Disease relevance of sodA

• A Staphylococcus aureus mutant (SPW1) which is unable to survive long-term starvation was shown to have a transposon insertion within a gene homologous to the sodA family of manganese-dependent superoxide dismutases (SOD) [1].
• A protein isolated from Brucella abortus is a Cu-Zn superoxide dismutase [2].
• Alignment of the superoxide dismutase sequences and the available structural information from X-ray crystallography suggest that the ligands to the iron in the P. ovalis superoxide dismutase are His-26, His-74, Asp-156 and His-160, which align with the ligands to the manganese in the Thermus thermophilus manganese-superoxide dismutase [3].
• Average values for SOD-1 in lysates of erythrocytes from normal individuals is 854 +/- 100 ng/mg hemoglobin and that of patients with trisomy-21 is 1313 +/- 110 ng/mg hemoglobin [4].
• Characterization of superoxide dismutase genes from gram-positive bacteria by polymerase chain reaction using degenerate primers [5].

High impact information on sodA

• Exogenous catalase (10,000 U/ml) increased the virulence of low-catalase staphylococci, but exogenous superoxide dismutase (200 mug/ml) did not alter the virulence of staphyloccal strains [6].
• Amino acid sequence of copper-zinc superoxide dismutase from horse liver [7].
• To inhibit superoxide-dependent processes, superoxide dismutase was cross-linked to immunoglobulin G and the conjugate was attached to the surface of S. aureus via protein A in its cell wall [8].
• There was no evidence of endothelial scavenging of O2- generated by hypoxanthine-xanthine oxidase, and inhibition of endothelial superoxide dismutase did not diminish the inhibitory effort [9].
• The inhibitor appears to be a polypeptide with an apparent molecular weight between 1,000 and 10,000 D and does not appear to be adenosine, an arachidonate metabolite, or superoxide dismutase [9].

Chemical compound and disease context of sodA

• Staphylococcus aureus with multiple sensitivity to ciprofloxacin, was investigated to detect alterations in the production of superoxide anion (O(2)(-)), other reactive oxidant species (ROS), and superoxide dismutase (SOD), and to relate them with ciprofloxacin accumulation and sensitivity [10].
• The complete amino acid sequence of Cu,Zn-superoxide dismutase (SOD) from spinach leaves has been determined on the basis of peptides obtained by cyanogen bromide (BrCN) cleavage and by enzymic hydrolyses with Achromobacter lyticus lysylendopeptidase, Staphylococcus aureus V8 protease, trypsin, and thermolysin [11].
• In contrast, the uptake of Staphylococcus aureus or zymosan was accompanied by the release of measurable O2-. This release of O2- was abrogated by the addition of 100 micrograms/ml of superoxide dismutase (SOD) [12].
• Malondialdehyde levels and superoxide dismutase activity in experimental maxillary sinusitis [13].

Biological context of sodA

• In a mouse abscess model of infection, isogenic sodA, sodM and sodA sodM mutants had reduced virulence compared to the parental strain, showing the importance of the enzymic scavenging system for the survival of the pathogen [14].
• Mangafodipir, a superoxide dismutase (SOD) mimic with catalase and glutathione reductase activities, protects normal cells from apoptosis induced by H2O2 [15].

Anatomical context of sodA

• A radioimmune assay for human cupro-zinc superoxide dismutase and its application to erythrocytes [4].
• Production of superoxide anion (O2-) by granulocytes was measured through superoxide dismutase inhibitable reduction of ferricytochrome C after incubation of cells for various times together with immunoglobulin (concentration ranging from 0.25 to 5.0 mg/ml) [16].
• Effects of copper status on neutrophil function, superoxide dismutase, and copper distribution in steers [17].
• Staphylococcal arthritis--effects of superoxide dismutase on infected knee joints of rabbits [18].

Associations of sodA with chemical compounds

• Expression of sodA and, consequently, SOD activity could be induced by methyl viologen but only during the transition from exponential- to postexponential-phase growth [1].
• Sensitivity to externally generated stress was only observed in a sodA sodM mutant and was Mn-independent [14].
• The sodA mutant was more resistant than the wild-type and also had a higher level of 3-phosphoglycerate dehydrogenase (a measure of PerR regulon activity) without exposure to HOCl [19].
• Phorbol myristate acetate-and HKB-stimulated increases in AM chemiluminescence were completely blocked by the enzyme superoxide dismutase [20].
• Superoxide dismutase and mannitol were less effective [21].

Other interactions of sodA

• Transcription of sodA and sodM was most strongly induced by either internally or externally generated, respectively [14].
• In addition, SCBM 1 showed extremely high sequence identities of hsp 60, sodA, and rpoB genes (more than 98.7%) to S. sciuri strains, while showing 70.3--94.2% identity of these genes to other staphylococcal species [22].
• Addition of superoxide dismutase or catalase to the O2.- generating system resulted in protection of thermally stressed and nonstressed cells, with the protective effect being greater for thermally stressed cells [23].

Analytical, diagnostic and therapeutic context of sodA

• A competition radioimmunoassay for human superoxide dismutase (SOD-1) is described [4].
• Influence of superoxide dismutase on staphylococcal arthritis--a histological and biochemical investigation using an experimental animal model [24].

References