme were determined. Individual and combined normal-mode vibrations were visualized interactively with the program Flex. Normal-mode motions are fast enough (approximately 10(-11) s cycle-1) to evade solvent damping, thus allowing long-range electrostatic interactions to dominate. The changing electrostatic environment of the protein was examined by animating precalculated frames of electrostatic field vectors with GRAMPS. With Vu, changes in electrostatic potential were displayed as variations in the color-coding of dots lying on a consensus surface that maintains the protein's shape. The consensus surface was calculated with the program Sphinx, and was derived from spherical harmonic approximations of expanded molecular surfaces. The ability to view the effects of molecular motions interactively should be useful in understanding the relationships of protein structure to function.
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PMID:Visualization of molecular flexibility and its effects on electrostatic recognition. 227 8

The ocular lens, which is continually exposed to light and ambient oxygen, is at high risk of photooxidative damage resulting in cataract. Oxygen free radicals appear to impair not only lens crystallins which will aggregate and precipitate forming opacities but also proteolytic enzymes whose function it would be to eliminate the damaged proteins. Apart from an enzymatic defense system consisting of superoxide dismutase, catalase and glutathione peroxidase against excited oxygen species the lens contains the antioxidant vitamins C, E and presumably beta-carotene as another line of defense. In vitro and in vivo studies in different animal species have demonstrated a significant protective effect of vitamins C and E against light-induced cataract. Sugar and steroid cataracts were prevented as well. Epidemiological evidence in humans suggests that persons with comparatively higher intakes or blood concentrations of antioxidant vitamins are at a reduced risk of cataract development. These positive findings established by several research groups justify extensive intervention trials with antioxidant vitamins in humans using presenile cataract development as a model.
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PMID:Antioxidant vitamins in cataract prevention. 265 16

The generation of reactive oxygen intermediates by microsomes from ethanol-fed rats and pair-fed controls was determined by assaying for NADPH-dependent chemiluminescence. In the absence or presence of added ferric complexes, microsomal light emission was elevated several-fold after chronic ethanol consumption. Iron complexes such as ferric-citrate or ferric-ATP stimulated, while ferric-EDTA, inhibited microsomal chemiluminescence. Freeze-thawing the microsomes to elevate their content of lipid hydroperoxides resulted in large increases in chemiluminescence; under all conditions, the light emission remained several-fold higher with microsomes from the ethanol-fed rats. Chemiluminescence was not sensitive to superoxide dismutase, catalase, or the hydroxyl radical scavenging agent, dimethyl sulfoxide, but was inhibited by antioxidants and by glutathione. Replacing air with a mixture of 50% nitrogen-50% air or 50% carbon monoxide-50% air had no effect on chemiluminescence by microsomes from the pair-fed controls. However, the chemiluminescent response by microsomes from the ethanol-fed rats was inhibited about 50% by the nitrogen mixture, and was further inhibited (about 75% of values found with 100% air, and 50% of values found with 50% nitrogen-50% air) with the carbon monoxide mixture. The sensitivity to carbon monoxide suggests the possibility that the alcohol-inducible cytochrome P-450 isozyme may contribute, in part, to the elevated light emission produced by microsomes from the ethanol-fed rats. The increase in chemiluminescence by microsomes after chronic ethanol consumption appears to reflect an elevated level of lipid hydroperoxides as well as an increased rate of generation of reactive oxygen species.
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PMID:Increased NADPH-dependent chemiluminescence by microsomes after chronic ethanol consumption. 319 Feb 38

Do eosinophils modulate lymphocyte function? This question was studied by examining the effect of purified eosinophils (eos) on lectin-induced human lymphocyte proliferation. Intact resting or zymosan-stimulated eos or their extracts were cocultured with phytohemagglutinin-stimulated mononuclear cells in vitro and [3H]thymidine uptake was measured at 72 hr. Zymosan-stimulated eos consistently suppressed (up to 90%) the lectin-induced proliferative response by a noncytotoxic mechanism. Freeze-thaw extracts from zymosan-stimulated eos also significantly suppressed lymphocyte proliferation to a similar degree. The amount of suppression was directly proportional to the number of eos or the amount of extract added to the lymphocyte cultures. Intact resting eos and their extracts occasionally exhibited suppressive effects (up to 40%) on lymphocyte proliferation; this suppression, however, was always less than that of activated eos or their extracts. Eos pretreated with the protein synthesis inhibitor, pactamycin, exhibited significantly less suppressive activity, suggesting that a protein was responsible in part for the reduction in proliferation. The addition of superoxide dismutase or catalase to the eos-mononuclear cell cocultures did not reduce the amount of suppression observed, thus making it unlikely that active oxygen products were involved in the mechanism of suppression. Heating extracts from stimulated eos to 80 degrees C for 30 min resulted in partial loss of suppressive activity while extensive dialysis of the extracts had no effect. The studies reported here provide evidence that a nondialyzable and heat sensitive factor(s) produced by stimulated eos may exert feedback inhibition of lymphocyte function.
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PMID:Human lymphocyte-eosinophil interactions. I. Modulation of phytohemagglutinin-induced lymphocyte proliferation by eosinophils. 399 94

Leukaemic blast cells from 20 patients with acute leukaemia were examined for their capacity to mediate cytotoxicity against ox red blood cells in the presence of phorbol myristate acetate (PMA), a system widely employed as an in vitro model of tissue damage by metabolically activated mature phagocytes. Blasts from certain patients with myelomonocytic and monocytic leukaemia behaved like efficient killer cells. Conversely, leukaemic myeloblasts and promyelocytes as well as leukaemic lymphoblasts were ineffective. Blast cells capable of inducing the target cell lysis were also capable of mounting an oxidative respiratory burst upon challenge with PMA, as detected by the superoxide anion release. N-ethyl-maleimide, superoxide dismutase and catalase completely inhibited the cytotoxicity by monocytoid blast cells, suggesting the involvement of oxygen reactive products in the lethal hit itself. The cytolytic potential of blasts committed to monocytic differentiation might be an additional factor contributing to the tissue damage in a subpopulation of leukaemic patients.
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PMID:Extracellular cytolysis by leukaemic blast cells. 632 32

Neuraminidase treatment of parental and butyrate-induced K562 tumor cells was associated with an increase in natural killer (NK) susceptibility of these target cells. The degree of enhancement with neuraminidase was significantly greater for the NK-resistant (NRR) butyrate-differentiated K562 cells so that the relative difference between the parental NK-sensitive (NKS) K562 line and its induced NKR variants, in terms of NK sensitivity, was no longer five- or six-fold but only two-fold. The predominant reason for the altered NK susceptibilities of the target cells after neuraminidase treatment was an increase in the target-cell-binding ability of these cells as assessed by a direct conjugate-forming cell assay using Percoll-enriched NK cells and cold target competition assays. The enhancement did not appear to be due simply to an increased membrane-membrane attraction caused by a reduction of net negative cell surface charges since protamine sulphate, a positively charged molecule, had no effect on NK activity. Compared with the NKS parental K562 tumor cells, the NKR butyrate-induced cells had 3.6- to 4.0-fold higher sialo-transferase activities and were associated with significantly greater amounts of cell surface sialic acid detected both in sialyl glycoproteins (2.2- to 2.9-fold higher) and particularly within ganglioside extracts (6.2- to 13.6-fold higher). In conformity with the marked neuraminidase enhancement of NK-mediated cytolysis of the butyrate-induced targets, these NKR cells were associated with significantly enhanced levels of neuraminidase-accessible sialic acid compared to the NKS parental K562 cell line. Other parameters such as sensitivity to superoxide radicals, intrinsic superoxide dismutase levels, altered membrane repair mechanisms and transferrin competition, were not significantly different between the NKS and NKR target phenotypes. Sugar inhibition studies demonstrated an enhanced inhibition against the butyrate-induced cells with a variety of neutral sugars. The degree of inhibition with phosphorylated sugars was comparable between the parental and induced K562 tumor target cells and is consistent with our previous findings showing that these hexose phosphates may be inhibiting cytolysis at a step independent of target-cell recognition.
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PMID:Modulation of K562 cells with sodium butyrate. Association of impaired NK susceptibility with sialic acid and analysis of other parameters. 686 94


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