Disease relevance of ECs2365

• SOD-null mutants have been prepared to reveal the biological effects of O2-. SodA, sodB E. coli exhibit dioxygen-dependent auxotrophies and enhanced mutagenesis, reflecting O2(-)-sensitive biosynthetic pathways and DNA damage [1].
• Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions [2].
• On the basis of observations with the model system, it is proposed that the cell may also decrease such toxicity by diminishing available NAD(P)H and by utilizing oxygen itself to scavenge active free radicals into superoxide, which is then destroyed by superoxide dismutase [3].
• Superoxide dismutase inhibited the phagocytic killing of Escherichia coli, Staphylococcus aureus, and Streptococcus viridans [4].
• Pretreatment with superoxide dismutase (SOD), a superoxide radical scavenging enzyme, significantly attenuated the capillary permeability change induced by regional ischemia [5].

Psychiatry related information on ECs2365

• The enzyme, superoxide dismutase (SOD), which catalyzes the breakdown of superoxide radicals to hydrogen peroxide and dioxygen is one of the bacterial cell's major defense mechanisms against oxidative damage [6].

High impact information on ECs2365

• No ALS-like phenotype is observed in mice overexpressing wild-type SOD1 or mice without any SOD1 activity [2].
• These dominant mutations, which do not necessarily decrease SOD1 activity, may confer a gain of function that is selectively lethal to motor neurons [2].
• Two mutations which have been successfully used to generate transgenic mice that develop an ALS-like syndrome are glycine 85 to arginine (G85R) and glycine 93 to alanine (G93A) with the mutant SOD1 allele overexpressed in a normal mouse genetic background [2].
• Both the iodinating and bactericidal activities were inhibited by catalase and the hydroxyl radical (OH.) scavenger mannitol, whereas superoxide dismutase was ineffective [7].
• Superoxide dismutase, which removes O2-, consistently inhibited phagocytosis-associated nitroblue tetrazolium (NBT) reduction indicating the involvement of O2- in this process [4].

Chemical compound and disease context of ECs2365

• Mu transposons carrying the chloramphenicol resistance marker have been inserted into the cloned Escherichia coli genes sodA and sodB coding for manganese superoxide dismutase (MnSOD) and iron superoxide dismutase (FeSOD) respectively, creating mutations and gene fusions [8].
• Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation [9].
• A mixed-sequence synthetic oligodeoxynucleotide probe was used to identify clones within the Escherichia coli genomic library of Clarke and Carbon having an extrachromosomal copy of iron superoxide dismutase [10].
• Superoxide dismutase participates in the enzymatic formation of the tyrosine radical of ribonucleotide reductase from Escherichia coli [11].
• Coincidentally, the reduced glutathione content of high superoxide dismutase E. coli declines more than in control E. coli [12].

Biological context of ECs2365

• Similarly, superoxide dismutase inhibited the luminescence that occurs with phagocytosis, implicating O2- in this phenomenon, perhaps through its spontaneous dismutation into singlet oxygen [4].
• Superoxide dismutase (15,000 U/kg IV) injected before either endotoxin or platelet-activating factor shortened the migrating myoelectric complex inhibition to 45.7 +/- 9.9 and 72.9 +/- 10.4 minutes, respectively (P less than 0.01) [13].
• The mutated sodA or sodB genes were introduced into the bacterial chromosome by allelic exchange [8].
• Escherichia coli iron superoxide dismutase targeted to the mitochondria of yeast cells protects the cells against oxidative stress [14].
• The rational protein design algorithm DEZYMER was used to introduce the active site of nonheme iron superoxide dismutase (SOD) into the hydrophobic interior of the host protein, Escherichia coli thioredoxin (Trx), a protein that does not naturally contain a transition metal-binding site [15].

Anatomical context of ECs2365

• Polyacrylamide electrophoresis separated this activity into a minor band that appeared to be the manganese-containing superoxide dismutase associated with mitochondria and a more concentrated, cyanide-sensitive, cytosol form of the enzyme with electrophoretic mobility that corresponded to that of erythrocyte cuprozinc superoxide dismutase [4].
• Activity of superoxide dismutase, the enzyme responsible for protecting the cell from the damaging effects of O2-, was approximately equal in homogenates of normal and CGD granulocytes [4].
• Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells [16].
• These defenses include antioxidant enzymes such as superoxide dismutase and catalase, DNA repair systems, scavenging substrates, and competition with phagocytes for molecular oxygen [17].
• The failure of intrabacterial catalase or superoxide dismutase to protect bacteria from killing by neutrophils might indicate either that the flux of O-2 and H2O2 in the phagosome is too great for the intrabacterial enzymes to alter or that the site of injury is at the bacterial surface [18].

Associations of ECs2365 with chemical compounds

• The loss of [2Fe-2S] clusters does not occur in anaerobic solution and is blocked in aerobic solution by the addition of superoxide dismutase and catalase [19].
• Plasmids pLC13-47 and pLC18-11 were shown to contain the structural gene of the iron superoxide dismutase and to overproduce this protein under conditions of chloramphenicol amplification of plasmid copy number [10].
• The superoxide-producing ability of arsenite-treated cells was also suppressed by diphenylene iodinium, 4,5-dihydroxy-1, 2-benzenedisulfonic acid disodium salt (Tiron), or superoxide dismutase [20].
• Elevated superoxide dismutase activity did not affect the aerobic inactivation of aconitase by NO., thus indicating a limited role of the NO.- and superoxide-derived species peroxynitrite [21].
• Hydrogen peroxide, formed by superoxide dismutase, is also harmful [22].

Regulatory relationships of ECs2365

• The ferric uptake regulation (fur) gene product participates in regulating expression of the manganese- and iron-containing superoxide dismutase genes of Escherichia coli [23].

Other interactions of ECs2365

• After purification to near homogeneity two of the proteins were identified as superoxide dismutase and NAD(P)H:flavin oxidoreductase (Fontecave, M., Eliasson, R., and Reichard, P. (1987) J. Biol. Chem. 262, 12325-12331) [22].
• P. leiognathi bacteriocuprein is the first bacteriocuprein whose gene has been isolated and sequenced and the first copper-zinc superoxide dismutase in which a leader peptide has been found [24].
• Overlapping genes encoding scavengase p20 and superoxide dismutase were recognized in H. pylori and their functional implications are discussed [25].
• Three cytosolic enzymes from the extremely thermoacidophilic archaeon Sulfolobus acidocaldarius (DSM 639) have been investigated: adenylate kinase, pyrophosphatase and superoxide dismutase [26].
• In superoxide dismutase-deficient E. coli mutants, glycolaldehyde induces fumarase C and nitroreductase A, which are regulated as members of the soxRS regulon [27].

Analytical, diagnostic and therapeutic context of ECs2365

• The intracellular localization of Cu,Zn superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1) has been examined by immunofluorescence using four monoclonal anti-Cu,Zn superoxide dismutase antibodies raised against a recombinant human Cu,Zn superoxide dismutase derivative produced and purified from Escherichia coli [16].
• Analysis of the hybrid protein's interaction with the neuron-like cell line, N18-RE-105, and cultured hippocampal neurons by enzyme immunoassay for human SOD-1 revealed that SOD:Tet451 association with cells was neuron-specific and dose-dependent [28].
• Northern blot analyses showed that the transcription of SOD3 is induced neither by the transition from the yeast to the mycelial form of C. albicans nor by drug-induced oxidative stress [29].
• Catalysis by Escherichia coli and Porphyromonas gingivalis iron superoxide dismutase was activated by addition of primary amines, as measured by pulse radiolysis and stopped-flow spectrophotometry [30].
• The instability of the dehydratase activity in cell extracts was exacerbated by selective removal of superoxide dismutase, but not of catalase, by immunoprecipitation [31].

References